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Blood, 1 December 2000, Vol. 96, No. 12, pp. 3786-3792
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
Roles of SLP-76, phosphoinositide 3-kinase, and
gelsolin in the platelet shape changes initiated by the collagen
receptor GPVI/FcR -chain complex
Hervé Falet,
Kurt L. Barkalow,
Vadim I. Pivniouk,
Michael J. Barnes,
Raif S. Geha, and
John H. Hartwig
From the Division of Hematology, Brigham and Women's
Hospital, and the Division of Immunology, Children's Hospital, Harvard
Medical School, Boston, MA; and the Department of Biochemistry,
Cambridge University, Cambridge, United Kingdom.
How platelet shape change initiated by a collagen-related peptide
(CRP) specific for the GPVI/FcR -chain complex (GPVI/FcR-chain) is
coupled to SLP-76, phosphoinositide (PI) 3-kinase, and gelsolin is
reported. As shown by video microscopy, platelets rapidly round and
grow dynamic filopodial projections that rotate around the periphery of
the cell after they contact a CRP-coated surface. Lamellae subsequently
spread between the projections. All the actin-driven shape changes
require SLP-76 expression. SLP-76 is essential for the Ca++
mobilization induced by CRP, whereas PI 3-kinase only modulates it. The
extension of lamellae requires net actin assembly and an exposure of
actin filament barbed ends downstream of PI 3-kinase. Gelsolin
expression is also required for the extension of lamellae, but
not for the formation of filopodia. Altogether, the data describe the role of SLP-76 in the platelet activation initiated by
GPVI/FcR-chain and the roles of PI 3-kinase and gelsolin in lamellae spreading.
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