Please use this identifier to cite or link to this item: http://repositorio.unifesp.br/handle/11600/35413
Title: A motif within the N-terminal domain of TSP-1 specifically promotes the proangiogenic activity of endothelial colony-forming cells
Authors: Dias, Juliana Vieira
Benslimane-Ahmim, Zahia
Egot, Marion
Lokajczyk, Anna
Grelac, Francoise
Galy-Fauroux, Isabelle
Juliano, Luiz [UNIFESP]
Le-Bonniec, Bernard
Takiya, Cristina Maeda
Fischer, Anne-Marie
Blanc-Brude, Olivier
Morandi, Veronica
Boisson-Vidal, Catherine
Universidade do Estado do Rio de Janeiro (UERJ)
INSERM
Univ Paris 05
Universidade Federal de São Paulo (UNIFESP)
Universidade Federal do Rio de Janeiro (UFRJ)
Hop Europeen Georges Pompidou
Keywords: thrombospondin-1
endothelial colony-forming cells
glycosaminoglycans
angiogenesis
Issue Date: 15-Oct-2012
Publisher: Elsevier B.V.
Citation: Biochemical Pharmacology. Oxford: Pergamon-Elsevier B.V., v. 84, n. 8, p. 1014-1023, 2012.
Abstract: Thrombospondin-1 (TSP-1) gives rise to fragments that have both pro- and anti-angiogenic effects in vitro and in vivo. the TSP-HepI peptide (2.3 kDa), located in the N-terminal domain of TSP-1, has proangiogenic effects on endothelial cells. We have previously shown that TSP-1 itself exhibits a dual effect on endothelial colony-forming cells (ECFC) by enhancing their adhesion through its TSP-HepI fragment while reducing their proliferation and differentiation into vascular tubes (tubulogenesis) in vitro. This effect is likely mediated through CD47 binding to the TSP-1 C-terminal domain. Here we investigated the effect of TSP-HepI peptide on the angiogenic properties of ECFC in vitro and in vivo. TSP-HepI peptide potentiated FGF-2-induced neovascularisation by enhancing ECFC chemotaxis and tubulogenesis in a Matrigel plug assay. ECFC exposure to 20 mu g/mL of TSP-HepI peptide for 18 h enhanced cell migration (p < 0.001 versus VEGF exposure), upregulated alpha 6-integrin expression, and enhanced their cell adhesion to activated endothelium under physiological shear stress conditions at levels comparable to those of SDF-1 alpha. the adhesion enhancement appeared to be mediated by the heparan sulfate proteoglycan (HSPG) syndecan-4, as ECFC adhesion was significantly reduced by a syndecan-4-neutralising antibody. ECFC migration and tubulogenesis were stimulated neither by a TSP-HepI peptide with a modified heparin-binding site (S/TSP-HepI) nor when the glycosaminoglycans (GAGS) moieties were removed from the ECFC surface by enzymatic treatment. Ex vivo TSP-HepI priming could potentially serve to enhance the effectiveness of therapeutic neovascularisation with ECFC. (C) 2012 Elsevier Inc. All rights reserved.
URI: http://repositorio.unifesp.br/handle/11600/35413
ISSN: 0006-2952
Other Identifiers: http://dx.doi.org/10.1016/j.bcp.2012.07.006
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