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

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 str...

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Bibliographic Details
Published in:FEBS letters 1988-02, Vol.228 (2), p.215-218
Main Authors: Clezardin, Philippe, Bourdillon, Marie-Claude, Hunter, Nikolas R., McGregor, John L.
Format: Article
Language:English
Subjects:
Adhesion assay
Blood Platelets - analysis
Cell Adhesion
Electrophoresis, Polyacrylamide Gel
ELISA
endothelium
Endothelium, Vascular - analysis
Endothelium, Vascular - cytology
Enzyme-Linked Immunosorbent Assay
Fibrinogen - metabolism
Glycoproteins - metabolism
Human endothelial cell, Platelet
Humans
Kinetics
Muscle, Smooth, Vascular - cytology
Peptide Fragments - isolation & purification
Peptide Fragments - metabolism
platelets
Thermolysin - metabolism
Thrombospondin
Thrombospondins
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(88)80001-2