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Platelet dense granule membranes contain both granulophysin and P- selectin
(GMP-140)
SJ Israels, JM Gerrard, YV Jacques, A McNicol, B Cham, M Nishibori and DF Bainton
Department of Paediatrics, University of Manitoba, Winnipeg, Canada.
We recently reported the characterization of a platelet granule membrane
protein of molecular weight (mol wt) 40,000 called granulophysin (Gerrard
et al: Blood 77:101, 1991), identified by a monoclonal antibody (MoAb D545)
raised to purified dense granule membranes. Using
immunoelectron-microscopic techniques on frozen thin sections, this protein
was localized in resting and thrombin-stimulated platelets. In resting
platelets, labeled with antigranulophysin antibodies and immunogold probes,
label was localized to the membranes of one or two clear granules per
platelet thin section. D545 also labeled dense granules in permeabilized
whole platelets and isolated dense granule preparations examined by
whole-mount techniques. Expression of granulophysin on the platelet surface
paralleled dense granule secretion as measured by 14C-serotonin release
under conditions in which lysosomal granule release, as measured by
beta-glucuronidase secretion, was less than 5%. After thrombin stimulation,
both the surface-connected canalicular system and the plasma membrane were
labeled, demonstrating redistribution of granulophysin associated with
degranulation. Double labeling experiments with D545 and antibodies to the
alpha-granule membrane protein, P-selectin, demonstrated labeling of both
P-selectin and granulophysin on dense granule membranes. Distribution of
both proteins on the plasma membrane after platelet stimulation was
similar. The results demonstrate that granulophysin is localized to the
dense granules of platelets and is redistributed to the plasma membrane
after platelet activation.
Volume 80,
Issue 1,
pp. 143-152,
07/01/1992
Copyright © 1992 by The American Society of Hematology
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