ORCID Profile
0000-0002-3968-1419
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Publisher: American Society for Pharmacology & Experimental Therapeutics (ASPET)
Date: 29-07-2016
Abstract: Aquaporin-1 (AQP1) is a major intrinsic protein that facilitates flux of water and other small solutes across cell membranes. In addition to its function as a water channel in maintaining fluid homeostasis, AQP1 also acts as a nonselective cation channel gated by cGMP, a property shown previously to facilitate rapid cell migration in a AQP1-expressing colon cancer cell line. Here we report two new modulators of AQP1 channels, bacopaside I and bacopaside II, isolated from the medicinal plant Bacopa monnieri Screening was conducted in the Xenopus oocyte expression system, using quantitative swelling and two-electrode voltage cl techniques. Results showed bacopaside I blocked both the water (IC50 117 μM) and ion channel activities of AQP1 but did not alter AQP4 activity, whereas bacopaside II selectively blocked the AQP1 water channel (IC50 18 μM) without impairing the ionic conductance. These results fit with predictions from in silico molecular modeling. Both bacopasides were tested in migration assays using HT29 and SW480 colon cancer cell lines, with high and low levels of AQP1 expression, respectively. Bacopaside I (IC50 48 μM) and bacopaside II (IC50 14 μM) impaired migration of HT29 cells but had minimal effect on SW480 cell migration. Our results are the first to identify differential AQP1 modulators isolated from a medicinal plant. Bacopasides could serve as novel lead compounds for pharmaceutic development of selective aquaporin modulators.
Publisher: American Society for Pharmacology & Experimental Therapeutics (ASPET)
Date: 14-10-2015
Publisher: Wiley
Date: 11-01-2018
Abstract: Aquaporin (AQP) channels in the major intrinsic protein (MIP) family are known to facilitate transmembrane water fluxes in prokaryotes and eukaryotes. Some classes of AQPs also conduct ions, glycerol, urea, CO
Publisher: Wiley
Date: 18-10-2016
DOI: 10.1111/PCE.12832
Abstract: The aquaporin AtPIP2 is an abundant plasma membrane intrinsic protein in Arabidopsis thaliana that is implicated in stomatal closure, and is highly expressed in plasma membranes of root epidermal cells. When expressed in Xenopus laevis oocytes, AtPIP2 increased water permeability and induced a non-selective cation conductance mainly associated with Na
Publisher: MDPI AG
Date: 03-11-2017
DOI: 10.3390/IJMS18112323
Publisher: American Society for Pharmacology & Experimental Therapeutics (ASPET)
Date: 11-03-2019
Abstract: This is the first work to use a newly designed Li
Publisher: Frontiers Media SA
Date: 27-04-2018
No related grants have been discovered for Mohamad Kourghi.