Isolation and characterization of a platelet surface collagen binding complex related to VLA-2.

Santoro SA, Rajpara SM, Staatz WD, Woods VL
Biochem Biophys Res Commun. 1988 153 (1): 217-23

PMID: 2837201 · DOI:10.1016/s0006-291x(88)81211-7

A heterodimeric, Mg++-dependent, collagen binding protein has been isolated from platelet membranes. Electrophoretic properties and monoclonal antibody reactivity indicate that the heavy chain of the complex is platelet membrane glycoprotein Ia and that the light chain is glycoprotein IIa. Furthermore, the receptor appears to be identical with the recently defined VLA-2 complex found on activated T-lymphocytes, platelets and other cells. When incorporated into liposomes, the purified complex mediates the Mg++-dependent adhesion of the liposomes to collagen substrates. These observations suggest that the VLA-2 complex mediates cellular adhesion to collagen in platelets and possibly in other cells.

MeSH Terms (11)

Antibodies, Monoclonal Antigens, Differentiation Blood Platelets Cell Adhesion Cross Reactions Humans Magnesium Molecular Weight Receptors, Cell Surface Receptors, Collagen Receptors, Very Late Antigen

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