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Blood, 1 April 2002, Vol. 99, No. 7, pp. 2442-2447
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
Role of the Src family kinase Lyn in TxA2 production, adenosine
diphosphate secretion, Akt phosphorylation, and irreversible
aggregation in platelets stimulated with  -thrombin
Moon J. Cho,
Tamara I. Pestina,
Shirley A. Steward,
Clifford A. Lowell,
Carl W. Jackson, and
T. Kent Gartner
From the Department of Microbiology and Molecular Cell
Sciences, University of Memphis; the Division of Experimental
Hematology, St Jude Children's Research Hospital, Memphis, TN; and the
Department of Laboratory Medicine, University of California, San
Francisco.
Members of the Src family of kinases are abundant in platelets.
Although their localization is known, their role(s) in platelet function are not well understood. Lyn is a Src-family kinase that participates in signal transduction pathways elicited by
collagen-related peptide; it has also been implicated through
biochemical studies in the regulation of von Willebrand factor
signaling. Here, we provide evidence that Lyn plays a role in
 -thrombin activation of platelets. Unlike the wild-type platelets,
platelets from Lyn-deficient mice do not undergo irreversible
aggregation, produce thromboxane A2, or secrete adenosine diphosphate
in response to submaximal -thrombin concentrations that cause
secretion-dependent irreversible aggregation. Phosphorylation of Akt, a
downstream effector of phosphatidylinositol 3-kinase, also requires a
higher concentration of -thrombin in Lyn-deficient platelets than in
wild-type platelets. These findings demonstrate that Lyn signaling is
required for thrombin induction of secretion-dependent platelet
aggregation. Specifically, Lyn is required under these conditions to
enable thrombin-induced TxA2 production and adenosine diphosphate
secretion, necessary steps in secretion-dependent platelet aggregation.
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