Heterogeneity of microfibrils: role of thrombospondin-microfibrils in the thrombogenicity of the subendothelium.

Abstract

We report the results of an immunogold electron microscopical analysis on microfibrils from the arterial subendothelium showing that thrombospondin (TSP) is present on 40 nm-diameter structures joining 8-10 nm-diameter microfibrils containing fibrillin. They differ from type VI collagen which forms 3-5 nm-diameter microfibrils. TSP containing microfibrils (TSP-MF) extracted from human umbilical arteries did not contain fibrillin or type VI collagen. Blood platelet interactions with TSP-MF were not modified by anti-fibrillin or anti-type VI collagen antibodies. In situ, vWF was bound to cross-linked microfibrils, at the level of their 40 nm junction, and a double-labeling with the anti-thrombospondin and anti-vWF antibodies was observed. In vitro, vWF binding to TSP-MF was not inhibited by anti-fibrillin or anti-type VI collagen antibodies. These results suggest a structural and functional heterogeneity of microfibrils and emphasize the role of TSP-MF in the thrombogenicity of the subendothelium.