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Proteomic study of human umbilical vein endothelial cells in culture

Arnaud Bruneel, Valérie Labas, Agnès Mailloux, Sanjiv Sharma Orcid Logo, Joelle Vinh, Michel Vaubourdolle, Bruno Baudin

PROTEOMICS, Volume: 3, Issue: 5, Pages: 714 - 723

Swansea University Author: Sanjiv Sharma Orcid Logo

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DOI (Published version): 10.1002/pmic.200300409

Abstract

The endothelium is a single layer of cells lining the inside face of all blood vessels. It constitutes a major metabolic organ which is critically involved in the generation and the regulation of multiple physiological and pathological processes such as coagulation, hemostasis, inflammation, atheros...

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Published in: PROTEOMICS
ISSN: 1615-9853 1615-9861
Published: 2003
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URI: https://cronfa.swan.ac.uk/Record/cronfa36261
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last_indexed 2018-02-09T05:28:20Z
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spelling 2017-10-26T09:25:26.5257194 v2 36261 2017-10-25 Proteomic study of human umbilical vein endothelial cells in culture b6b7506358522f607b171ec9c94757b7 0000-0003-3828-737X Sanjiv Sharma Sanjiv Sharma true false 2017-10-25 MEDE The endothelium is a single layer of cells lining the inside face of all blood vessels. It constitutes a major metabolic organ which is critically involved in the generation and the regulation of multiple physiological and pathological processes such as coagulation, hemostasis, inflammation, atherosclerosis, angiogenesis and cancerous metastasis dissemination. In order to increase our knowledge about the protein content and the main biological pathways of human vascular endothelial cells, we have undertaken the proteomic analysis of the most explored present endothelial cell model, i.e. primocultures of human umbilical vein endothelial cells (HUVECs). Using low levels of protein loads (&#126; 30 νg), the association of two-dimensional electrophoresis with matrix-assisted laser desorption/ionization-time of flight mass spectrometry, liquid chromatography-tandem mass spectrometry and database interrogations allowed us to identify 53 proteins of suspected endothelial origin in quiescent HUVECs. Beside cytoskeletal proteins such as actin, tubulin, tropomyosin and vimentin, we identified various proteins more especially implicated in cellular motility and plasticity (e.g. cofilin, F-actin capping protein and prefoldin), in regulation of apoptosis and senescence (protease inhibitor 9, glucose related proteins, heat shock proteins, thioredoxin peroxidase, nucleophosmin) as well as other proteins implicated in coagulation (annexin V, high mobility group protein), antigen presentation (valosin containing protein and ubiquitin carboxyl terminal hydrolase isozyme L1) and enzymatic capabilities (glutathione-S-transferase, protein disulfide isomerases, lactate deshydrogenase). The presented annotated 2-D maps of HUVECs will be soon available on the web at http://www. huvec.com. Journal Article PROTEOMICS 3 5 714 723 1615-9853 1615-9861 Endothelium; Human umbilical vein endotheial cells; Liquid chromatography-tandem mass spectrometry; Matrix-assisted laser desorption; ionization-time of flight; Proteome; Two-dimensional gel electrophoresis 31 5 2003 2003-05-31 10.1002/pmic.200300409 COLLEGE NANME Biomedical Engineering COLLEGE CODE MEDE Swansea University 2017-10-26T09:25:26.5257194 2017-10-25T14:06:30.5414403 Faculty of Science and Engineering School of Engineering and Applied Sciences - Biomedical Engineering Arnaud Bruneel 1 Valérie Labas 2 Agnès Mailloux 3 Sanjiv Sharma 0000-0003-3828-737X 4 Joelle Vinh 5 Michel Vaubourdolle 6 Bruno Baudin 7
title Proteomic study of human umbilical vein endothelial cells in culture
spellingShingle Proteomic study of human umbilical vein endothelial cells in culture
Sanjiv Sharma
title_short Proteomic study of human umbilical vein endothelial cells in culture
title_full Proteomic study of human umbilical vein endothelial cells in culture
title_fullStr Proteomic study of human umbilical vein endothelial cells in culture
title_full_unstemmed Proteomic study of human umbilical vein endothelial cells in culture
title_sort Proteomic study of human umbilical vein endothelial cells in culture
author_id_str_mv b6b7506358522f607b171ec9c94757b7
author_id_fullname_str_mv b6b7506358522f607b171ec9c94757b7_***_Sanjiv Sharma
author Sanjiv Sharma
author2 Arnaud Bruneel
Valérie Labas
Agnès Mailloux
Sanjiv Sharma
Joelle Vinh
Michel Vaubourdolle
Bruno Baudin
format Journal article
container_title PROTEOMICS
container_volume 3
container_issue 5
container_start_page 714
publishDate 2003
institution Swansea University
issn 1615-9853
1615-9861
doi_str_mv 10.1002/pmic.200300409
college_str Faculty of Science and Engineering
hierarchytype
hierarchy_top_id facultyofscienceandengineering
hierarchy_top_title Faculty of Science and Engineering
hierarchy_parent_id facultyofscienceandengineering
hierarchy_parent_title Faculty of Science and Engineering
department_str School of Engineering and Applied Sciences - Biomedical Engineering{{{_:::_}}}Faculty of Science and Engineering{{{_:::_}}}School of Engineering and Applied Sciences - Biomedical Engineering
document_store_str 0
active_str 0
description The endothelium is a single layer of cells lining the inside face of all blood vessels. It constitutes a major metabolic organ which is critically involved in the generation and the regulation of multiple physiological and pathological processes such as coagulation, hemostasis, inflammation, atherosclerosis, angiogenesis and cancerous metastasis dissemination. In order to increase our knowledge about the protein content and the main biological pathways of human vascular endothelial cells, we have undertaken the proteomic analysis of the most explored present endothelial cell model, i.e. primocultures of human umbilical vein endothelial cells (HUVECs). Using low levels of protein loads (&#126; 30 νg), the association of two-dimensional electrophoresis with matrix-assisted laser desorption/ionization-time of flight mass spectrometry, liquid chromatography-tandem mass spectrometry and database interrogations allowed us to identify 53 proteins of suspected endothelial origin in quiescent HUVECs. Beside cytoskeletal proteins such as actin, tubulin, tropomyosin and vimentin, we identified various proteins more especially implicated in cellular motility and plasticity (e.g. cofilin, F-actin capping protein and prefoldin), in regulation of apoptosis and senescence (protease inhibitor 9, glucose related proteins, heat shock proteins, thioredoxin peroxidase, nucleophosmin) as well as other proteins implicated in coagulation (annexin V, high mobility group protein), antigen presentation (valosin containing protein and ubiquitin carboxyl terminal hydrolase isozyme L1) and enzymatic capabilities (glutathione-S-transferase, protein disulfide isomerases, lactate deshydrogenase). The presented annotated 2-D maps of HUVECs will be soon available on the web at http://www. huvec.com.
published_date 2003-05-31T03:45:17Z
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score 11.036334

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