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Cell attachment and fibrinogen binding properties of platelet and endothelial cell thrombospondin are not affected by structural differences in the 70 and 18 kDa protease‐resistant domains
Author(s) -
Clezardin Philippe,
Bourdillon Marie-Claude,
Hunter Nikolas R.,
McGregor John L.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80001-2
Subject(s) - thrombospondin , platelet , fibrinogen , thrombospondins , endothelial stem cell , protease , chemistry , cell , thrombospondin 1 , metalloproteinase , microbiology and biotechnology , disintegrin , biochemistry , biology , angiogenesis , immunology , matrix metalloproteinase , enzyme , in vitro , cancer research
Structural differences between platelet and endothelial cell thrombospondin (TBSP) were found in two protease‐resistant domains (70 and 18 kDa). The 70 kDa fragment is involved in the binding of TBSP to fibrinogen and the 18 kDa fragment in the attachment to various cultured cells. Despite these structural differences, platelet and endothelial cell TBSP bound with the same affinity to fibrinogen and mediated the attachment of smooth muscle cells but not of endothelial cells.