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Alpha-granule membrane mirrors the platelet plasma membrane and contains
the glycoproteins Ib, IX, and V
G Berger, JM Masse and EM Cramer
INSERM U91, Hopital Henri Mondor, Creteil, France.
We have recently shown that several components from the platelet plasma
membrane were also present at different rates in the alpha-granule
membrane. This is the case for the glycoprotein (GP) IIb-IIIa (CD41), CD36,
CD9, PECAM1, and Rap1b, while the GPIB-IX-V complex was considered to
escape the rule. In this investigation, we studied the subcellular
localization of GPIb, GPIX, and GPV in the resting platelets of normal
subjects, patients with Bernard-Soulier syndrome, patients with Gray
platelet syndrome, and human cultured megakaryocytes. Ultra-thin sections
of the cells were labeled with antibodies directed against glycocalicin,
GPIb, GPIX, and GPV. We have shown that a significant and reproducible
labeling for the three GPs was associated with the alpha-granule membrane,
accounting for approximately 10% of the total labeling. Furthermore, GPIb
labeling appears Willebrand factor (vWF). After thrombin activation, vWF
remained close to the limiting membrane of the open canalicular system
(OCS), suggesting an early association of both receptor and ligand. Plasma
membrane and alpha-granule labeling was virtually absent from the
Bernard-Soulier platelets (characterized by a GPIb deficiency), thus
proving the specificity of the reaction. In Gray platelets (storage granule
deficiency syndrome), the small residual alpha- granules were also
occasionally labeled for GPIb, GPIX, and GPIX. Cultured megakaryocytes that
displayed the classical GPIb distribution, eg, demarcation and plasma
membranes, exhibited also a discrete labeling associated to the
alpha-granules. In conclusion, this study shows that, evenly for these
three GPs, the alpha-granule membrane mirrors the plasma membrane
composition. This might occur through an endocytotic process affecting each
plasma membrane protein to a different extent and could have a physiologic
relevance in further presentation of a receptor bound to its alpha-granule
ligand to the platelet surface.
Volume 87,
Issue 4,
pp. 1385-1395,
02/15/1996
Copyright © 1996 by The American Society of Hematology
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