ORCID Profile
0000-0002-1820-0057
Current Organisation
Griffith University
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Publisher: Elsevier BV
Date: 10-1990
DOI: 10.1016/0014-4835(90)90154-M
Abstract: Bovine corneal aldehyde dehydrogenase was purified to homogeneity and characterized with aldehyde substrates at pH 7.4. The enzyme was a dimer with a subunit size of 65 kDa. Using kcat/Km values as an indication of substrate efficacy, aldehyde products of lipid peroxidation were recognized as the likely 'natural' substrates. Protein yields from enzyme purification, as well as electrophoretic analyses of crude and purified enzyme preparations, demonstrated that this enzyme is the major soluble protein in bovine cornea, and constitutes around 0.5% wet weight of tissue. A dual role in protecting the eye against UV-B light is proposed--oxidation of aldehydes generated by light induced lipid peroxidation, and the direct absorption of UV-B light by bovine corneal ALDH.
Publisher: Elsevier BV
Date: 1968
DOI: 10.1016/0005-2744(68)90169-1
Abstract: Depression and brief periods of manic symptoms are linked to a significant risk of progression to bipolar disorder (BD) in children who have a first-degree relative with BD I or II. However, little evidence exists to guide the pharmacologic management of children with these high-risk phenotypes. We propose a pharmacological treatment algorithm for high-risk youth and present results on its use in a study of children with a first-degree relative with BD. Subjects were 40 youth (mean 12.7 years, range 9-17 years) who had (1) a first-degree relative with lifetime history of BD I or II, (2) DSM-IV-TR diagnoses of BD not otherwise specified, major depressive disorder or cyclothymic disorder, and (3) active symptoms of depression, mania, or hypomania. Participants and their families were enrolled in a randomized trial examining the effects of two psychosocial interventions on the 1-year course of mood disorder. At study intake, participants received a psychiatric evaluation and were offered medications or had existing medications optimized to decrease symptom severity. During the 1-year study, psychiatrists treated participants using a medication algorithm to treat depressive or manic symptoms as well as comorbid anxiety and/or attention-deficit/hyperactivity disorder. At study entry, 25 of 40 (62.5%) of the participants were taking at least one psychiatric medication. At 1 year, nearly an identical proportion were taking medications (22 of 35, 63%). Independent ratings indicated that in 84.7% of the study visits, physicians maintained adherence to the algorithm. No patients experienced antidepressant- or stimulant-induced mania during the study. An algorithmic approach to pharmacologic interventions may aid in the management of youth (i.e., age <18) at high risk for BD. Future studies should compare outcomes in high-risk patients receiving algorithm-prescribed treatment versus those receiving treatment as usual. Early Family-Focused Treatment for Youth at Risk for Bipolar Disorder www.clinicaltrials.gov/ NCT00943085.
Publisher: Springer Science and Business Media LLC
Date: 12-1976
DOI: 10.1007/BF00485130
Publisher: Elsevier BV
Date: 11-1969
DOI: 10.1016/0005-2744(69)90273-3
Abstract: To compare rates of unintended pregnancy, method continuation and reasons for removal among women using the 52-mg levonorgestrel (daily release 20 microg) intrauterine device (LNG-IUD) or the copper T 380 A IUD (TCu380A). This was an open-label 7-year randomized controlled trial in 20 centres, 11 of which in China. Data on 1884 women with interval insertion of the LNG-IUD and 1871 of the TCu380A were analysed using life tables with 30-day intervals and Cox proportional hazards models. The cumulative 7-year pregnancy rate of the LNG-IUD was 0.5 (standard error 0.2) per 100, significantly lower than 2.5 (0.4) per 100 of the TCu380A, cumulative method discontinuation rates at 7 years were 70.6 (1.2) and 40.8 (1.3) per 100, respectively. Dominant reasons for discontinuing the LNG-IUD were amenorrhea (26.1 [1.3] per 100) and reduced bleeding (12.5 [1.1] per 100), particularly in Chinese women and, for the TCu380A, increased bleeding (9.9 [0.9] per 100), especially among non-Chinese women. Removal rates for pain were similar for the two intrauterine devices (IUDs). Cumulative rates of removal for symptoms compatible with hormonal side effects were 5.7 (0.7) and 0.4 (0.2) per 100 for the LNG-IUD and TCu380A, respectively, and cumulative losses to follow-up at 7 years were 26.0 (1.4) and 36.9 (1.3) per 100, respectively. The LNG-IUD and the TCu380A have very high contraceptive efficacy, with the LNG-IUD significantly higher than the TCu380A. Overall rates of IUD removals were higher among LNG-IUD users than TCu380A users. Removals for amenorrhea appeared culturally associated. The 52-mg LNG-IUD and the TCu380A have very high contraceptive efficacy through 7 years. As an IUD, the unique side effects of the LNG-IUD are reduced bleeding, amenorrhea and symptoms compatible with hormonal contraceptives.
Publisher: Elsevier BV
Date: 1983
DOI: 10.1016/0020-711X(83)90124-6
Abstract: 1. The sorbitol dehydrogenase (L-iditol: NAD oxidoreductase, EC 1.1.1.14) from mouse liver has been purified to homogeneity. 2. The enzyme has a mol. wt of 140,000 and is composed of four identical subunits of mol. wt 35,000. 3. the purified enzyme catalyses both sorbitol oxidation and fructose reduction. 4. It is specific for NAD+ (NADH) and does not function with NADP+ (NADPH). 5. The Michaelis constants for sorbitol, fructose, NAD+ and NADPH are 1.54 and 154 mM, 58.8 and 15 microM, respectively. 6. The enzyme is SH-group reagent sensitive and is strongly inhibited by 1,10-phenanthroline.
Publisher: Elsevier BV
Date: 1985
DOI: 10.1016/0020-711X(85)90085-0
Abstract: Aldehyde dehydrogenase isozymes (AHD-1 and AHD-5) have been isolated in a highly purified state from extracts of mouse liver mitochondria. The enzymes have distinct subunit sizes, as determined by SDS olyacrylamide gel electrophoresis: AHD-1, 63,000 AHD-5, 49,000. Gel exclusion chromatography, using sephadex G-200, indicated that both isozymes are dimers, although AHD-1 may also exist as a monomeric form as well. The enzymes exhibited widely ergent kinetic characteristics. The purified allelic forms of AHD-1, AHD-1A (C57BL/6J mice) and AHD-1B (CBA/H mice), exhibited high Km values with acetaldehyde as substrate, 1.4 mM and 0.78 mM respectively, whereas AHD-5 exhibited a low Km value with acetaldehyde of 0.2 microM. In addition, the isozymes exhibited distinct pH optima for catalysis (AHD-1, pH range 6.5-7.5 AHD-5, pH range 8.5-10.0), and were differentially sensitive towards disulphuram inhibition, with 50% inhibition occurring 13 and 0.1 microM for the AHD-1 and AHD-5 isozyme respectively. Based upon the kinetic characteristics, it is suggested that AHD-5 may be the primary enzyme for oxidizing mitochondrial acetaldehyde during ethanol oxidation in vivo.
Publisher: Elsevier BV
Date: 05-1986
DOI: 10.1016/0741-8329(86)90046-7
Abstract: Isoelectric focusing (IEF) and cellulose acetate electrophoresis were used to examine the multiplicity and distribution of aldehyde dehydrogenases (ALDHs), aldehyde oxidase (AOX) and xanthine oxidase (XOX) from tissues of olive and yellow baboons. Five ALDHs were resolved and distinguished on the basis of their differential tissue and subcellular distribution or substrate specificity. Some ALDHs exhibited multiple activity zones. Baboon liver ALDHs were differentially distributed in cytosol (ALDHs II, III and V) and large granular (mitochondrial) fractions (ALDHs I and IV). The major liver ALDHs (I and II) were also broadly distributed in other tissues, as was the major stomach enzyme (ALDH-III). Three brain ALDHs were resolved, which were also differentially distributed between large granular (mitochondrial) (ALDHs I and IV) and cytosolic (ALDH-III) fractions. Electrophoretic variability between in iduals was observed for the major liver mitochondrial isozyme (ALDH-I), the major stomach isozyme (ALDH-III) and the minor liver isozymes (ALDHs IV and V). Single forms of AOX and XOX were found in baboon tissue extracts, with the highest activities in liver (AOX) and intestine extracts (XOX). Both oxidases were predominantly localized in the liver soluble fraction.
Publisher: Elsevier BV
Date: 07-1982
DOI: 10.1016/0005-2760(82)90084-4
Abstract: The uptake of radioactively labelled glycerol into the phospholipid fractions of mouse liver has been studied. The incorporation of phospholipid into peroxisomal and microsomal membranes was found to be rapid, and of a similar timescale, whereas mitochondrial membranes were appreciably slower in their uptake of label. Discernible differences were shown to exist between these membrane types in relation to phospholipid composition and lipid turnover. These data are interpreted as supportive of a model for peroxisomal biogenesis which involves formation of these organelles by a budding process from the smooth endoplasmic reticulum.
Publisher: Springer Science and Business Media LLC
Date: 24-12-2009
DOI: 10.1007/S10528-009-9318-3
Abstract: Mammalian ALDH3 isozymes participate in peroxidic and fatty aldehyde metabolism, and in anterior eye tissue UV-filtration. BLAT analyses were undertaken of the opossum genome using rat ALDH3A1, ALDH3A2, ALDH3B1, and ALDH3B2 amino acid sequences. Two predicted opossum ALDH3A1-like genes and an ALDH3A2-like gene were observed on chromosome 2, as well as an ALDH3B-like gene, which showed similar intron-exon boundaries with other mammalian ALDH3-like genes. Opossum ALDH3 subunit sequences and structures were highly conserved, including residues previously shown to be involved in catalysis and coenzyme binding for rat ALDH3A1. Eleven glycine residues were conserved for all of the opossum ALDH3-like sequences examined, including two glycine residues previously located within the stem of the rat ALDH3A1 active site funnel. Phylogeny studies of human, rat, opossum, and chicken ALDH3-like sequences indicated that the common ancestor for ALDH3A- and ALDH3B-like genes predates the appearance of birds during vertebrate evolution.
Publisher: Wiley
Date: 24-04-2022
DOI: 10.1111/J.1365-2052.1982.TB01569.X
Abstract: A 'null' activity variant phenotype for sorbitol dehydrogenase (SDH) was observed in C57BL/LiA mice and used to examine the genetics of this enzyme. Linkage studies of the locus (Sdh-1) with non-agouti (a) and a biochemical locus encoding liver L-alpha-hydroxyacid oxidase (Hao-1) demonstrated that it is coincident with or closely linked to the structural locus, previously localized on chromosome 2. Alcohol dehydrogenase (ADH) isozymes were also examined, since the liver A2 isozyme exhibited some activity as a sorbitol dehydrogenase on cellulose acetate zymograms. It is apparent that SDH activity is not 'essential' in this mouse strain.
Publisher: Wiley
Date: 17-10-2016
DOI: 10.1111/J.1365-2052.1981.TB01550.X
Abstract: A 'null' activity variant for the major liver isozyme of aldehyde oxidase (AOX-1) in adult male mice and an electrophoretically distinct, high activity variant of the second liver isozyme (AOX-2) were used to examine the segregation of the genetic loci encoding these enzymes (Aox-1 and Aox-2 respectively) in breeding studies. A single recombinant between these loci was observed among the 147 backcross progeny examined, which confirms a previous report (Holmes, 1979) for close linkage and genetic distinctness of the two loci. An activity variant for mouse liver xanthine oxidase (XOX) is also reported which behaved as though controlled by codominant alleles at a single locus (designated Xox-1). Genetic analyses showed that the Xox-1 locus segregated independently of the multiple-Aox loci.
Publisher: MDPI AG
Date: 23-08-2011
DOI: 10.3390/BIOM1010003
Publisher: Portland Press Ltd.
Date: 11-1978
DOI: 10.1042/BJ1750377
Abstract: Aldolase was purified from rabbit liver by affinity-elution chromatography. By taking precautions to avoid rupture of lysosomes during the isolation procedure, a stable form of liver aldolase was obtained. The stable form of the enzyme had a specific activity with respect to fructose 1,6-bisphosphate cleavage of 20-28 mumol/min per mg of protein and a fructose 1,6-bisphosphate cleavage of 20-28mumol/min per mg of protein and a frutose 1,6-bisphosphate/fructose 1-phosphate activity ratio of 4. It was distinguishable from rabbit muscle aldolase, as previously isolated, on the basis of its electrophoretic mobility and N-terminal analysis. Muscle and liver aldolases were immunologically distinct. The stable liver aldolase was degraded with a lysosomal extract to a form with catalytic properties resembling those reported for aldolase B4. It is postulated that liver aldolase prepared by previously described methods has been modified by proteolysis and does not constitute the native form of the enzyme.
Publisher: Informa UK Limited
Date: 1997
DOI: 10.1076/CEYR.16.6.539.5075
Abstract: To examine a possible genetic basis for corneal sensitivity to UV-B light exposure. To this end, adult male mice from the 14 SWXJ recombinant inbred albino strains (originating from SJL/J and SWR/J parental strains) were subjected to ultraviolet (UV) radiation exposure of 0.078 J/cm2 and photographed four days post-exposure, to assess corneal opacity and the possible correlation with corneal aldehyde dehydrogenase (ALDH) activity, alcohol dehydrogenase (ADH) activity and soluble protein content. Those recombinant strains that exhibited the SWR/J strain phenotype of having low levels of ALDH and decreased soluble protein levels also exhibited greater levels of corneal clouding after UV-exposure than the other strains, which exhibited "normal" levels of both ALDH activity and soluble protein in the cornea. These data support an hypothesis for a major role for ALDH in assisting the cornea to protect the eye against UV-induced tissue damage.
Publisher: Elsevier BV
Date: 10-1979
Publisher: Elsevier BV
Date: 1980
DOI: 10.1016/0020-711X(80)90270-0
Abstract: Since the Centers for Disease Control and Prevention published opioid prescribing guidelines in March 2016, 31 states have implemented legislation to restrict the duration of opioid prescriptions for acute pain. However, the association of these policies with the amount of opioid prescribed following surgery remains unknown. To examine the association of opioid prescribing duration limits with postoperative opioid prescribing in Massachusetts and Connecticut, the first 2 states to implement limits after March 2016. This interrupted time series analysis and cross-sectional study examined immediate level and slope changes in monthly outcomes after prescribing limit implementation in Massachusetts and Connecticut. These states implemented 7-day limits on initial opioid prescriptions on March 14, 2016, and July 1, 2016, respectively. Using the 2014 to 2017 IBM MarketScan Research Database, 16 281 opioid-naive adults in these states who filled a prescription within 3 days of surgery between July 1, 2014, and November 30, 2017, were identified. Data were analyzed from December 2018 to June 2019. The primary outcome was the prescription size in oral morphine equivalents (OMEs) for the initial postoperative opioid prescription (one 5/325 mg hydrocodone-acetaminophen pill = 5 OMEs). Secondary outcomes included days supplied in the initial prescription and the proportion of initial prescriptions exceeding a 7-day supply. In total, 16 281 opioid-naive patients (9708 [59.6%] female median [interquartile range] age range, 45-54 [35-44 to 55-64] years) undergoing surgical procedures were included. In Massachusetts, there were 5340 and 5435 patients in the preimplementation and postimplementation periods, respectively. In Connecticut, there were 2869 and 2637 patients in the preimplementation and postimplementation periods, respectively. Limit implementation in Massachusetts was associated with an immediate mean level decrease in prescription size (-38 OMEs [95% CI, -44 to -32 OMEs]) and with a mean decrease in slope (-1.5 OMEs/mo [95% CI, -2.1 to -0.9 OMEs/mo]). Implementation was also associated with an immediate mean level decrease in days supplied (-0.4 days [95% CI, -0.6 to -0.2 days]) and the proportion of prescriptions exceeding a 7-day supply (-5.9 percentage points [95% CI, -7.9 to -3.9 percentage points]). In contrast, limit implementation in Connecticut was not associated with level or slope changes in any outcome. Opioid prescribing duration limits had a variable association with postoperative opioid prescribing in Massachusetts and Connecticut. The mean opioid prescription size filled, days supplied, and prescribing exceeding a 7-day supply decreased after limit implementation in Massachusetts only. Given the potential differences in policy dissemination and uptake, efforts to reduce opioid prescribing should also include surgeon education and evidence-based prescribing recommendations.
Publisher: Springer Science and Business Media LLC
Date: 1974
DOI: 10.1007/BF00486616
Abstract: Proponents of personalized medicine predict that genetic information will provide pivotal perspectives for the prevention and management of complex disorders. Personalized medicine differs from traditional Western medicine, in that it focuses on more complex disorders that require mechanistic disease modeling and outcome simulation by integrating genomic risk, environmental stressors, and biomarkers as indicators of disease state. This information could be useful to guide targeted therapy and prevent pathologic outcomes. However, gaps exist in the process of linking the pieces together currently, genetic data are seldom used to assist physicians in clinical decision making. With rapid growth in genetic data and the requirements for new paradigms for complex disorders comes the need to train professionals to understand and manage the impact of genetic information on patients within these clinical settings. Here we describe the challenges, controversies, and opportunities for genetics and genetic counselors in managing complex disorders and discuss the rationale for modifications in genetic counselor training and function. We conclude that a major paradigm shift is underway and a compelling functional, ethical, and financial argument can be made for employing properly trained genetic counselors to be strategically positioned within the health-care industries that are responsible for managing complex disorders.
Publisher: Springer Science and Business Media LLC
Date: 11-04-2017
Publisher: Elsevier BV
Date: 06-2011
Publisher: Elsevier BV
Date: 02-1982
Publisher: Elsevier BV
Date: 1977
DOI: 10.1016/0305-0491(77)90159-6
Abstract: 1. Starch gel electrophoretic patterns of carbonic anhydrase (CA) isozymes were examined from tissue extracts of cats, sheep, rabbits and mice. 2. In addition to the widely distributed and extensively studied B and C isozymes, an additional isozyme (called CA-A) was observed. 3. Tissue distribution studies showed the A isozyme to be predominantly localized in red skeletal muscles, although this activity was also observed in white and "mixed" skeletal muscles of the cat, sheep and rabbit, as well as sheep lung and rabbit liver. 4. A, B and C isozymes of carbonic anhydrase from cat, sheep and mice exhibited independent variations in nett surface charge. In terms of decreasing anodal migration, the following results are reported: cat A greater than C greater than B sheep C greater than B greater than A and mouse B greater than C greater than A. 5. These results are consistent with the existence of 3 genetic loci encoding carbonic anhydrase in mammalian tissues.
Publisher: Wiley
Date: 24-04-2200
Publisher: Elsevier BV
Date: 1983
DOI: 10.1016/0020-711X(83)90075-7
Abstract: The processes associated with the biogenesis of peroxisomes in mouse liver have been studied by following the incorporation of radiolabelled leucine into major enzymic components of this organelle. Maximal incorporation of label into peroxisomal catalase and urate oxidase occurred within 2 hr, with the urate oxidase being labelled before catalase, but subsequent to the incorporation of phospholipid into this organelle. Subsequently, immunoprecipitation of catalase from the large granular fraction of mouse liver was shown to result in the isolation of a catalase molecule which had lost a peptide of approx. 2000 dalton from each subunit by comparison with the newly-synthesized enzyme. It was observed that the modification of catalase was obviated by the presence of leupeptin and iodoacetamide and this information has enabled the purification of both modified and unmodified forms of the enzyme. The possible significance of these data has been discussed and the major features incorporated into a working model of peroxisomal biogenesis.
Publisher: Wiley
Date: 11-1969
Abstract: Ornithine δ-aminotransferase (OAT, E.C. 2.6.1.13) catalyzes the transfer of the δ-amino group from ornithine (Orn) to α-ketoglutarate (aKG), yielding glutamate-5-semialdehyde and glutamate (Glu), and vice versa. In mammals, OAT is a mitochondrial enzyme, mainly located in the liver, intestine, brain, and kidney. In general, OAT serves to form glutamate from ornithine, with the notable exception of the intestine, where citrulline (Cit) or arginine (Arg) are end products. Its main function is to control the production of signaling molecules and mediators, such as Glu itself, Cit, GABA, and aliphatic polyamines. It is also involved in proline (Pro) synthesis. Deficiency in OAT causes gyrate atrophy, a rare but serious inherited disease, a further measure of the importance of this enzyme.
Publisher: Springer Science and Business Media LLC
Date: 04-1988
DOI: 10.1007/BF00561459
Abstract: Overexpression of type I interferon (IFN-I)-induced genes is a common feature of systemic lupus erythematosus (SLE) and its experimental models, but the participation of endogenous overproduction of IFN-I on it is not clear. To explore the possibility that abnormally increased IFN-I receptor (IFNAR) signaling could participate in IFN-I-induced gene overexpression of SLE, we examined the phosphorylation status of the IFNAR-associated signaling partners Jak1 and STAT2, and its relation with expression of its physiologic inhibitor SOCS1 and with plasma levels of IFNα and IFN-like activity. Peripheral blood mononuclear cells (PBMC) from SLE patients with or without disease activity and healthy controls cultured in the presence or in the absence of IFNβ were examined by immunoprecipitation and/or western blotting for expression of the two IFNAR chains, Jak1, Tyk2, and STAT2 and their phosphorylated forms. In SLE but not in healthy control PBMC, Jak1 and STAT2 were constitutively phosphorylated, even in the absence of disease activity (basal pJak1: controls vs. active SLE p<0.0001 and controls vs. inactive SLE p = 0.0006 basal pSTAT2: controls vs. active and inactive SLE p<0.0001). Although SOCS1 protein was slightly but significantly decreased in SLE in the absence or in the presence of IFNβ (p = 0.0096 to p<0.0001), in SOCS1 mRNA levels were markedly decreased (p = 0.036 to p<0.0001). IFNβ induced higher levels of the IFN-I-dependent MxA protein mRNA in SLE than in healthy controls, whereas the opposite was observed for SOCS1. Although there was no relation to increased serum IFNα, active SLE plasma could induce expression of IFN-dependent genes by normal PBMC. These findings suggest that in some SLE patients IFN-I dependent gene expression could be the result of a low IFNAR signaling threshold.
Publisher: Springer Science and Business Media LLC
Date: 04-1981
DOI: 10.1007/BF00504278
Abstract: Phosphoinositides (PPIns) are lipid signaling molecules that act as master regulators of cellular signaling. Recent studies have revealed novel roles of PPIns in myriad cellular processes and multiple human diseases mediated by misregulation of PPIn signaling. This review will present a timely summary of recent discoveries in PPIn biology, specifically their role in regulating unexpected signaling pathways, modification of signaling outcomes downstream of integral membrane proteins, and novel roles in lipid transport. This has revealed new roles of PPIns in regulating membrane trafficking, immunity, cell polarity, and response to extracellular signals. A specific focus will be on novel opportunities to target PPIn metabolism for treatment of human diseases, including cancer, pathogen infection, developmental disorders, and immune disorders.
Publisher: Elsevier BV
Date: 1981
Publisher: Springer Science and Business Media LLC
Date: 12-1978
DOI: 10.1007/BF00484541
Publisher: Wiley
Date: 03-2004
Publisher: Elsevier BV
Date: 05-2011
DOI: 10.1016/J.CBI.2011.01.014
Abstract: Mammalian ALDH3 genes (ALDH3A1, ALDH3A2, ALDH3B1 and ALDH3B2) encode enzymes of peroxidic and fatty aldehyde metabolism. ALDH3A1 also plays a major role in anterior eye tissue UV-filtration. BLAT and BLAST analyses were undertaken of several vertebrate genomes using rat, chicken and zebrafish ALDH3-like amino acid sequences. Predicted vertebrate ALDH3 sequences and structures were highly conserved, including residues involved in catalysis, coenzyme binding and enzyme structure as reported by Liu et al. [27] for rat ALDH3A1. Phylogeny studies of human, rat, opossum, platypus, chicken, xenopus and zebrafish ALDH3-like sequences supported three hypotheses: (1) the mammalian ALDH3A1 gene was generated by a tandem duplication event of an ancestral vertebrate ALDH3A2 gene (2) multiple mammalian and chicken ALDH3B-like genes were generated by tandem duplication events within genomes of related species and (3) vertebrate ALDH3A and ALDH3B genes were generated prior to the appearance of bony fish more than 500 million years ago.
Publisher: Elsevier BV
Date: 02-2013
Publisher: Elsevier BV
Date: 05-2011
Publisher: Wiley
Date: 1988
Publisher: Wiley
Date: 11-1978
Abstract: Cellulose acetate zymograms of alcohol dehydrogenase (ADH) and sorbitol dehydrogenase (SDH) extracted from male reproductive tissues of inbred mice were examined. ADH isozymes were differentially distributed in these tissues of C3H/He mice ADH-B2 was observed in all tissues and testis cellular preparations examined ADH-C2 was localized predominantly in the epididymis but was also present in the seminal vesicles, coagulating gland, and prostate gland. SDH was broadly distributed in these tissues but exhibited highest activities in the seminal vesicles, coagulating glands, and germinal cells of mature testes. Genetic variants for ADH-C2 and SDH provided evidence for (1) the identity of a second form of SDH in epididymis with ADH-C2 (2) the genetic identity of kidney, seminal vesicle, and testis SDH and (3) the gentic identity of stomach and epididymal ADH-C2. Developmental changes in testis and epididymal ADH isozymes during maturation were examined. ADH-C2 appeared in the mature epididymis whereas ADH-B2 exhibited no major changes in activity in testis and epididymis during development.
Publisher: Elsevier BV
Date: 1978
Publisher: Hindawi Limited
Date: 10-1990
DOI: 10.1017/S0016672300035369
Abstract: A didelphid marsupial, the gray short-tailed opossum ( Monodelphis domestica ), was used as a model species to study the biochemical genetics of alcohol dehydrogenases (ADHs) and aldehyde dehydrogenase (ALDH) in corneal tissue. Isoelectric point variants of corneal ALDH (designated ALDH3) and a major soluble protein in corneal extracts were observed among eight families of animals used in studying the genetics of these proteins. Both phenotypes exhibited identical patterns following PAGE-IEF and were inherited in a normal Mendelian fashion, with two alleles at a single locus ( ALDH3 ) showing codominant expression. The data provided evidence for genetic identity of corneal ALDH with this major soluble protein, and supported biochemical evidence, recently reported for purified bovine corneal ALDH, that this enzyme constitutes a major portion of soluble corneal protein (Abedinia et al. 1990). Isoelectric point variants for corneal ADH were also observed, with patterns for the two major forms (ADH3 and ADH4) and one minor form (ADH5) being consistent with the presence of two ADH subunits (designated γ and δ), and variant phenotypes existing for the γ subunit. The genetics of this enzyme was studied in the eight families, and the results were consistent with codominant expression of two alleles at a single locus (designated ADH3 ). It is relevant that a major detoxification function has been proposed for corneal ADH and ALDH, in the oxidoreduction of peroxidic aldehydes induced by available oxygen and UV-B light (Holmes & VandeBerg, 1986 a ). In addition, a direct role for corneal ALDH as a UV-B photoreceptor in this anterior eye tissue has also been proposed (Abedinia et al. 1990).
Publisher: SAGE Publications
Date: 10-1983
DOI: 10.1258/002367783781062235
Abstract: 36 genetic markers were examined in 14 inbred strains of mice maintained at the Cancer Research Institute, Bombay. The genetic marker profiles of these strains when compared with the profiles of similar strains maintained elsewhere revealed discrepancies in 4 of them which are reported and discussed. The results emphasize the importance of genetic monitoring of inbred strains.
Publisher: Elsevier BV
Date: 1985
Publisher: Springer Science and Business Media LLC
Date: 26-01-2011
Publisher: Elsevier BV
Date: 03-1980
Publisher: Wiley
Date: 1985
DOI: 10.1111/J.1365-2052.1985.TB01451.X
Abstract: The genetic variability of alcohol dehydrogenase (C2 isozyme), aldehyde dehydrogenase (A2 isozyme) and aldehyde oxidase (A2 isozyme) has been examined among recombinant inbred strains of mice which have been previously studied concerning their differential behavioural responses towards alcohol. The results showed no correlation between biochemical phenotype for these loci and behavioural response.
Publisher: Elsevier BV
Date: 06-2015
Publisher: Springer Science and Business Media LLC
Date: 06-1985
DOI: 10.1007/BF00499088
Abstract: Studies using allergen challenge models have suggested Th2 cytokines promote airway inflammation in asthma. We assessed mediators of airway inflammation during the chronic asymptomatic phase of asthma. Nine non-atopic asthma (NAA) patients, 19 atopic asthma (AA) patients, 20 atopic controls (AC), and 38 normal controls (NC) underwent sputum induction while asymptomatic. Sputum total cell counts and differentials were determined levels of cytokines IL-4, IL-5, IL-13, GM-CSF, and IFN-gamma, and chemokines eotaxin (CCL11) and RANTES (CCL5) were measured by ELISA and levels of eosinophil-derived neurotoxin (EDN) were measured by radioimmunoassay. NAA patients showed higher % eosinophils and total eosinophils compared to AA. NAA and AA patients showed higher IFN-gamma and EDN levels compared to AC and NC, with no differences in IL-4, IL-5, or IL-13 levels among the four groups. GM-CSF levels were higher in AA patients compared to AC or NC. In NAA, AA, and AC patients, % eosinophils and EDN levels correlated positively with IFN-gamma, GM-CSF, eotaxin, and RANTES, but not with IL-5 levels. Baseline airway inflammation of intrinsic and extrinsic asthma is characterized by eosinophilic inflammation and the Th1 cytokine, IFN-gamma. GM-CSF, instead of IL-5, and chemokines may coordinate airway eosinophilia during the chronic asymptomatic phase of asthma.
Publisher: Elsevier BV
Date: 09-2008
Publisher: Wiley
Date: 24-04-2009
DOI: 10.1111/J.1365-2052.1982.TB01048.X
Abstract: Genetic analysis of a proposed cis-acting temporal locus (Adh-3t), which regulates alcohol dehydrogenase C2 (ADH-C2) activity in mouse epididymis extracts, among F1 (ddN X BALB/c) X ddN male backcross progeny provided evidence for genetic distinctness between the structural (Adh-3) and temporal (Adh-3t) loci on chromosome 3. Genetic analysis also confirmed the close linkage of Adh-1 (encoding liver and kidney ADH-A2) and Adh-3 (encoding stomach ADH-C2) to within 0.3 centimorgans on the mouse genome. Evidence is presented for a proposed closely linked cis-acting temporal locus (designated Adh-lt) for the A2 isozyme (encoded by Adh-1) controlling the activity of this enzyme in mouse kidney extracts, but having no apparent affect on liver and intestine ADH-A2 activities. An extensive survey of the distribution of Adh-1, Adh-3 and Adh-3t alleles among 65 strains of mice is reported--with the exception of two Japanese strains (ddN and KF), linkage disequilibrium between Adh-3 and Adh-3t was observed. Sex differences in mouse liver and kidney ADH-A2 activities were observed, with male/female ratios of approximately 0.6 and 3 respectively for these tissue extracts.
Publisher: The Endocrine Society
Date: 06-1996
DOI: 10.1210/JC.81.6.2247
Publisher: Elsevier BV
Date: 1989
DOI: 10.1016/0305-0491(89)90081-3
Abstract: 1. Isoelectric focusing (IEF) and zymogram methods were used to examine the tissue distribution, multiplicity and substrate specificities of alcohol dehydrogenases (ADHs), aldehyde dehydrogenases (ALDHs) and ocular oxidases (EOXs) from mammalian anterior eye tissues. 2. Baboon, cattle, pig and sheep corneal extracts exhibited high ALDH activities the corneal ALDHs were distinct from the major liver ALDHs and distinguished by their preference for medium-chain aldehydes. 3. Baboon and pig corneal extracts also showed high ADH activities, by comparison with ovine and bovine s les. Moreover, the ADHs were distinct from the major liver isozymes in pI value and substrate specificity. 4. Mammalian lens extracts exhibited significant ALDH activity of a form corresponding to the major liver cytosolic isozyme. Minor activity of the corneal enzyme was also observed in some species. 5. Lens ADH phenotypes were species-specific, and consisted of either Class II activity (baboon and sheep), Class III ADH activity (pig), or activities of both ADH classes (cattle). 6. Lens extracts also exhibited a complex pattern of ocular oxidase (EOX) activities following IEF. 7. A role in peroxidatic aldehyde detoxification is proposed for these enzymes in anterior eye tissues.
Publisher: Springer Science and Business Media LLC
Date: 12-1981
DOI: 10.1007/BF00484575
Publisher: Springer Science and Business Media LLC
Date: 08-1971
Publisher: Springer Science and Business Media LLC
Date: 08-1970
DOI: 10.1007/BF00486597
Abstract: In this study, CN-TiO₂ was modified with cryptomelane octahedral molecular sieves (OMS-2) by the sol-gel method based on the self-assembly technique to enhance its photocatalytic activity under the daylight irradiation. The synthesized s les were characterized by X-ray diffraction (XRD), UV-vis spectroscopy, Fourier transform infrared spectroscopy (FT-IR) and porosimeter analysis. The results showed that the addition of OMS-2 in the sol lead to higher Brunauer-Emmett-Teller (BET) surface area, pore volume, porosity of particle after heat treatment and the specific surface area, porosity, crystallite size and pore size distribution could be controlled by adjusting the calcination temperature. Compared to the CN-TiO₂-400 s le, CN-TiO₂/OMS-2-400 exhibited greater red shift in absorption edge of s les in visible region due to the OMS-2 coated. The enhancement of photocatalytic activity of CN-TiO₂/OMS-2 composite photocatalyst was subsequently evaluated for the degradation of the methyl orange dye under the daylight irradiation in water. The results showed that the methyl orange dye degradation rate reach to 37.8% for the CN-TiO₂/OMS-2-400 s le under the daylight irradiation for 5 h, which was higher than that of reference s le. The enhancement in daylight photocatalytic activities of the CN-TiO₂/OMS s les could be attributed to the synergistic effects of OMS-2 coated, larger surface area and red shift in adsorption edge of the prepared s le.
Publisher: Elsevier BV
Date: 10-1970
DOI: 10.1016/0304-4165(70)90360-0
Abstract: We aimed to study the efficacy and safety of the tension-free vaginal tape (TVT)-Abbrevo procedure for female stress urinary incontinence (SUI). This was a prospective cohort study that aimed to determine the subjective and objective cure, improvement of SUI and incidence of complications among women who underwent TVT-Abbrevo for SUI during a period of 22 months from September 2011 to June 2013. A total of 76 patients, with a mean age of 48.2 ± 8.1 years, underwent TVT-Abbrevo during the study period. Among them, 86.8% had vaginal delivery and 5.3% had instrumental delivery. Mean parity was 2.3 ± 0.8 and mean body mass index was 27.0 ± 5.0 kg/m Our results are comparable with those of other studies, although long-term results remain to be seen.
Publisher: Wiley
Date: 03-1974
DOI: 10.1111/J.1432-1033.1974.TB03397.X
Abstract: Bacterial infections are a major threat to the health of patients in healthcare facilities including hospitals. One of the major causes of patient morbidity is infection with Staphylococcus aureus. One of the the most dominant nosocomial bacteria, Methicillin Resistant Staphylococcus aureus (MRSA) have been reported to survive on hospital surfaces (e.g. privacy window glasses) for up to 5 months. None of the current anti-bacterial technology is efficient in eliminating Staphylococcus aureus. A novel transparent, immobilised and superhydrophilic coating of titanium dioxide, co-doped with fluorine and copper has been prepared on float glass substrates. Antibacterial activity has demonstrated (by using Staphylococcus aureus), resulting from a combination of visible light activated (VLA) photocatalysis and copper ion toxicity. Co-doping with copper and fluorine has been shown to improve the performance of the coating, relative to a purely fluorine-doped VLA photocatalyst. Reductions in bacterial population of log10 = 4.2 under visible light irradiation and log10 = 1.8 in darkness have been achieved, compared with log10 = 1.8 under visible light irradiation and no activity, for a purely fluorine-doped titania. Generation of reactive oxygen species from the photocatalytic coatings is the major factor that significantly reduces the bacterial growth on the glass surfaces.
Publisher: Wiley
Date: 05-1981
Publisher: Elsevier BV
Date: 04-2006
Publisher: Elsevier BV
Date: 1972
DOI: 10.1016/0003-9861(72)90134-8
Abstract: Epigenetic reprogramming allows cancer cells to bypass normal checkpoints and potentiate aberrant proliferation. Several chromatin regulators are subject to reversible SUMO-modification but little is known about how SUMOylation of chromatin-remodelers modulates the cancer epigenome. Recently, we demonstrated that SUMO-protease SENP7L is upregulated in aggressive BCa and maintains hypoSUMOylated heterochromatin protein 1-α (HP1α). Canonical models define HP1α as a "reader" of repressive H3K9m3 marks that supports constitutive heterochromatin. It is unclear how SUMOylation affects HP1α function in BCa cells. This report shows HP1α SUMO-dynamics are closely regulated in a complex with SENP7L and SUMO-E3 Polycomb-2 (PC2/CBX4). This complex accumulates at H3K9m3 sites, hypoSUMOylates HP1α and PC2, and reduces PC2's SUMO-E3 activity. HyperSUMO conditions cause complex dissociation, SUMOylation of PC2 and HP1α, and recruitment of SUMOylated HP1α to multiple DNA-repair genes including Rad51C. SUMOylated HP1α's enrichment at euchromatin requires chromatin-bound non-coding RNA (ncRNA), reduces Rad51C protein, and increases DNA-breaks in BCa cells. Hence, HP1α SUMOylation and consistently low SENP7L increase efficacy of DNA-damaging chemotherapeutic agents. BCa patients on chemotherapy that express low SENP7L exhibit greater survival rates than patients with high SENP7L. Collectively, these studies suggest that SUMOylated HP1α is a critical epigenetic-regulator of DNA-repair in BCa that could define chemotherapy responsiveness.
Publisher: Elsevier BV
Date: 07-1991
DOI: 10.1016/0378-1119(91)90275-G
Abstract: Five alcohol dehydrogenases (ADH alcohol: NAD+ oxidoreductase EC 1.1.1.1) have been identified in the baboon. All are homodimers of five distinct ADH subunits, with the two class-I ADH subunits being differentially expressed in the liver (the beta-subunit) and kidney. We have hybridized restriction-enzyme-digested baboon DNA to a 30-bp probe or a 337-bp DNA fragment, to reveal the presence of three genes encoding class-I ADH subunits in the baboon genome. This result was confirmed by the lification of three different baboon ADH (bADH) nucleotide (nt) sequences, corresponding to exon 5 in the human gene encoding ADH beta (hADHB) from baboon DNA. Two of these sequences are identical to previously isolated liver and kidney cDNA nt sequences. These results are consistent with a phylogenetic analysis of the nt sequences of class-I hADH and bADH genes. Then, using primers based on the nt sequence of hADHB, we lified a 336-bp DNA fragment, from genomic DNA, encoding the 5' region of the bADHB gene. In a 49-bp region of overlap, the nt sequence of this DNA fragment was identical to the sequence of a cDNA fragment lified from baboon liver mRNA, whereas there were seven differences between this DNA fragment and the sequence of a cDNA lified from baboon kidney mRNA. We used primer extension analysis to identify three adjacent transcriptional start points (tsp) for bADHB mRNA. Initiation of transcription at the most 5' bp leaves a 72-bp untranslated region. Examination of the sequence upstream from the tsp reveals a number of conserved putative regulatory sequence elements.
Publisher: Ovid Technologies (Wolters Kluwer Health)
Date: 1994
DOI: 10.1097/00003226-199401000-00011
Abstract: Adult male mice from four inbred albino strains (SJL/J, NZW/BL, BALB/c HeA, and SWR/J) were subjected to ultraviolet radiation (UVR) exposure (302 nm peak wavelength, intensity 398 microW/cm2) for 3.25 min and photographed 4 days postexposure to assess corneal clouding. Corneal extracts from control (unexposed) mice from each strain, were also monitored for aldehyde dehydrogenase (ALDH) and alcohol dehydrogenase (ADH) activity and soluble protein content. The SWR/J strain exhibited more extensive corneal clouding after UV exposure than did the other strains, and control SWR/J mice exhibited a low activity variant phenotype for the major ocular ALDH AHD-4, and decreased levels of soluble protein in corneal extracts. These data support earlier proposals for a major role for ALDH in assisting the cornea in protecting the eye against UVR-induced tissue damage.
Publisher: Elsevier BV
Date: 04-1989
DOI: 10.1016/0167-4838(89)90076-9
Abstract: The major isozyme of aldehyde dehydrogenase in mouse stomach, AHD-4, has been purified to homogeneity and characterized with a range of aldehyde substrates at pH 7.4. The enzyme was a dimer with a subunit size of 65 kDa. Using V/Km values as an indication of substrate efficacy, aromatic aldehydes were the preferred substrates. The enzyme used either NAD+ or NADP+ as cofactor, but showed a preference for NAD+. AHD-4 showed 'high-Km' properties with respect to acetaldehyde, but differed from the 'high-Km' liver mitochondrial enzyme (AHD-1), in that it was not a semialdehyde dehydrogenase. The enzyme was significantly active towards the peroxidic aldehyde, 4-hydroxynonenal, and may play a role in vivo in the detoxification of aromatic aldehydes and the aldehyde products of lipid peroxidation.
Publisher: Wiley
Date: 14-01-2009
Publisher: Springer Science and Business Media LLC
Date: 2008
Publisher: Elsevier BV
Date: 1985
DOI: 10.1016/0305-0491(85)90380-3
Abstract: Isoelectric focusing techniques (IEF) were used to examine the tissue distribution and genetic variability of aldehyde dehydrogenases (AHDs) from inbred strains of mice. Twelve zones of AHD activity were resolved which were differentially distributed between tissues. Liver extracts exhibited highest activity for most enzymes, with the exception of isozymes found in stomach (AHD-4) and testis (AHD-4 and AHD-6). Genetic variants for AHD-1 (liver mitochondrial isozyme) and AHD-4 (stomach isozyme) were examined from inbred strains and F1 hybrid animals. The results were consistent with dimeric subunit structures (designated as A2 and D2 isozymes respectively). IEF patterns for activity variants of testis-specific AHD-6 were identical, with 3-banded phenotypes being observed. pI values for the AHD forms as well as for aldehyde oxidase and xanthine oxidase isozymes, which stain in the absence of coenzyme, were reported.
Publisher: Elsevier BV
Date: 04-2019
DOI: 10.1016/J.CBI.2019.01.023
Abstract: Bioinformatic analyses of salmon (Salmo salar) ALDH amino acid sequences supported the presence of at least 30 ALDH genes, which is more than for any other higher vertebrate and is greater than the 19 human ALDH genes currently reported. These included 8 polyploid ALDH genes and proteins: ALDH1A2 (chromosomes 11 and 26) ALDH1L2 (chromosomes 7 and 17) ALDH2, encoding mitochondrial ALDH2 (chromosomes 2 and 5) ALDH3A2 (chromosomes 4, 9 and 20), for which evidence for 5 genes was obtained ALDH3B1 (chromosomes 3, 6 and 24) ALDH4A1 (chromosomes 12 and 22) ALDH6A1 (chromosomes 1, 6 and 15) and ALDH18A1 (chromosomes 19 and 28). In contrast, 7 salmon ALDH gene families (ALDH1A1, ALDH1A3, ALDH5, ALDH7, ALDH8, ALDH9 and ALDH16) possessed only one gene family member. Phylogenetic studies of salmon and rainbow trout ALDH3A2 genes and proteins suggested that salmonid gene tetraploidy has occurred in at least 2 distinct stages of ALDH3A2 gene evolution.
Publisher: Elsevier BV
Date: 1984
DOI: 10.1016/0305-0491(84)90156-1
Abstract: Cellulose acetate zymograms of alcohol dehydrogenase (ADH), aldehyde dehydrogenase (AHD), aldehyde reductase (AHR), aldehyde oxidase (AOX) and xanthine oxidase (XOX) extracted from horse tissues were examined. Five ADH isozymes were resolved: three corresponded to the previously reported class I ADHs (EE, ES and SS) (Theorell, 1969) a single form of class II ADH (designated ADH-C2) and of class III ADH (designated ADH-B2) were also observed. The latter isozyme was widely distributed in horse tissues whereas the other enzymes were found predominantly in liver. Four AHD isozymes were differentially distributed in subcellular preparations of horse liver: AHD-1 (large granules) AHD-3 (small granules) and AHD-2, AHD-4 (cytoplasm). AHD-1 was more widely distributed among the horse tissues examined. Liver represented the major source of activity for most AHDs. A single additional form of NADPH-dependent AHR activity (identified as hexonate dehydrogenase), other than the ADHs previously described, was observed in horse liver. Single forms of AOX and XOX were observed in horse tissue extracts, with highest activities in liver.
Publisher: Elsevier BV
Date: 04-1968
DOI: 10.1016/0005-2744(68)90246-5
Abstract: As proton therapy becomes increasingly popular, so does the need for Monte Carlo simulation studies involving accurate beam line modeling of proton treatment units. In this study, the 24 beam configurations of the Mevion S250 proton therapy system installed recently at our institution were modeled using the TOolkit for PArticle Simulation (TOPAS) code. Pristine Bragg peak, spread out Bragg peak (SOBP), and lateral beam profile dose distributions were simulated and matched to the measurements taken during commissioning of the unit. Differences in the range for all Percent Depth Dose (PDD) curves between measured and simulated data agreed to within 0.1 cm. For SOBP scans, the SOBP widths all agreed to within 0.3 cm. With regards to lateral beam profile comparisons between the measured and simulated data, the penumbras differed by less than 1 mm and the flatness differed by less than 1% in nearly all cases. This study shows that Monte Carlo simulation studies involving the Mevion S250 proton therapy unit can be a viable tool in commissioning and verification of the proton treatment planning system.
Publisher: Wiley
Date: 11-1980
Publisher: Wiley
Date: 11-1986
DOI: 10.1111/J.1530-0277.1986.TB05157.X
Abstract: Isoelectric focusing and cellulose acetate electrophoresis were used to examine the multiplicity, tissue distribution, and variability of alcohol dehydrogenase (ADH) among baboons, a primate species used as a model for research on alcohol metabolism and alcohol-induced liver pathology. Five major ADH isozymes were resolved and distinguished on the basis of their isoelectric points, tissue distributions, relative activities with alcohol substrates, and sensitivities to inhibition with 4-methyl pyrazole. ADH-1 and ADH-2 exhibited class I kinetic properties and were observed in high activity in kidney and liver extracts, respectively. ADH-3 showed class II kinetic properties, exhibiting high activity in stomach extracts, and was widely distributed in extracts of other baboon tissues, including kidney, esophagus, heart, testis, brain, and male sex accessory tissues. ADH-4 also showed class II ADH properties but was found only in liver (similar to human "pi-ADH"). ADH-5 exhibited class III ADH kinetic properties, being inactive with ethanol up to 0.5 M (similar to human "chi-ADH") and was distributed widely in baboon tissue extracts. Major activity variation was observed for liver ADH-4 between different animals. An electrophoretic variant for ADH-3 was observed for the enzyme in stomach, kidney, and testis extracts, and activity variation existed for this isozyme in kidney extracts. It is apparent that baboon ADH shares a number of features with the human ADH phenotype however, several species-specific differences were observed, particularly for the liver and kidney class I isozymes and for stomach ADH.
Publisher: Elsevier BV
Date: 12-1975
Publisher: Elsevier BV
Date: 09-2023
Publisher: Wiley
Date: 02-1995
DOI: 10.1111/J.1530-0277.1995.TB01490.X
Abstract: A partial human stomach alcohol dehydrogenase (ADH) encoding cDNA has been isolated, cloned, and sequenced, which contains 222 nucleotides encoding amino acid residues 227-299 of the ADH subunit. The amino acid sequence deduced from this cDNA was highly homologous with the rat stomach class IV ADH sequence recently reported (81.1% sequence identity). Homology with other human ADH classes was also observed: class I, 58.1% sequence identity class II, 39.2% sequence identity class III, 55.4% sequence identity and class V, 50.0% sequence identity. These results support a proposal that the isolated cDNA encodes a partial sequence for human stomach class IV ADH. This sequence retains val294 for all other human ADH classes reported, as compared with an ala294 at this position reported for rat class IV ADH. This ala residue may contribute to the very high Km values with ethanol for the latter enzyme. In addition, three substitutions are reported for key residues in the coenzyme binding site: 251, gln/ser 260, gly/asn and 261, gly/asn, which may contribute to the weak coenzyme binding properties reported for human class IV ADH.
Publisher: Wiley
Date: 12-1983
DOI: 10.1111/J.1432-1033.1983.TB07807.X
Abstract: Alcohol dehydrogenase isozymes from mouse liver (A 2 and B 2 ) and stomach (C 2 ) tissues have been purified to homogeneity using triazine‐dye affinity chromatography. The enzymes are dimers with similar but distinct subunit sizes, as determined by SDS olyacrylamide gel electrophoresis: A, 43000 B, 39000, and C, 47000. Zinc analyses and 1,10‐phenanthroline inhibition studies indicated that the A and C subunits each contained two atoms of zinc, with at least one being involved catalytically, whereas the B subunit probably contained a single non‐catalytic zinc atom. The isozymes exhibited widely ergent kinetic characteristics. A 2 exhibited a K m value for ethanol of 0.15 mM and a broad substrate specificity, with K m values decreasing dramatically with an increase in chain length: C 2 also exhibited this broad specificity for alcohols but showed a K m value of 232 mM for ethanol. These isozymes also showed broad substrate specificities as aldehyde reductases. In contrast, B 2 showed no detectable activity as an aldehyde reductase for the aldehydes examined, and used ethanol as substrate only at very high concentrations ( .5 M). The isozyme exhibited low K m and high V max values, however, with medium‐chain alcohols. Immunological studies showed that A 2 was immunologically distinct from the B 2 and C 2 isozymes. In vitro molecular hybridization studies gave no evidence for association between the alcohol dehydrogenase subunits. The results confirm genetic analyses [Holmes, Albanese, Whitehead and Duley (1981) J. Exp. Zool. 215 , 151–157] which are consistent with at least three structural genes encoding alcohol dehydrogenase in the mouse and confirm the role of the major liver isozyme (A 2 ) in ethanol metabolism.
Publisher: Elsevier BV
Date: 06-2015
DOI: 10.1016/J.CBI.2014.11.002
Abstract: Vertebrate ALDH1A-like genes encode cytosolic enzymes capable of metabolizing all-trans-retinaldehyde to retinoic acid which is a molecular 'signal' guiding vertebrate development and adipogenesis. Bioinformatic analyses of vertebrate and invertebrate genomes were undertaken using known ALDH1A1, ALDH1A2 and ALDH1A3 amino acid sequences. Comparative analyses of the corresponding human genes provided evidence for distinct modes of gene regulation and expression with putative transcription factor binding sites (TFBS), CpG islands and micro-RNA binding sites identified for the human genes. ALDH1A-like sequences were identified for all mammalian, bird, lizard and frog genomes examined, whereas fish genomes displayed a more restricted distribution pattern for ALDH1A1 and ALDH1A3 genes. The ALDH1A1 gene was absent in many bony fish genomes examined, with the ALDH1A3 gene also absent in the medaka and tilapia genomes. Multiple ALDH1A1-like genes were identified in mouse, rat and marsupial genomes. Vertebrate ALDH1A1, ALDH1A2 and ALDH1A3 subunit sequences were highly conserved throughout vertebrate evolution. Comparative amino acid substitution rates showed that mammalian ALDH1A2 sequences were more highly conserved than for the ALDH1A1 and ALDH1A3 sequences. Phylogenetic studies supported an hypothesis for ALDH1A2 as a likely primordial gene originating in invertebrate genomes and undergoing sequential gene duplication to generate two additional genes, ALDH1A1 and ALDH1A3, in most vertebrate genomes.
Publisher: Elsevier BV
Date: 03-1967
DOI: 10.1016/0005-2744(67)90157-X
Abstract: Assess visual impairment in school children of upper-middle socioeconomic status in Kathmandu for comparison with rural Jhapa District. Random selection of classes from secondary private schools in Kathmandu was used to identify the study s le. Children in 130 classes at 43 schools were enumerated using school records and examined between January-May 2006. Examinations included visual acuity testing, ocular motility evaluation, cycloplegic refraction, and examination of the external eye, anterior segment, media, and fundus. The principal cause was determined for eyes with uncorrected visual acuity < or = 20/40. A total of 4,501 children in grades 5-9 were enumerated 4282 (95.1%) were examined. The prevalence of uncorrected, presenting, and best-corrected visual impairment (< or = 20/40) in the better eye was 18.6%, 9.1%, and 0.86%, respectively. Refractive error was a cause in 93.3% of children with uncorrected visual impairment, amblyopia 1.8%, retinal disorders 1.3%, other causes 0.3%, and unexplained causes 4.4%. Among children correctable in at least one eye, 46.3% presented without the necessary spectacles. Visual impairment with myopia (-0.50 diopters) ranged from 10.9% in 10 year-olds to 27.3% in 15 year-olds, compared to 0.5%-3.0% in rural Jhapa District. Myopic visual impairment was associated with grade level, female gender, parental education, parental spectacle usage, and Mongol ethnicity. Visual impairment with myopia among upper-middle socioeconomic school children in Kathmandu is higher than that in rural Nepal, and a public health problem because nearly half are without corrective spectacles. Effective strategies are needed to eliminate this easily treatable cause of visual impairment.
Publisher: Elsevier BV
Date: 1980
Publisher: Elsevier BV
Date: 1984
DOI: 10.1016/0020-711X(84)90084-3
Abstract: An alcohol dehydrogenase (ADH) from horse liver was purified by ion-exchange and affinity chromatography. The enzyme (designated ADH-C2), is a dimer with a similar subunit size (47,300 mol. wt), as determined by SDS-polyacrylamide gel electrophoresis, to other mammalian ADHs. Zinc analyses and 1,10 phenanthroline inhibition studies indicated that each subunit contained 2 g atoms of zinc, with at least one involved catalytically. The enzyme exhibited similar kinetic properties to human pi-ADH and mouse ADH-C2, previously classified as class II ADHs [Vallee and Bazzone (1983) Isozymes, Vol. 8, pp. 219-244 Algar et al. (1983) Eur. J. Biochem. 137, 139-147] but differed in most respects from the extensively investigated horse Class I ADHs EE, ES and SS. Horse ADH-C2 exhibited a Km value for ethanol of 42 mM and a broad substrate specificity, with Km values decreasing dramatically with an increase in chain length. The enzyme was much less sensitive to pyrazole inhibition (by at least 3 orders of magnitude) as compared with the Class I ADHs.
Publisher: Elsevier BV
Date: 08-1970
Publisher: Oxford University Press (OUP)
Date: 1999
DOI: 10.1093/OXFORDJOURNALS.MOLBEV.A026035
Abstract: The three class I alcohol dehydrogenases (ADHs) in humans comprise homo- and heterodimers of three subunits (alpha, beta, and gamma) with greater than 90% sequence identity. These are encoded by distinct genes (ADH1, ADH2, and ADH3, respectively) and are all expressed in the liver. In baboons, only the beta ADH subunit is expressed in liver. A second class I ADH is expressed in the kidney we isolated, cloned, and sequenced the cDNA corresponding to this ADH and conclude that it is of the gamma ADH lineage. We also lified and sequenced the 5' noncoding regions of all three class I baboon ADH genes and the rhesus monkey ADH1 gene and compared their nucleotide sequences with the corresponding human sequences. There is clear evidence that the evolution of these genes has been reticulate. At least three gene conversion events, affecting the coding and 3' noncoding regions of the genes, are inferred from compatibility and partition matrices and phylogenetic analysis of the sequences. Our estimation of the evolutionary history of these genes provides a framework for the investigation of relative substitution rates and functional variation among the sequences. Relative-rate tests, designed to account for the reticulate evolution of these genes, indicate no difference in substitution rate either between genes encoding different subunits or between human and Old World monkey lineages. The human and baboon gamma ADH sequences do not show clear differences at functionally important sites within the coding region, but they do differ at a number of sites in regions previously proposed to be regulatory sites for transcriptional control. This variation may explain the different patterns of gene expression in humans and baboons.
Publisher: Elsevier BV
Date: 09-2010
Publisher: Wiley
Date: 04-1975
Abstract: Mouse liver hydroxyacid oxidase isozymes are present at low levels at birth and increase in activity until day 13 after which HAOX-B almost disappears and HZOS-A is reduced to approximately one half the maximum level in the adultkidney. HAOX-G appears near day 13 post partum and increases until adult levels are reached, the female having four times the activity of the male. The pregnant female has significantly lower levels of HAOX-A and HAOX-B in the liver and higher activity of HAOX-B in the kidney. Developmental changes occur in the extent of epigenetic modification of mouse liver HAOX-A during the early neonatal period.
Publisher: Wiley
Date: 06-1986
DOI: 10.1111/J.1365-2052.1986.TB03195.X
Abstract: The distribution of biochemical genetic variants was examined among eight inbred strains of mice, which served as contributors to a heterogeneous stock of mice (HS), and in short-sleep (SS) and long-sleep (LS) mice, selectively bred from the HS stock for differential ethanol sensitivity. Fifteen loci for enzymes of alcohol and aldehyde metabolism, as well as 12 other biochemical loci, were investigated. Thirteen of these loci exhibited allelic variation between strains, of which six were separately fixed in the SS and LS mice. Comparisons of genetic similarity coefficients, based upon the distributions of allelic variants for the loci examined, with behavioural sensitivities (sleep-time) to an acute dose of ethanol for the inbred and selected strains of mice, indicated no correlations between these data. This suggests that this collective group of loci are not useful indicators of the genes selectively bred in the SS and LS strains, which are responsible for the differential sensitivities to acute doses of ethanol.
Publisher: Springer Science and Business Media LLC
Date: 06-1979
DOI: 10.1007/BF00498887
Publisher: MDPI AG
Date: 24-09-2012
DOI: 10.3390/BIOM2030389
Publisher: Elsevier BV
Date: 03-2010
DOI: 10.1016/J.CBD.2009.09.004
Abstract: BLAT (BLAST-Like Alignment Tool) analyses of the opossum (Monodelphis domestica) and zebrafish (Danio rerio) genomes were undertaken using amino acid sequences of the acylglycerol acyltransferase (AGAT) superfamily. Evidence is reported for 8 opossum monoacylglycerol acyltransferase-like (MGAT) (E.C. 2.3.1.22) and diacylglycerol acyltransferase-like (DGAT) (E.C. 2.3.1.20) genes and proteins, including DGAT1, DGAT2, DGAT2L6 (DGAT2-like protein 6), AWAT1 (acyl CoA wax alcohol acyltransferase 1), AWAT2, MGAT1, MGAT2 and MGAT3. Three of these genes (AWAT1, AWAT2 and DGAT2L6) are closely localized on the opossum X chromosome. Evidence is also reported for six zebrafish MGAT- and DGAT-like genes, including two DGAT1-like genes, as well as DGAT2-, MGAT1-, MGAT2- and MGAT3-like genes and proteins. Predicted primary, secondary and transmembrane structures for the opossum and zebrafish MGAT-, AWAT- and DGAT-like subunits and the intron-exon boundaries for genes encoding these enzymes showed a high degree of similarity with other members of the AGAT superfamily, which play major roles in triacylglyceride (DGAT), diacylglyceride (MGAT) and wax ester (AWAT) biosynthesis. Alignments of predicted opossum, zebrafish and other vertebrate DGAT1, DGAT2, other DGAT2-like and MGAT-like amino acid sequences with known human and mouse enzymes demonstrated conservation of residues which are likely to play key roles in catalysis, lipid binding or in maintaining structure. Phylogeny studies of the human, mouse, opossum, zebrafish and pufferfish MGAT- and DGAT-like enzymes indicated that the common ancestors for these genes predated the appearance of bony fish during vertebrate evolution whereas the AWAT- and DGAT2L6-like genes may have appeared more recently prior to the appearance of marsupial and eutherian mammals.
Publisher: Wiley
Date: 03-1976
DOI: 10.1111/J.1432-1033.1976.TB10219.X
Abstract: L-alpha-Hydroxyacid oxidase isozymes from rat liver (A isozyme) and kidney (B isozyme) have been isolated in a high state of purity with specific activities of 61 and 14.7 microkatals per gram protein respectively. The subunit molecular weights determined by sodium dodecylsulphate polyacrylamide gel electrophoresis were 40000 +/- 3000 the mouse A and B isozymes were also partially purified and their subunit molecular weights shown to be 37000.
Publisher: Elsevier BV
Date: 03-2009
Publisher: Elsevier BV
Date: 04-1976
DOI: 10.1016/0005-2795(76)90211-7
Abstract: As the published values for the molecular weight of L-alpha-hydroxyacid oxidase vary from 89 000 to 430 000, it is possible that such variations could be due to a concentration dependence of the molecular weight. The molecular weight of rat L-alpha-hydroxyacid oxidase was studied over a wide range of concentrations, using equilibrium sedimentation and gel exclusion chromatography. The partial specific volumes (0.726 and 0.730 for hydroxyacid oxidase A and hydroxyacid oxidase B, respectively) were calculated from the amino acid compositions, and were used to calculat molecular weights from the equilibrium sedimentation data. The molecular weight at infinite dilution was found to be 150 000 for both the A and B isozymes. Both isozymes exhibit association-dissociation behaviour at low concentrations. The self-association of the hydroxyacid oxidase B isozyme can be described by the relation (see article) where K1,2 = 5.4-10(5) M-1 and K2,4 = 1.7-10(5) M-1. Previously published values of the molecular weight of these isozymes are in accord with the observed concentration dependence.
Publisher: Wiley
Date: 08-1972
Publisher: Wiley
Date: 08-1979
Abstract: Lactate dehydrogenase (LDH) C, activity was observed in testis extracts from normal mice but was progressively reduced in mice carrying the male-sterile translocations T31H, T32H, T37H, T38H, T40H and T42H, with no detectable activity being observed in the last two mice. None of the vesicular gland extracts from these male-steriles showed LDH-C4 activity, unlike normal mice. The differential LDH-C4 activity in male-sterile testes is interpreted as reflecting the varying stages of the spermatogenic defect during meiosis. In general, early meiotic defects exhibited no LDH-C4 activity whereas late stage (usually after metaphase-1 stage) defect animals exhibited some activity. The results also provide evidence for contaminating sperm being the source of normal vesicular gland LDH-C4 activity.
Publisher: Wiley
Date: 08-1976
Abstract: Starch gel electrophoretic patterns of carbonic anhydrase (CA) isozymes were examined from tissue extracts of sheep, mice, rabbits, and chickens. In addition to the widely distributed and extensively studied B and C isozymes, an additional isozyme (called CA-A) was observed, which was predominantly localized in muscle tissue. Immunochemical studies showed the A isozyme to be homologous with CA-B. Developmental and tissue distribution analyses suggested that a third locus (A) is involved in carbonic anhydrase synthesis in mammals.
Publisher: Elsevier BV
Date: 1977
DOI: 10.1016/0020-711X(77)90089-1
Abstract: l. Antisera were prepared in rabbits against purified (>95%) rat L-alpha-hydroxyacid oxidase(HAOX) A(4), and B(4), isozymes and used in immunochemical titration and immunodiffusion experiments.2. Immunochemical homologies were demonstrated between mammalian HAOX isozymes.3. This provides further evidence that loci (Hao-1 Hao-2) encoding these isozymes are products of a recent gene duplication event.
Publisher: Springer Science and Business Media LLC
Date: 04-1978
DOI: 10.1007/BF00484076
Abstract: To elucidate the role of thyroid hormone receptors (TRs) alpha1 and beta in the development of hearing, cochlear functions have been investigated in mice lacking TRalpha1 or TRbeta. TRs are ligand-dependent transcription factors expressed in the developing organ of Corti, and loss of TRbeta is known to impair hearing in mice and in humans. Here, TRalpha1-deficient (TRalpha1(-/-)) mice are shown to display a normal auditory-evoked brainstem response, indicating that only TRbeta, and not TRalpha1, is essential for hearing. Because cochlear morphology was normal in TRbeta-/- mice, we postulated that TRbeta regulates functional rather than morphological development of the cochlea. At the onset of hearing, inner hair cells (IHCs) in wild-type mice express a fast-activating potassium conductance, IK,f, that transforms the immature IHC from a regenerative, spiking pacemaker to a high-frequency signal transmitter. Expression of IK,f was significantly retarded in TRbeta-/- mice, whereas the development of the endocochlear potential and other cochlear functions, including mechanoelectrical transduction in hair cells, progressed normally. TRalpha1(-/-) mice expressed IK,f normally, in accord with their normal auditory-evoked brainstem response. These results establish that the physiological differentiation of IHCs depends on a TRbeta-mediated pathway. When defective, this may contribute to deafness in congenital thyroid diseases.
Publisher: Springer Science and Business Media LLC
Date: 21-05-2009
DOI: 10.1007/S10528-009-9245-3
Abstract: Evidence is presented for six opossum ALDH1A genes, including four ALDH1A1-like genes on chromosome 6 and ALDH1A2- and ALDH1A3-like genes on chromosome 1. Predicted structures for the opossum aldehyde dehydrogenase (ALDH) subunits and the intron-exon boundaries for opossum ALDH genes showed a high degree of similarity with other mammalian ALDHs. Phylogenetic analyses supported the proposed designation of these opossum class 1 ALDHs as ALDH1A-like, ALDH1A2-like, and ALDH1A3-like and are therefore likely to play important roles in retinal and peroxidic aldehyde metabolism. Alignments of predicted opossum ALDH1A amino acid sequences with sheep ALDH1A1 and rat ALDH1A2 sequences demonstrated conservation of key residues previously shown to participate in catalysis and coenzyme binding. Amino acid substitution rates observed for family 1A ALDHs during vertebrate evolution indicated that ALDH1A2-like genes are evolving slower than ALDH1A1- and ALDH1A3-like genes. It is proposed that the common ancestor for ALDH1A genes predates the appearance of birds during vertebrate evolution.
Publisher: Springer Science and Business Media LLC
Date: 1983
DOI: 10.1007/BF00496638
Abstract: Gastrocolic fistulae have been described for benign conditions including penetrating peptic ulcer and complicated pancreatitis. Malignant etiology can arise from gastric or colon cancer and is a rare and late complication with an incidence of 0.3-0.4%. Usual presentation is the classic triad of weight loss, diarrhea, and feculent vomiting. Barium enema has been shown to have the highest diagnostic accuracy but endoscopy offers additional advantage of biopsy to aid in diagnosis of malignant etiology the role of computed tomography (CT) scan is controversial. Treatment by one-stage en bloc surgical approach is the current acceptable standard of care with variable recurrence and survival rates. Adjuvant chemotherapy would be based on lymph node involvement and patient discussion.
Publisher: Elsevier BV
Date: 1985
DOI: 10.1016/0741-8329(85)90018-7
Abstract: Aldehyde dehydrogenase (AHD) exists as isozymes which are differentially distributed among tissues and subcellular fractions of mouse tissues. Genetic variants for liver mitochondrial (AHD-1) and cytoplasmic (AHD-2) isozymes have been used to map the responsible loci (Ahd-1 and Ahd-2) on chromosomes 4 and 19 respectively. Evidence for a regulatory locus (Ahd-3r) controlling the inducibility of the mouse liver microsomal isozyme (AHD-3) has also been obtained. More recent studies have described genetic and biochemical evidence for three additional AHD isozymes: a stomach isozyme (AHD-4) another liver mitochondrial enzyme (AHD-5) and a testis isozyme (AHD-6). Genetic analyses have indicated that AHD-4 and AHD-6 are encoded by distinct but closely linked loci on the mouse genome (Ahd-4 and Ahd-6), which segregate independently of Ahd-1 and Ahd-2. Liver mitochondrial isozymes, AHD-1 and AHD-5, have been purified to homogeneity using affinity chromatography. The very high affinity of AHD-5 for acetaldehyde suggests that this enzyme is predominantly responsible for acetaldehyde oxidation in mouse liver mitochondria.
Publisher: Elsevier BV
Date: 1977
Publisher: Elsevier BV
Date: 12-1990
DOI: 10.1016/0006-2952(90)90582-6
Abstract: In a panel of 10 human tumour cell lines with no prior exposure to drugs in vitro, resistance to cisplatin correlated with resistance to the nitrogen mustard derivatives Asta Z-7557 (mafosfamide, an activated form of cyclophosphamide), melphalan and chlorambucil. Simultaneous treatment with DL-buthionine-S,R-sulfoximine did not enhance the toxicity of cisplatin or Asta Z-7557, and no correlation was found between drug resistance and cellular levels of metallothioneins (as judged by sensitivity to cadmium chloride), glutathione (GSH), GSH reductase, GSH transferase, or gamma-glutamyltranspeptidase. The two cell lines most resistant to Asta Z-7557 expressed aldehyde dehydrogenase cytosolic isozyme 1, found also in normal ovary, but not isozyme 3. Treatment of resistant cells with cisplatin or Asta Z-7557 inhibited cellular DNA synthesis and replication of adenovirus 5 to a lesser extent than in sensitive cells. The virus could be directly inactivated by both drugs prior to infection, subsequent replication being inhibited to the same extent in sensitive and resistant cells. In contrast to Asta Z-7557 and other DNA damaging agents, cisplatin was much more toxic to adenovirus (D37 0.022-0.048 microM) than to cells (D37 0.25-2.5 microM). The adenovirus 5 mutant Ad5ts125 having a G----A substitution was even more sensitive to cisplatin (D37 7-8 nM) than wild type virus and another mutant. Cisplatin was detoxified less by sonicated resistant resistant cells than sensitive cells, as judged by inactivation of Ad5ts125 added to the reaction mixture. It can be inferred that (i) the major differences in cellular resistance to cisplatin and Asta Z-7557 in the present material did not involve enhanced DNA repair or protection by metallothioneins or GSH, but were associated with the ability to continue cellular and viral DNA synthesis during treatment, (ii) resistance was not associated with less template damage, and (iii) the adenovirus genome may be a suitable probe for predicting tumour resistance to cisplatin and for elucidating the DNA sequence dependence of cisplatin toxicity.
Publisher: Springer Science and Business Media LLC
Date: 12-1984
DOI: 10.1007/BF00499626
Publisher: Springer Science and Business Media LLC
Date: 12-1982
DOI: 10.1007/BF00498933
Abstract: A fundamental challenge in neuroscience is to understand what structure in the world is represented in spatially distributed patterns of neural activity from multiple single-trial measurements. This is often accomplished by learning a simple, linear transformations between neural features and features of the sensory stimuli or motor task. While successful in some early sensory processing areas, linear mappings are unlikely to be ideal tools for elucidating nonlinear, hierarchical representations of higher-order brain areas during complex tasks, such as the production of speech by humans. Here, we apply deep networks to predict produced speech syllables from a dataset of high gamma cortical surface electric potentials recorded from human sensorimotor cortex. We find that deep networks had higher decoding prediction accuracy compared to baseline models. Having established that deep networks extract more task relevant information from neural data sets relative to linear models (i.e., higher predictive accuracy), we next sought to demonstrate their utility as a data analysis tool for neuroscience. We first show that deep network's confusions revealed hierarchical latent structure in the neural data, which recapitulated the underlying articulatory nature of speech motor control. We next broadened the frequency features beyond high-gamma and identified a novel high-gamma-to-beta coupling during speech production. Finally, we used deep networks to compare task-relevant information in different neural frequency bands, and found that the high-gamma band contains the vast majority of information relevant for the speech prediction task, with little-to-no additional contribution from lower-frequency litudes. Together, these results demonstrate the utility of deep networks as a data analysis tool for basic and applied neuroscience.
Publisher: Wiley
Date: 16-02-1970
Publisher: Elsevier BV
Date: 1982
Publisher: Wiley
Date: 1993
DOI: 10.1080/09595239300185781
Abstract: Mammalian alcohol dehydrogenases (ADHs) constitute an enzyme family of multiple forms (isozymes) which are differentially distributed throughout the body. Subunit types alpha, beta and gamma in dimeric combinations constitute the isozymes of human liver class I ADH, and are >94% homologous in structure. Human pi and chi subunits form homodimeric Class II and III ADH isozymes. pi-ADH is liver specific whereas chi-ADH is widely distributed throughout the body. A sixth human ADH subunit (designated mu or sigma), forming a new dimeric human stomach ADH, has been recently reported as Class IV ADH. Evidence for a seventh human ADH subunit has also been described, designated as Class V, the transcripts having been reported in the stomach and liver. All five classes of ADH represent isozymes which are homologous but exhibit at least 30% sequence differences in primary srtructure. Kinetic analyses of four of these classes of ADH indicated differential functions, serving either in the oxidative or reductive mode. Studies from various laboratories indicate the following respective functions: oxidation of aliphatic and aromatic alcohols-liver Class I and Class II, and stomach Class IV ADHs reduction of peroxidic aldehydes-Classes I, II and IV 'biogenic' alcohol oxidation-Classes I and II and glutathione-dependent formaldehyde dehydrogenase-Class III.
Publisher: Proceedings of the National Academy of Sciences
Date: 09-1969
Abstract: Lactate dehydrogenase is a tetrameric enzyme, generally composed of one or two kinds of subunits each encoded in a separate gene. Most vertebrates synthesize five major isozymic forms of lactate dehydrogenase, but the salmonid fish, particularly trout, synthesize many more. The numerous lactate dehydrogenase isozymes of trout can be selectively removed from tissue homogenates by suitably prepared antisera to specific lactate dehydrogenase subunits of fish. Electrophoretic resolution of such antisera-treated homogenates then permits an identification of each isozyme and a determination of its subunit composition and probable genetic basis. Such data indicate that trout are tetraploid organisms and have duplicate and slightly different loci for two and perhaps three of the lactate dehydrogenase loci found in other fish. The evolutionary relationships among the lactate dehydrogenase loci can also be assessed by these immunochemical data.
Publisher: Wiley
Date: 04-1973
Abstract: Biofilms are complex communities of microorganisms in organized structures attached to surfaces. Importantly, biofilms are a major cause of bacterial infections in humans, and remain one of the most significant challenges to modern medical practice. Unfortunately, conventional therapies have shown to be inadequate in the treatment of most chronic biofilm infections based on the extraordinary innate tolerance of biofilms to antibiotics. Antagonists of quorum sensing signaling molecules have been used as means to control biofilms. QS and other cell-cell communication molecules are able to revert biofilm tolerance, prevent biofilm formation and disrupt fully developed biofilms, albeit with restricted effectiveness. Recently however, it has been demonstrated that Pseudomonas aeruginosa produces a small messenger molecule cis-2-decenoic acid (cis-DA) that shows significant promise as an effective adjunctive to antimicrobial treatment of biofilms. This molecule is responsible for induction of the native biofilm dispersion response in a range of Gram-negative and Gram-positive bacteria and in yeast, and has been shown to reverse persistence, increase microbial metabolic activity and significantly enhance the cidal effects of conventional antimicrobial agents. In this manuscript, the use of cis-2-decenoic acid as a novel agent for biofilm control is discussed. Stimulating the biofilm dispersion response as a novel antimicrobial strategy holds significant promise for enhanced treatment of infections and in the prevention of biofilm formation.
Publisher: Elsevier BV
Date: 09-1986
DOI: 10.1016/S0014-4835(86)80075-6
Abstract: Isoelectric focusing (IEF) techniques and spectrophotometric analyses were used to examine the distribution and properties of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) isozymes in ocular tissue of olive and yellow baboons. Cornea extracts exhibited very high specific activities of the 'stomach-specific' ADH and ALDH isozymes (designated ADH-3 and ALDH-III respectively), and were devoid of the major liver and kidney isozymes. Lens extracts exhibited lower activities of ADH-3 and ALDH-III, and also showed significant activity of ALDH-II (the major liver cytosolic isozyme) and a group of 'lens-specific' ALDHs of low isoelectric point. Extracts of baboon retina also exhibited ADH-3 and ALDH-III activities, together with activities of the major liver cytosolic (ALDH-II) and mitochondrial (ALDH-I) isozymes of ALDH and ADH-5 (or chi-ADH) activity. Evidence was obtained for in idual variation of ALDH-III activity in the lens. An electrophoretic variant for ADH-3 indicated genetic identity of the major stomach and ocular ADH isozyme. The catalytic properties of the high specific activity corneal ADH and ALDH isozymes indicated a role in the detoxification of lipid peroxidation by-products.
Publisher: Wiley
Date: 10-1996
Publisher: Wiley
Date: 09-1977
Publisher: Elsevier BV
Date: 03-2009
DOI: 10.1016/J.CBI.2008.09.009
Abstract: BLAT (BLAST-Like Alignment Tool) analyses and interrogations of the recently published opossum genome were undertaken using previously reported rat ADH amino acid sequences. Evidence is presented for six opossum ADH genes localized on chromosome 5 and organized in a comparable ADH gene cluster to that reported for human and rat ADH genes. The predicted amino acid sequences and secondary structures for the opossum ADH subunits and the intron-exon boundaries for opossum ADH genes showed a high degree of similarity with other mammalian ADHs, and four opossum ADH classes were identified, namely ADH1, ADH3, ADH6 and ADH4 (for which three genes were observed: ADH4A, ADH4B and ADH4C). Previous biochemical analyses of opossum ADHs have reported the tissue distribution and properties for these enzymes: ADH1, the major liver enzyme ADH3, widely distributed in opossum tissues with similar kinetic properties to mammalian class 3 ADHs and ADH4, for which several forms were localized in extrahepatic tissues, especially in the digestive system and in the eye. These ADHs are likely to perform similar functions to those reported for other mammalian ADHs in the metabolism of ingested and endogenous alcohols and aldehydes. Phylogenetic analyses examined opossum, human, rat, chicken and cod ADHs, and supported the proposed designation of opossum ADHs as class I (ADH1), class III (ADH3), class IV (ADH4A, ADH4B and ADH4C) and class VI (ADH6). Percentage substitution rates were examined for ADHs during vertebrate evolution which indicated that ADH3 is evolving at a much slower rate to that of the other ADH classes.
Publisher: Elsevier BV
Date: 09-2009
Publisher: Elsevier BV
Date: 1965
Publisher: Wiley
Date: 05-1969
Abstract: The determinants of cognitive deficits among in iduals with Klinefelter syndrome (KS) are not well understood. This study was conducted to assess the impact of general intelligence, personality, and social engagement on cognitive performance among patients with KS and a group of controls matched for age and years of education. Sixty-nine patients with KS and 69 controls were assessed in terms of IQ, NEO personality inventory, the Autism Spectrum Quotient (AQ) scale, and measures of cognitive performance reflecting working memory and executive function. Patients with KS performed more poorly on memory and executive-function tasks. Patients with KS also exhibited greater neuroticism and less extraversion, openness, and conscientiousness than controls. Memory deficits among patients with KS were associated with lower intelligence, while diminished executive functioning was mediated by both lower intelligence and less social engagement. Our results suggest that among patients with KS, memory deficits are principally a function of lower general intelligence, while executive-function deficits are associated with both lower intelligence and poorer social skills. This suggests a potential influence of social engagement on executive cognitive functioning (and/or vice-versa) among in iduals with KS, and perhaps those with other genetic disorders. Future longitudinal research would be important to further clarify this and other issues discussed in this research.
Publisher: Elsevier BV
Date: 06-2017
DOI: 10.1016/J.COMPBIOLCHEM.2017.02.009
Abstract: At least 19 sulfatase genes have been reported on the human genome, including four arylsulfatase (ARS) genes (ARSD ARSE ARSF ARSH) and a sterylsulfatase (STS) gene located together on the X-chromosome. Bioinformatic analyses of mammalian genomes were undertaken using known human STS and ARS amino acid sequences to study the evolution of these genes and proteins encoded on eutherian and marsupial genomes. Several domain regions and key residues were conserved including signal peptides, active site residues, metal (Ca
Publisher: Elsevier BV
Date: 09-1967
DOI: 10.1016/0005-2744(67)90080-0
Abstract: Research indicates that older adults receive only about half of their recommended care, with varying quality and limited attention to social issues impacting their health through the most commonly used quality measures. Additionally, many existing measures neglect to address nonclinical social determinants of health. Evidence of the need for more comprehensive measures for seniors is growing. The primary purpose of this article, which is supported by a limited review of literature, is to describe gaps among current quality measures in addressing certain nonclinical needs of older adults, including key social determinants of health. In doing so, the authors describe their position on the need for expanded measures to incorporate these factors to improve care and quality of life. The authors conducted a limited review of the literature to inform this article, focusing specifically on selected measures for older adults rather than a broader systematic review of all measures. Most research identified was related to clinical practice guidelines rather than quality measures of care as applied to older adults. Furthermore, the literature reviewed reflected limited evidence of efforts to tailor quality measures for the unique social needs of older adults, confirming a potential gap in this area. A growing need exists for improved quality measures specifically designed to help providers address the unique social needs of older adults. Filling this gap will improve overall understanding of seniors and help them to achieve optimal health and successful aging.
Publisher: Elsevier BV
Date: 10-2009
Publisher: Wiley
Date: 05-1985
DOI: 10.1111/J.1530-0277.1985.TB05747.X
Abstract: Isoelectric focusing and electrophoresis were used to identify the various isozymes of alcohol dehydrogenase (ADH), aldehyde dehydrogenase (ALDH), aldehyde oxidase (AOX), and xanthine oxidase (XOX). ADH types I, II, and III were located primarily in the cytosol fraction of liver, but some activity was found also in the small granule fraction. The ALDH-I and -IV isozymes were found in the large granule fraction, while ALDH-II and -III were present in the cytosol and ALDH-V in the small granule fraction. AOX and XOX each appeared as a single cytosolic form with some small granule activity. The tissue distribution of these isozymes is presented and the physiological role of each enzyme is discussed.
Publisher: Hindawi Limited
Date: 21-11-2011
DOI: 10.1155/2011/781643
Abstract: Bile-salt activated carboxylic ester lipase (CEL) is a major triglyceride, cholesterol ester and vitamin ester hydrolytic enzyme contained within pancreatic and lactating mammary gland secretions. Bioinformatic methods were used to predict the amino acid sequences, secondary and tertiary structures and gene locations for CEL genes, and encoded proteins using data from several vertebrate genome projects. A proline-rich and O-glycosylated 11-amino acid C-terminal repeat sequence (VNTR) previously reported for human and other higher primate CEL proteins was also observed for other eutherian mammalian CEL sequences examined. In contrast, opossum CEL contained a single C-terminal copy of this sequence whereas CEL proteins from platypus, chicken, lizard, frog and several fish species lacked the VNTR sequence. Vertebrate CEL genes contained 11 coding exons. Evidence is presented for tandem duplicated CEL genes for the zebrafish genome. Vertebrate CEL protein subunits shared 53–97% sequence identities demonstrated sequence alignments and identities for key CEL amino acid residues and conservation of predicted secondary and tertiary structures with those previously reported for human CEL. Phylogenetic analyses demonstrated the relationships and potential evolutionary origins of the vertebrate CEL family of genes which were related to a nematode carboxylesterase ( CES ) gene and five mammalian CES gene families.
Publisher: Japanese Association for Laboratory Animal Science
Date: 1986
DOI: 10.1538/EXPANIM1978.35.3_263
Abstract: In order to establish the genetic relatedness of the inbred mouse strains kept in Nara, genetic marker patterns were determined in conjunction with a study on endogenous mammary tumor viral genes in these strains. Isoenzyme patterns combined with patterns of other genetic markers, show that the unrelatedness between various inbred strains of the dd stock is as high or even higher as between strains of known different origin and geneology. Based on endogenous viral gene patterns the dd stock derived mice can be sub ided into three group, DDD, DDN, DDO, KF and DD/Tbr. The DD/Tbr and its foster-nursed substrain (DD/Tbrf) have the lowest number of endogenous viral genes, i.e. two, while the other strains carry 4-6 such genes. The SLN and SHN strains, derived from a Swiss stock, have a similar pattern of viral genes different that of all other strains studied, also strains of Swiss origin from other sources, such as the NFS and the GR.
Publisher: CSIRO Publishing
Date: 1974
DOI: 10.1071/BI9740677
Abstract: A genetic polymorphism for the soluble isozyme (MDH-A2) of malate dehydrogenase (L-malate : NAD+ oxidoreductase EC 1.1.1.37) was found in a Townsville-Inkerman population of short-nosed bandicoots, 1. macrourus. The enzyme seems to be inherited in a normal autosomal codominant manner. The gene frequencies for the MDH-A and MDH-A' alleles were O' 82 and 0�18 respectively. The genotypic frequencies indicated that the population was in Hardy-Weinberg equilibrium. None of 22 pouch young from seven litters expressed a phenotype inconsistent with its mother's genotype, assuming autosomal co dominance. Other populations of I. macrourus and of the long-nosed bandicoot (Perameles nasuta) exhibited only the MDH-A allele. Homologous relationships of bandicoot MDH-A2 and MDH-B2 isozymes to those of other vertebrates were established by immunochemical studies.
Publisher: Springer Science and Business Media LLC
Date: 12-1978
DOI: 10.1038/HDY.1978.111
Abstract: Electrophoretic variants of in idual isozymes of L-alpha-hydroxyacid oxidase (HAOX-B4) and amylase (AMY-A) in an Asian subspecies of mouse, Mus musculus castaneus, have been used to localise the gene encoding the HAOX B subunit. The structural gene loci for these isozymes (Hao-2 and Amy-1) are apparently linked (4.9 +/- 2.4 per cent recombinants) in this organism, which places Hao-2 on linkage group XVI, since previous studies by Eicher and co-workers (1976) have localised Amy-1 on this chromosome.
Publisher: Wiley
Date: 10-1992
DOI: 10.1111/J.1530-0277.1992.TB01894.X
Abstract: The major isozyme of alcohol dehydrogenase in baboon stomach, ADH3, has been purified to homogeneity and characterized with a range of alcohol and aldehyde substrates. Using kcat/Km values as an indication of substrate efficacy, medium-chain length aliphatic alcohols and aldehydes were identified as the preferred substrates. ADH3 showed 'high-Km' properties with respect to ethanol, and is expected to significantly contribute to 'first-pass' metabolism of alcohol. The enzyme exhibited more than two orders of magnitude higher turnover of substrate than the baboon liver 'low-Km' ADH, and may play a role in the rapid metabolism of a wide range of ingested alcohols in the diet.
Publisher: Springer Science and Business Media LLC
Date: 04-1991
DOI: 10.1007/BF02401810
Publisher: Wiley
Date: 11-1985
DOI: 10.1111/J.1530-0277.1985.TB05599.X
Abstract: The distribution of genetic variants (or gene markers) for alcohol dehydrogenase, aldehyde dehydrogenase, aldehyde oxidase, and aldehyde reductase isozymes has been examined among 12 inbred strains of mice. Electrophoretic variants are described for the major liver and stomach alcohol dehydrogenase isozymes (ADH-A2 and C2) liver, kidney, and stomach aldehyde dehydrogenase isozymes (AHD-1 AHD-2 AHD-4) a liver-specific aldehyde reductase (AHR-A2) and a liver aldehyde oxidase isozyme (AOX-2). Genetically determined activity variants were observed for a testis-specific aldehyde dehydrogenase (AHD-6) liver and kidney aldehyde reductase isozymes (AHR-3 and AHR-4) and the major liver AOX isozyme (AOX-1). These variants may serve as useful gene markers in alcohol research involving animal model studies with inbred strains in mice.
Publisher: Elsevier BV
Date: 09-1987
DOI: 10.1016/0047-6374(87)90010-8
Abstract: The postnatal development of aldehyde dehydrogenase (AHD) isozymes from C57BL/6J mouse tissues was examined using agarose-IEF zymogram methods. Mitochondrial isozymes (AHD-1 and AHD-5) were present throughout, increasing to high levels in liver, kidney and stomach by weaning (3 weeks). These activities remained high subsequently, except for kidney AHD-5, which decreased significantly after week 4. The appearance of the cytosolic isozymes was tissue specific and time dependent: liver AHD-2 was undetected until day 21, and increased subsequently stomach AHD-4 was first observed at day 5, increasing to adult levels by day 21 AHD-6 was active in neonatal kidney and stomach extracts, but was undetected after day 8 and AHD-7 was observed in liver and kidney extracts from day 16. These results supported previous proposals for multiple genes encoding aldehyde dehydrogenases in the mouse, based upon the distinct developmental profiles for the liver, kidney and stomach isozymes.
Publisher: Elsevier BV
Date: 1985
DOI: 10.1016/0020-711X(85)90142-9
Abstract: Using the reverse 13C----1H DEPT polarization-transfer pulse sequence the metabolism of 13C ethanol in vitro and in vivo has been monitored by 1H-NMR spectroscopy. Using yeast alcohol dehydrogenase, acetaldehyde, the hydrated form of acetaldehyde and acetate were identified as metabolites of [2-13C]-ethanol. The ratio of hydrated to free acetaldehyde was dependent upon the protein concentration of the reaction mixture. Binding of acetaldehyde in an irreversible Schiffs base resulted in optimal enzyme activity. Hepatocytes from rats fasted for 20 h, metabolised [1-13C] and [2-13C]ethanol in a linear fashion, but no [13C]acetaldehyde was detected. Metabolic integrity of the hepatocytes was confirmed with [2-13C]acetate. The addition of disulfiram (50 micron) to hepatocyte suspensions which had been incubated with [1-13C]ethanol, resulted in the resynthesis of [13C]ethanol. The amount of [13C]ethanol resynthesized under these conditions represents intracellular acetaldehyde whose concentration was in the range of 400-800 mumol/g wet weight of hepatocytes when 50 mM ethanol had been originally incubated with the hepatocyte suspension. These studies show how NMR-polarization transfer pulse sequences can be used to monitor the metabolism of 13C-ethanol in vivo, and provide a unique tool to measure in vivo concentrations of acetaldehyde. The studies also suggest that cytoplasmic aldehyde dehydrogenase may play a major role in hepatic ethanol metabolism.
Publisher: Elsevier BV
Date: 08-1999
DOI: 10.1016/S0006-2952(99)00065-9
Abstract: The alcohol dehydrogenase (ADH) gene family encodes enzymes that metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. Studies on 19 vertebrate animals have identified ADH orthologs across several species, and this has now led to questions of how best to name ADH proteins and genes. Seven distinct classes of vertebrate ADH encoded by non-orthologous genes have been defined based upon sequence homology as well as unique catalytic properties or gene expression patterns. Each class of vertebrate ADH shares 80% sequence identity such as the case for class I ADH where humans have three class I ADH genes, horses have two, and mice have only one. Presented here is a nomenclature that uses the widely accepted vertebrate ADH class system as its basis. It follows the guidelines of human and mouse gene nomenclature committees, which recommend coordinating names across species boundaries and eliminating Roman numerals and Greek symbols. We recommend that enzyme subunits be referred to by the symbol "ADH" (alcohol dehydrogenase) followed by an Arabic number denoting the class i.e. ADH1 for class I ADH. For genes we recommend the italicized root symbol "ADH" for human and "Adh" for mouse, followed by the appropriate Arabic number for the class i.e. ADH1 or Adh1 for class I ADH genes. For organisms where multiple species-specific isoenzymes exist within a class, we recommend adding a capital letter after the Arabic number i.e. ADH1A, ADH1B, and ADH1C for human alpha, beta, and gamma class I ADHs, respectively. This nomenclature will accommodate newly discovered members of the vertebrate ADH family, and will facilitate functional and evolutionary studies.
Publisher: Elsevier BV
Date: 04-1985
DOI: 10.1016/0006-2952(85)90617-3
Abstract: 2-beta-D-Ribofuranosyl-4-selenazolecarboxamide (selenazofurin, CI-935), the selenium analog of tiazofurin (CI-909), was 3- to 10-fold more cytotoxic to murine or human tumor cells in vitro than tiazofurin and was also more active against P388 mouse leukemia in vivo. In vitro cytotoxicity could be reversed by guanosine or guanine but not by other purine nucleosides or bases. Three human tumor cell lines selected for selenazofurin or tiazofurin resistance showed cross resistance between selenazofurin and tiazofurin. Treatment with tiazofurin, selenazofurin, or mycophenolic acid decreased guanylate pools and caused an accumulation of IMP in WIL2 human lymphoma cells. The decrease in guanylate pools was accompanied by inhibition of RNA and DNA synthesis. The NAD analogs of tiazofurin and selenazofurin were inhibitors of L1210 IMP dehydrogenase (IMP:NAD oxidoreductase, EC 1.2.1.14), and both showed uncompetitive inhibition with respect to NAD having Kii values of 5.7 X 10(-8)M and 3.3 X 10(-8)M respectively.
Publisher: Elsevier BV
Date: 09-1968
Publisher: Hindawi Limited
Date: 12-1981
DOI: 10.1017/S0016672300020668
Abstract: Mouse mutant genes which result in defects similar to those of medical importance in man may be of value as models for the study of the defect concerned. We report here a new gene causing congenital cataract in the mouse, which may be useful in the understanding of cataract in man. A further point of interest is that Kratochvilova & Ehling (1979) have recently developed a new method of measuring increased mutation rates in the mouse, by examining offspring of animals treated with mutagens for the presence of cataracts due to mutant genes. For the purposes of this test it is valuable to have information on the number and map position of loci which can mutate to give cataracts.
Publisher: Elsevier BV
Date: 1986
DOI: 10.1016/0020-711X(86)90007-8
Abstract: Liver cytosolic aldehyde dehydrogenases (AHD-2) have been isolated in a highly purified state from "alcohol-drinking" (C57BL/6J) and "alcohol-avoiding" (DBA/2J) strains of mice. The purified enzymes were resolved into three major and one minor form of activity by isoelectric focusing (IEF) techniques and showed similar zymogram patterns. The enzymes had identical subunit sizes on SDS-polyacrylamide gels: 53,000. Gel exclusion chromatography, using Ultrogel AcA34, indicated that the enzymes were dimers. The enzymes exhibited biphasic kinetic characteristics and were readily distinguished from each other. The purified forms of AHD-2 from C57BL/6J and DBA/2J mice exhibited two apparent Km values in each case: 10 microM/100 microM and 30 microM/330 microM respectively. AHD-2 exhibited a broad pH optimum in the range 7.0-9.0 and was very sensitive towards disulphuram inhibition, with 50% inhibition occurring at 0.17 microM. The kinetic results support proposals that AHD-2 may be the primary enzyme for oxidizing acetaldehyde during ethanol oxidation in vivo.
Publisher: Elsevier BV
Date: 1978
DOI: 10.1016/0305-0491(78)90134-7
Abstract: 1. Cellulose acetate zymograms of alcohol dehydrogenase (ADH), aldehyde dehydrogenase, sorbitol dehydrogenase, aldehyde oxidase, "phenazine" oxidase and xanthine oxidase extracted from tissues of inbred mice were examined. 2. ADH isozymes were differentially distributed in mouse tissues: A2--liver, kidney, adrenals and intestine B2--all tissues examined C2--stomach, adrenals, epididymis, ovary, uterus, lung. 3. Two NAD+-specific aldehyde dehydrogenase isozymes were observed in liver and kidney and differentially distributed in other tissues. Alcohol dehydrogenase, aldehyde oxidase, "phenazine" oxidase and xanthine oxidase were also stained when aldehyde dehydrogenase was being examined. 4. Two aldehyde oxidase isozymes exhibited highest activities in liver. 5. "Phenazine oxidase" was widely distributed in mouse tissues whereas xanthine oxidase exhibited highest activity in intestine and liver extracts. 6. Genetic variants for ADH-C2 established its identity with a second form of sorbitol dehydrogenase observed in stomach and other tissues. The major sorbitol dehydrogenase was found in high activity in liver, kidney, pancreas and male reproductive tissues.
Publisher: Springer Science and Business Media LLC
Date: 28-04-2010
Publisher: Wiley
Date: 15-11-1972
DOI: 10.1016/0014-5793(72)80675-6
Abstract: Salacia oblonga, an inhabitant of tropical regions has been used in traditional Indian medicinal systems. Phytochemicals were extracted in methanol from the plant and analyzed for various biological activities. The results of biochemical tests for total phenolics (297 ± 0.005 and 275 ± 0.006) and flavonoids (95 ± 0.004 and 61.6 ± 0.004) in the aerial and root parts were indicated as Gallic acid and quercetin equivalents respectively. The Aerial and root extracts showed strong reducing ability based on reducing power and FRAP assays. The extracts exhibited significant IC50 values in DPPH, super oxide and nitric oxide radical scavenging assays. The extracts displayed low IC50 values (<50 μg/ml) when assessed for antiproliferative activity against breast cancer cell lines using the MTT assay. GC-MS analysis of methanolic extracts have revealed the presence of compounds viz. n-Hexadecanoic acid, N-Methoxy-N-methylacetamide, Ursa-9(11), 12-dien-3-ol, Gamma-sitosterol etc., that might be potential candidates for the biological activity exhibited by the extract.
Publisher: Wiley
Date: 09-11-1970
Publisher: Wiley
Date: 04-1976
Publisher: Ovid Technologies (Wolters Kluwer Health)
Date: 11-1992
DOI: 10.1097/00003226-199211000-00013
Abstract: The regional distribution of mouse aldehyde dehydrogenase (ALDH) and alcohol dehydrogenase activities in mouse ocular tissues was examined using spectrophotometric and agarose-isoelectric focusing techniques. The results established that these enzymes are predominantly localized in the cornea. Biochemical and histochemical analyses of the localization of these enzymes in the corneas of common domestic mammals (pigs, sheep, and cattle) and in baboons revealed species differences, with high levels being reported in corneal epithelium (pigs and baboons) and endothelium (sheep and cattle). The presence of these enzymes in the corneal epithelium is consistent with their proposed catalytic role in the detoxification of ultraviolet (UV)-induced peroxidic aldehydes, and with the proposed role for corneal ALDH in UVB absorption.
Publisher: Elsevier BV
Date: 03-2009
Publisher: Elsevier BV
Date: 10-2017
DOI: 10.1016/J.CBI.2016.12.012
Abstract: Vertebrate ALDH18A1 genes encode a bifunctional mitochondrial enzyme, catalyzing a 2-step conversion of glutamate to glutamyl semialdehyde, subsequently converted into proline, ornithine and arginine. Bioinformatic analyses of vertebrate and invertebrate genomes were undertaken using known ALDH18A1 amino acid sequences. G5K (glutamyl kinase) and GPR (glutamyl phosphate reductase) domain sequences were identified for all vertebrate and invertebrate genomes examined, whereas bacterial sequences encoded separate enzymes. Vertebrate ALDH18A1 (also called P5CS) sequences were highly conserved throughout vertebrate evolution. A mechanism for generating two major vertebrate ALDH18A1 isoforms is proposed with 'a' isoform containing Asn239-Val240 with wide tissue expression, whereas the 'b' isoform lacking the dipeptide has been reported in gut tissues. Phylogenetic analyses describe the relationships and potential origins of the ALDH18A1 gene during vertebrate and invertebrate evolution and a proposal for generating the bifunctional vertebrate and invertebrate ALDH18A1 gene from a bacterial operon (proBA) encoding G5K and GPR. A more recent Aldh18a1 gene duplication event has apparently occurred with a primordial rat genome.
Publisher: Elsevier BV
Date: 11-1975
Publisher: Springer Science and Business Media LLC
Date: 06-1979
DOI: 10.1007/BF00498884
Publisher: Wiley
Date: 06-1988
DOI: 10.1111/J.1365-2052.1988.TB00811.X
Abstract: Isoelectric focusing (IEF) and histochemical techniques were used to examine the genetics, postnatal development and biochemical properties of ocular oxidases (EOXs) among inbred strains of mice. The designation as EOX was made on a provisional basis, since the 'natural' substrate(s) for this enzyme have not been identified. Five major forms were resolved from adult animals, which exhibited high activity in murine lens and low activity in the cornea. An additional ocular oxidase was observed in neonatal animals. Genetic analyses demonstrated that one of these enzymes (EOX-1) is encoded by a locus (Eox-1) which is closely linked with, but distinct from, the aldehyde oxidase (Aox) gene complex on chromosome one of the mouse. These results support the proposal that ocular oxidases are distinct from the major liver AOXs in this organism.
Publisher: Wiley
Date: 08-1981
Abstract: Electrophoretic variants for the stomach isozyme (ADH-C2) and liver isozyme (ADH-A2) of alcohol dehydrogenase in strains of Mus musculus have been used in genetic analyses to demonstrate close linkage between the structural genes (Ahd-3 and Adh-1, respectively) encoding these enzymes. No recombinants were observed between these loci among 126 backcross animals, which places them less than 0.8 centimorgans apart. Previous studies have positioned Adh-3, and a temporal locus (ADh-3t), on chromosome 3 (Holmes, "79 Holmes et al., "80). Kinetic analyses on partially purified preparations of these isozymes have demonstrated widely ergent catalytic properties and inhibitor specificities. The liver isozyme exhibited Michaelis constants that were nearly 3 orders of magnitude lower than the stomach isozyme for various alcohol and aldehyde substrates. Moreover, aminopropyl pyrazole strongly inhibited ADH-A2 (Ki=1.2M), whereas ADH-C2 was insensitive to inhibition under the conditions used. It is proposed that Adh-1 and Adh-3 are products of a recent gene duplication event during mammalian evolution and that considerable ergence in the active sites of these enzymes and the "temporal" genes controlling loci expression in differentiated tissues has subsequently occurred.
Publisher: Wiley
Date: 1979
Abstract: Lactate dehydrogenase (LDH) C4 activity was observed in testis extracts of sex-reversed mice (Sxr) and in male sex accessory gland (seminal vesicle and prostate) extracts from C3H/He and C57BL/Go mice. These results reflect either (1) the presence of low concentrations of germinal cells in these tissues or (2) the synthesis of LDH-C4 by somatic cells in Sxr testes and normal male sex accessory glands.
Publisher: Wiley
Date: 04-1981
DOI: 10.1111/J.1445-5994.1981.TB04221.X
Abstract: Alcohol dehydrogenase (ADH) of mouse tissues was investigated using electrophoretic zymogram methods. ADH activity is widely distributed in mouse tissues and exists as at least two genetic isozymes, designated A2 and C2, which are predominantly localised in liver and stomach respectively. Electrophoretic and activity variants of ADH-C2 among inbred strains of mice have been used to localise the gene encoding this enzyme (Adh-3) and a closely linked temporal locus (Adh-3-t) on chromosome 3 of this organism. Recent developmental studies on ADH isozymes in the mouse have been reviewed.
Publisher: Ovid Technologies (Wolters Kluwer Health)
Date: 05-1993
DOI: 10.1097/00003226-199305000-00010
Abstract: Adult male C57BL/6J inbred mice were subjected to ultraviolet radiation (UVR) exposure (302-nm peak wavelength average intensity 282 microW/cm2) for 1 h and monitored for ocular aldehyde dehydrogenase (ALDH) and alcohol dehydrogenase (ADH) activity changes over a period of 25 days. Dramatic reductions in activities were observed by 4-6 days postexposure, resulting in enzyme levels of 15-16% of control animals. Major decreases in corneal enzyme levels were predominantly responsible for these changes. Ocular morphology was observed throughout using a photoslit-l biomicroscope, with maximum corneal clouding occurring at days 4-6. These data support earlier proposals for major roles for these corneal enzymes in assisting the cornea in protecting the eye against UVR-induced tissue damage.
No related grants have been discovered for Roger Holmes.