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Differential redistribution of platelet glycoproteins Ib and IIb-IIIa after
plasmin stimulation [published erratum appears in Blood 1991 Jul
15;78(2):545]
EM Cramer, H Lu, JP Caen, C Soria, MC Berndt and D Tenza
Institut des Vaisseaux et du Sang, Paris, France.
The subcellular localization of the platelet membrane receptors
glycoproteins (GP) Ib and IIb/IIIa [corrected] has been studied within
resting platelets by a combination of biochemical and cytochemical
techniques. While both GPIb and GPIIb/IIIa are localized within the plasma
membrane and surface-connected canalicular system (SCCS) membranes, only
GPIIb/IIIa is present within the internal face of alpha- granular
membranes. Previous studies demonstrated that plasmin can induce platelet
stimulation and also decrease ristocetin-induced platelet aggregation; it
was suggested that this was because of GPIb degradation by plasmin. In this
study, the respective localizations of both GPIb and GPIIb/IIIa were
visualized during in vitro plasmin stimulation of platelets. Generally,
plasmin induced shape change, pseudopod formation, organelle centralization
either with or without alpha-granule release depending on the conditions of
stimulation. Plasmin treatment of platelets at 37 degrees C resulted in the
disappearance of GPIb from the cell surface and its subsequent
redistribution into the channels and vesicles of the SCCS with no
significant modification of GPIIb/IIIa remaining on the plasma membrane.
Within degranulated platelets, GPIIb/IIIa was expressed on the plasma
membrane and within membranes of large vacuoles containing the
alpha-granule proteins. GPIb was virtually absent from these structures and
mainly restricted to the SCCS. Addition of cytochalasin D inhibited the
migration of GPIb to the SCCS. Biochemical measurements confirmed that no
important hydrolysis of GPIb had occurred because only very little amounts
of glycocalicin were generated during the reaction. In conclusion, in
plasmin-treated platelets GPIIb/IIIa is externalized to the plasma membrane
while GPIb is internalized into the SCCS. Although previous studies have
suggested that plasmin degrades GPIb, the reduction in ristocetin-induced
aggregation may be explained by its apparent redistribution within the
membranes of the SCCS.
Volume 77,
Issue 4,
pp. 694-699,
02/15/1991
Copyright © 1991 by The American Society of Hematology
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