Abstract
Three monoclonal antibodies, P256 , P140, and P112 , react with the 135,000 mol wt IIb component of the glycoprotein IIb/IIa complex. They also react with a 200,000-mol wt protein present at low levels in the complex. Using immunofluorescence techniques, monoclonal antibodies P140 and P112 , but not P256 , can be shown to bind to 80% of human monocytes. However, P256 was able to immunoprecipitate the IIb/IIIa complex from detergent-solubilized monocytes, suggesting that the P256 epitope is less accessible on monocytes than on platelets. The monoclonal antibodies also precipitated molecules of approximately 200,000 mol wt from the monocytes. Two other monoclonal antibodies, J15 (specific for the IIb/IIIa complex) and AN51 (which reacts with the second major platelet glycoprotein complex, I), also react with monocytes. Binding of the monoclonal antibodies to the histiocytic cell line, U937, and promyelocytic cell line, HL-60, reflected the pattern of reaction with monocytes. The presence on monocytes of these glycoproteins, instrumental to the role of platelets in clotting, raises the possibility that monocytes might have similar functions in particular circumstances.
