Isolation and characterization of a platelet surface collagen binding complex related to VLA-2.
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.
Santoro
S A
SA
Division of Laboratory Medicine, Washington University School of Medicine, St. Louis, Missouri 63110.
Rajpara
S M
SM
Staatz
W D
WD
Woods
V L
VL
D000911:Antibodies, Monoclonal; D000943:Antigens, Differentiation / Q000032:analysis*; D001792:Blood Platelets / Q000032:analysis*; D002448:Cell Adhesion; D003429:Cross Reactions; D006801:Humans; D008274:Magnesium / Q000378:metabolism; D008970:Molecular Weight; D011956:Receptors, Cell Surface / Q000302:isolation & purification*; D038981:Receptors, Collagen; D016029:Receptors, Very Late Antigen
D000911:Antibodies, Monoclonal; D000943:Antigens, Differentiation; D011956:Receptors, Cell Surface; D038981:Receptors, Collagen; D016029:Receptors, Very Late Antigen; D008274:Magnesium