ORCID Profile
0000-0001-9521-5124
Current Organisation
Southern University of Science and Technology
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Publisher: American Chemical Society (ACS)
Date: 26-01-2023
Publisher: Elsevier BV
Date: 10-2012
DOI: 10.1016/J.CELL.2012.08.037
Abstract: Vascular endothelial growth factor and its receptors, FLK1/KDR and FLT1, are key regulators of angiogenesis. Unlike FLK1/KDR, the role of FLT1 has remained elusive. FLT1 is produced as soluble (sFLT1) and full-length isoforms. Here, we show that pericytes from multiple tissues produce sFLT1. To define the biologic role of sFLT1, we chose the glomerular microvasculature as a model system. Deletion of Flt1 from specialized glomerular pericytes, known as podocytes, causes reorganization of their cytoskeleton with massive proteinuria and kidney failure, characteristic features of nephrotic syndrome in humans. The kinase-deficient allele of Flt1 rescues this phenotype, demonstrating dispensability of the full-length isoform. Using cell imaging, proteomics, and lipidomics, we show that sFLT1 binds to the glycosphingolipid GM3 in lipid rafts on the surface of podocytes, promoting adhesion and rapid actin reorganization. sFLT1 also regulates pericyte function in vessels outside of the kidney. Our findings demonstrate an autocrine function for sFLT1 to control pericyte behavior.
Publisher: Elsevier BV
Date: 05-2017
DOI: 10.1016/J.CHROMA.2017.01.033
Abstract: Multidimensional peptide fractionation strategies have been approved as the efficient approaches to significantly improve the depth of proteome coverage. In this study, a simple and integrated spintip-based protein digestion and three-dimensional peptide fractionation technology (3D-SISPROT) was developed for the deep proteome profiling from low microgram of proteins as starting materials. All the s le preparation steps, including protein digestion, strong anion exchange (SAX)-based fractionation, and high-pH reversed phase (RP) fractionation were integrated into one pipette tip packed with SAX and C
Publisher: American Chemical Society (ACS)
Date: 20-04-2016
DOI: 10.1021/ACS.ANALCHEM.6B00631
Abstract: Great efforts have been taken for developing high-sensitive mass spectrometry (MS)-based proteomic technologies, among which s le preparation is one of the major focus. Here, a simple and integrated spintip-based proteomics technology (SISPROT) consisting of strong cation exchange beads and C18 disk in one pipet tip was developed. Both proteomics s le preparation steps, including protein preconcentration, reduction, alkylation, and digestion, and reversed phase (RP)-based desalting and high-pH RP-based peptide fractionation can be achieved in a fully integrated manner for the first time. This easy-to-use technology achieved high sensitivity with negligible s le loss. Proteomic analysis of 2000 HEK 293 cells readily identified 1270 proteins within 1.4 h of MS time, while 7826 proteins were identified when 100000 cells were processed and analyzed within only 22 h of MS time. More importantly, the SISPROT can be easily multiplexed on a standard centrifuge with good reproducibility (Pearson correlation coefficient > 0.98) for both single-shot analysis and deep proteome profiling with five-step high-pH RP fractionation. The SISPROT was exemplified by the triplicate analysis of 100000 stem cells from human exfoliated deciduous teeth (SHED). This led to the identification of 9078 proteins containing 3771 annotated membrane proteins, which was the largest proteome data set for dental stem cells reported to date. We expect that the SISPROT will be well suited for deep proteome profiling for fewer than 100000 cells and applied for translational studies where multiplexed technology with good label-free quantification precision is required.
Publisher: Springer New York
Date: 2017
DOI: 10.1007/978-1-4939-7262-3_4
Abstract: Cell microenvironment consists of various types of cells which communicate with each other by vast number of secreted proteins. An unbiased profiling of these secreted proteins on a global scale is often critical for understanding the intercellular signaling in an autocrine or paracrine manner. Mass spectrometry-based proteomics has become one of the most popular technology for characterization of the secreted proteins. In this chapter, we discuss the standard workflow for secreted proteins characterization, including harvesting secreted proteins from conditioned media, digesting the obtained proteins, liquid chromatography-mass spectrometry analysis, and downstream data analysis.
No related grants have been discovered for Ruijun Tian.