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Serglycin in Quiescent and Proliferating Primary Endothelial Cells

Proteoglycans are fundamental components of the endothelial barrier, but the functions of the proteoglycan serglycin in endothelium are less described. Our aim was to describe the roles of serglycin in processes relevant for endothelial dysfunction. Primary human umbilical vein endothelial cells (HU...

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Autores principales: Reine, Trine M., Vuong, Tram T., Rutkovskiy, Arkady, Meen, Astri J., Vaage, Jarle, Jenssen, Trond G., Kolset, Svein O.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4687888/
https://www.ncbi.nlm.nih.gov/pubmed/26694746
http://dx.doi.org/10.1371/journal.pone.0145584
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author Reine, Trine M.
Vuong, Tram T.
Rutkovskiy, Arkady
Meen, Astri J.
Vaage, Jarle
Jenssen, Trond G.
Kolset, Svein O.
author_facet Reine, Trine M.
Vuong, Tram T.
Rutkovskiy, Arkady
Meen, Astri J.
Vaage, Jarle
Jenssen, Trond G.
Kolset, Svein O.
author_sort Reine, Trine M.
collection PubMed
description Proteoglycans are fundamental components of the endothelial barrier, but the functions of the proteoglycan serglycin in endothelium are less described. Our aim was to describe the roles of serglycin in processes relevant for endothelial dysfunction. Primary human umbilical vein endothelial cells (HUVEC) were cultured in vitro and the expression of proteoglycans was investigated. Dense cell cultures representing the quiescent endothelium coating the vasculature was compared to sparse activated cell cultures, relevant for diabetes, cancer and cardiovascular disease. Secretion of (35)S- proteoglycans increased in sparse cultures, and we showed that serglycin is a major component of the cell-density sensitive proteoglycan population. In contrast to the other proteoglycans, serglycin expression and secretion was higher in proliferating compared to quiescent HUVEC. RNAi silencing of serglycin inhibited proliferation and wound healing, and serglycin expression and secretion was augmented by hypoxia, mechanical strain and IL-1β induced inflammation. Notably, the secretion of the angiogenic chemokine CCL2 resulting from IL-1β activation, was increased in serglycin knockdown cells, while angiopoietin was not affected. Both serglycin and CCL2 were secreted predominantly to the apical side of polarized HUVEC, and serglycin and CCL2 co-localized both in perinuclear areas and in vesicles. These results suggest functions for serglycin in endothelial cells trough interactions with partner molecules, in biological processes with relevance for diabetic complications, cardiovascular disease and cancer development.
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spelling pubmed-46878882015-12-31 Serglycin in Quiescent and Proliferating Primary Endothelial Cells Reine, Trine M. Vuong, Tram T. Rutkovskiy, Arkady Meen, Astri J. Vaage, Jarle Jenssen, Trond G. Kolset, Svein O. PLoS One Research Article Proteoglycans are fundamental components of the endothelial barrier, but the functions of the proteoglycan serglycin in endothelium are less described. Our aim was to describe the roles of serglycin in processes relevant for endothelial dysfunction. Primary human umbilical vein endothelial cells (HUVEC) were cultured in vitro and the expression of proteoglycans was investigated. Dense cell cultures representing the quiescent endothelium coating the vasculature was compared to sparse activated cell cultures, relevant for diabetes, cancer and cardiovascular disease. Secretion of (35)S- proteoglycans increased in sparse cultures, and we showed that serglycin is a major component of the cell-density sensitive proteoglycan population. In contrast to the other proteoglycans, serglycin expression and secretion was higher in proliferating compared to quiescent HUVEC. RNAi silencing of serglycin inhibited proliferation and wound healing, and serglycin expression and secretion was augmented by hypoxia, mechanical strain and IL-1β induced inflammation. Notably, the secretion of the angiogenic chemokine CCL2 resulting from IL-1β activation, was increased in serglycin knockdown cells, while angiopoietin was not affected. Both serglycin and CCL2 were secreted predominantly to the apical side of polarized HUVEC, and serglycin and CCL2 co-localized both in perinuclear areas and in vesicles. These results suggest functions for serglycin in endothelial cells trough interactions with partner molecules, in biological processes with relevance for diabetic complications, cardiovascular disease and cancer development. Public Library of Science 2015-12-22 /pmc/articles/PMC4687888/ /pubmed/26694746 http://dx.doi.org/10.1371/journal.pone.0145584 Text en © 2015 Reine et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Reine, Trine M.
Vuong, Tram T.
Rutkovskiy, Arkady
Meen, Astri J.
Vaage, Jarle
Jenssen, Trond G.
Kolset, Svein O.
Serglycin in Quiescent and Proliferating Primary Endothelial Cells
title Serglycin in Quiescent and Proliferating Primary Endothelial Cells
title_full Serglycin in Quiescent and Proliferating Primary Endothelial Cells
title_fullStr Serglycin in Quiescent and Proliferating Primary Endothelial Cells
title_full_unstemmed Serglycin in Quiescent and Proliferating Primary Endothelial Cells
title_short Serglycin in Quiescent and Proliferating Primary Endothelial Cells
title_sort serglycin in quiescent and proliferating primary endothelial cells
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4687888/
https://www.ncbi.nlm.nih.gov/pubmed/26694746
http://dx.doi.org/10.1371/journal.pone.0145584
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