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(Received for publication, July 1, 1997)
From the The mechanism by which occupancy of collagen
receptors is coupled to platelet activation has been uncertain. Our
group previously demonstrated that glycoprotein (GP) VI, an
uncharacterized platelet membrane protein, is specifically required for
collagen-platelet interaction leading to activation of protein-tyrosine
kinase Syk. Since collagen stimulation of platelets has recently been
found to induce tyrosine phosphorylation of Fc receptor (FcR)
Volume 272, Number 38,
Issue of September 19, 1997
pp. 23528-23531
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
-Chain with
Glycoprotein VI and Their Co-expression as a Collagen Receptor
in Human Platelets
,
,
Department of Hematology and Oncology,
-chain, a signal-generating subunit of FcR, we further investigated
the relationships between FcR -chain and GPVI in human platelets. Our present study revealed the following. FcR -chain was physically and stably associated with GPVI in human platelets; both FcR -chain and GPVI were proportionally absent in GPVI-deficient platelets; GPVI
cross-linking or collagen stimulation of platelets resulted in tyrosine
phosphorylation of GPVI-associated FcR -chain accompanied by Syk
association and activation. These findings strongly suggest that the
associated complex of GPVI and FcR -chain is a collagen receptor
featuring the signaling through immune receptors.
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