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Y Bai, H Durbin and N Hogg
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.
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| Copyright © 1984 by American Society of Hematology Online ISSN: 1528-0020 | |||||||||