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

FEBS Letters

Clezardin, Philippe²  Hunter, Nikolas R.¹  Bourdillon, Marie-Claude²  McGregor, John L.² 

[1] MRC/SNBTS Blood Components Assay Group, 2 Forrest Road, Edinburgh EH1 2QW, Scotland;INSERM U63, Laboratoire d'Hémobiologie, Faculté de Médecine A. Carrell, rue G. Paradin, F-69372 Lyon, France

关键词: Thrombospondin;    ELISA;    Adhesion assay;    (Human endothelial cell;    Platelet);   

DOI  :  10.1016/0014-5793(88)80001-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown