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Title: Endothelial stress induces the release of vitamin D-binding protein, a novel growth factor

Abstract

Endothelial cells (EC) under stress release paracrine mediators that facilitate accumulation of vascular smooth muscle cells (VSCM) at sites of vascular injury. We found that medium conditioned by serum-starved EC increase proliferation and migration of VSCM in vitro. Fractionation of the conditioned medium followed by mass spectral analysis identified one bioactive component as vitamin D-binding protein (DBP). DBP induced both proliferation and migration of VSMC in vitro in association with increased phosphorylation of ERK 1/2. PD 98059, a biochemical inhibitor of ERK 1/2, abrogated these proliferative and migratory responses in VSMC. DBP is an important carrier for the vitamin-D sterols, 25-hydroxyvitamin-D, and 1{alpha},25-dihydroxyvitamin-D. Both sterols inhibited the activity of DBP on VSMC, suggesting that vitamin D binding sites are important for initiating the activities of DBP on VSMC. Release of DBP at sites of endothelial injury represents a novel pathway favoring accumulation of VSMC at sites of vascular injury.

Authors:
 [1];  [1];  [1];  [1];  [1];  [1];  [2];  [1]
  1. Research Centre CHUM, University of Montreal, 1560 Sherbrooke East, Montreal, Que., H2L 4M1 (Canada)
  2. Ste-Justine Hospital Research Centre, University of Montreal, 3175 Cote Ste-Catherine, Montreal, Que., H3T 1C5 (Canada)
Publication Date:
OSTI Identifier:
20793234
Resource Type:
Journal Article
Journal Name:
Biochemical and Biophysical Research Communications
Additional Journal Information:
Journal Volume: 338; Journal Issue: 3; Other Information: DOI: 10.1016/j.bbrc.2005.10.105; PII: S0006-291X(05)02323-5; Copyright (c) 2005 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; BIOLOGICAL STRESS; CELL PROLIFERATION; DBP; GROWTH FACTORS; INJURIES; MUSCLES; PHOSPHORYLATION; STEROLS; VITAMIN D

Citation Formats

Raymond, Marc-Andre, Desormeaux, Anik, Labelle, Andree, Soulez, Mathilde, Soulez, Gilles, Langelier, Yves, Pshezhetsky, Alexey V, and Hebert, Marie-Josee. Endothelial stress induces the release of vitamin D-binding protein, a novel growth factor. United States: N. p., 2005. Web. doi:10.1016/J.BBRC.2005.1.
Raymond, Marc-Andre, Desormeaux, Anik, Labelle, Andree, Soulez, Mathilde, Soulez, Gilles, Langelier, Yves, Pshezhetsky, Alexey V, & Hebert, Marie-Josee. Endothelial stress induces the release of vitamin D-binding protein, a novel growth factor. United States. https://doi.org/10.1016/J.BBRC.2005.1
Raymond, Marc-Andre, Desormeaux, Anik, Labelle, Andree, Soulez, Mathilde, Soulez, Gilles, Langelier, Yves, Pshezhetsky, Alexey V, and Hebert, Marie-Josee. 2005. "Endothelial stress induces the release of vitamin D-binding protein, a novel growth factor". United States. https://doi.org/10.1016/J.BBRC.2005.1.
@article{osti_20793234,
title = {Endothelial stress induces the release of vitamin D-binding protein, a novel growth factor},
author = {Raymond, Marc-Andre and Desormeaux, Anik and Labelle, Andree and Soulez, Mathilde and Soulez, Gilles and Langelier, Yves and Pshezhetsky, Alexey V and Hebert, Marie-Josee},
abstractNote = {Endothelial cells (EC) under stress release paracrine mediators that facilitate accumulation of vascular smooth muscle cells (VSCM) at sites of vascular injury. We found that medium conditioned by serum-starved EC increase proliferation and migration of VSCM in vitro. Fractionation of the conditioned medium followed by mass spectral analysis identified one bioactive component as vitamin D-binding protein (DBP). DBP induced both proliferation and migration of VSMC in vitro in association with increased phosphorylation of ERK 1/2. PD 98059, a biochemical inhibitor of ERK 1/2, abrogated these proliferative and migratory responses in VSMC. DBP is an important carrier for the vitamin-D sterols, 25-hydroxyvitamin-D, and 1{alpha},25-dihydroxyvitamin-D. Both sterols inhibited the activity of DBP on VSMC, suggesting that vitamin D binding sites are important for initiating the activities of DBP on VSMC. Release of DBP at sites of endothelial injury represents a novel pathway favoring accumulation of VSMC at sites of vascular injury.},
doi = {10.1016/J.BBRC.2005.1},
url = {https://www.osti.gov/biblio/20793234}, journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 3,
volume = 338,
place = {United States},
year = {Fri Dec 23 00:00:00 EST 2005},
month = {Fri Dec 23 00:00:00 EST 2005}
}