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Plasmin-induced redistribution of platelet glycoprotein Ib
AD Michelson and MR Barnard
Department of Pediatrics, University of Massachusetts Medical School,
Worcester 01655.
Platelet membrane glycoprotein Ib (GPIb), a receptor for von Willebrand
factor and thrombin, is present on the platelet surface membrane, in
intraplatelet stores, and in plasma (as the proteolytic fragment
glycocalicin). We examined the hypothesis that after plasmin-mediated
cleavage of platelet surface GPIb, platelets can replenish their surface
GPIb pool. Incubation of washed platelets with plasmin (1 hour, 22 degrees
C) resulted in loss of platelet surface GPIb, but further incubation (3
hours, 37 degrees C) in autologous plasma resulted in restoration of
platelet surface GPIb, as determined by ristocetin- induced platelet
agglutination and a flow cytometric assay of platelet binding of three
GPIb-specific monoclonal antibodies. Despite the restoration of platelet
surface GPIb after the 3-hour incubation of plasmin-treated platelets in
autologous plasma, the whole platelet GPIb content (measured by
enzyme-linked immunosorbent assay [ELISA], sodium dodecyl
sulfate-polyacrylamide gel electrophoresis, and flow cytometry) remained
reduced, quantitatively corresponding to an increase in plasma glycocalicin
concentration (measured by ELISA). The loss and restoration of platelet
surface GPIb occurred on all platelets and, as evidenced by lack of
inhibition by prostaglandin E1, EDTA, and cytochalasins, was not mediated
by cyclic AMP, extracellular Ca2+, or the platelet microfilament system. In
summary, this study shows that after plasmin-mediated cleavage of platelet
surface GPIb, platelets can replenish their surface GPIb pool by
recruitment of GPIb molecules from the intraplatelet pool (or from a
sequestered surface site).
Volume 76,
Issue 10,
pp. 2005-2010,
11/15/1990
Copyright © 1990 by The American Society of Hematology
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