PMID: 8601718Feb 1, 1996Paper

Human microvascular endothelial cells adhere to thrombospondin-1 via an RGD/CSVTCG domain independent mechanism

The Journal of Investigative Dermatology
Z S ChenR A Swerlick

Abstract

Thrombospondin-1 (TSP-1), 450-kDa glycoprotein secreted by platelets and endothelial cells at sites of tissue injury or inflammation, plays an important role in angiogenesis, inflammation, and vascular occlusive skin diseases. Many of the physiologic and pathologic activities of TSP-1 are dependent upon its interactions with endothelial cells. To better understand the basis of these activities, we examined the mechanisms mediating the binding of human dermal microvascular endothelial cells (HDMEC) to immobilized TSP-1. HDMEC bound to but did not spread on TSP-1 in a concentration-dependent manner. Monoclonal antibodies (MoAbs) which recognize two purported TSP-1 binding proteins, CS36 and the alphav integrin chain, or TSP-1-derived peptides CGRGDS and CSVTCG, alone or in combination with heparin, did not inhibit HDMEC adhesion to immobilized TSP-1. Furthermore, CSVTCG-ovalbumin conjugates failed to support HDMEC adhesion. Although RGD-containing peptides immobilized on plastic wells supported HDMEC binding, they also induced cell spreading not characteristic of cell binding to TSP-1 and binding was inhibited by free RGD peptide. Two MoAbs against different domains of TSP-1 (A 4.1 and C 6.1) failed to block HDMEC binding to TSP-...Continue Reading

References

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Citations

Nov 16, 2006·Journal of Molecular Medicine : Official Organ of the Gesellschaft Deutscher Naturforscher Und Ärzte·N I Fernandez-GarciaB Jimenez
Aug 11, 1997·The Journal of Cell Biology·D W DawsonN P Bouck
Dec 3, 1999·Biochemical and Biophysical Research Communications·S LarruceaM López-Trascasa
Apr 20, 2004·The International Journal of Biochemistry & Cell Biology·Josephine C Adams

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