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Platelet alpha-granule and plasma membrane share two new components: CD9
and PECAM-1
EM Cramer, G Berger and MC Berndt
Inserm U.348, Hopital Lariboisiere, Paris, France.
CD9 (p24) and PECAM1 (CD31) antigens are well-defined components of the
platelet plasma membrane. Both are integral glycoproteins (GPs) implicated
in the adhesive and aggregative properties of human platelets. In the
present report, we have investigated their subcellular localization using
immunoelectron microscopy. The monospecificity of the two polyclonal
antibodies used was confirmed by immunoblotting. On normal resting
platelets, immunolabeling for CD9 and PECAM1 was found lining the plasma
membrane and the luminal face of the open canalicular system. Some labeling
was also consistently found on the alpha-granule limiting membrane. This
was confirmed by double labeling experiments in which fibrinogen and von
Willebrand factor (vWF) were used as alpha-granule markers. CD9 and PECAM-1
were found lining the membrane of the same granules that contained
fibrinogen and vWF in their matrix. CD9 and PECAM-1 thus appear to have an
intracellular distribution identical to GPIIb-IIIa, a major aggregation
platelet receptor. To rule out a cross-reactivity of the two polyclonal
antibodies with GPIIb/IIIa, we studied PECAM1 and CD9 expression on the
platelets from a patient with type I Glanzmann's thrombasthenia whose
platelets are devoid of GPIIb/IIIa. The same pattern of labeling was
observed for both antigens as for normal platelets. Normal platelets were
further observed after stimulation by agonists that either fail to induce
(ADP) or induce granule secretion (thrombin). After treatment with ADP,
platelets changed shape and centralized their granules; the plasma membrane
immunolabeling remained unchanged; and gold particles were still found
decorating the periphery of the centralized alpha- granules. After thrombin
treatment, alpha-granules fused with the platelet membrane and secretion
occurred. A significant increase of labeling was then observed on the
platelet surface. From these results we conclude that the alpha-granule
membrane contains two additional receptors in common with the plasma
membrane. This suggests that alpha- granule membrane receptors may
originate from a dual mechanism: direct targeting from the Golgi complex in
megakaryocytes (for alpha-granule- specific receptors such as P-selectin)
or by endocytosis from the plasma membrane (for proteins distributed in the
two compartments).
Volume 84,
Issue 6,
pp. 1722-1730,
09/15/1994
Copyright © 1994 by The American Society of Hematology
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