Isolation and characterization of a platelet surface collagen binding complex related to VLA-2
SA Santoro, SM Rajpara, WD Staatz… - … and Biophysical Research …, 1988 - Elsevier
SA Santoro, SM Rajpara, WD Staatz, VL Woods Jr
Biochemical and Biophysical Research Communications, 1988•ElsevierSummary 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 …
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 …
Summary
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.
Elsevier