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Receptor patching and capping of platelet membranes induced by monoclonal
antibodies
S Santoso, U Zimmermann, J Neppert and C Mueller-Eckhardt
Redistribution of glycoproteins (GP) Ib, glycocalicin, IIb, and IIIa on the
surface of human platelets in response to stimulation with corresponding
monoclonal antibodies (MoAb) and a polyclonal antiglycocalicin antibody was
studied by immunofluorescence, immunoelectron microscopy, and a
quantitative radioimmune assay. Immobilization of the antigens by
prefixation with formaldehyde showed a uniform distribution over the
surface of the platelet. Incubation of unfixed platelets with specific MoAb
against various epitopes on GPIIb and/or IIIa resulted in a time-dependent
patching, subsequent capping, and after prolonged exposure to the
antibody/label complex, internalization of the complex, possibly by
endocytosis. In contrast, GPIb could not be shown to cap. From these
results we conclude that platelet GPIIb and/or IIIa undergo spatial
rearrangement in a manner analogous to that observed in lymphocytes,
whereas GPIb does not. Since both GPIb and GPIIb and/or IIIa seem to be
transmembraneous GP associated with the cytoskeleton, a special, though
unidentified, role of GPIIb/IIIa in the induction of lateral membrane
mobility is postulated.
Volume 67,
Issue 2,
pp. 343-349,
02/01/1986
Copyright © 1986 by The American Society of Hematology
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