期刊
BLOOD
卷 99, 期 7, 页码 2442-2447出版社
AMER SOC HEMATOLOGY
DOI: 10.1182/blood.V99.7.2442
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- NCI NIH HHS [P30 CA 21765, P01 CA 20180] Funding Source: Medline
- NHLBI NIH HHS [HL 54476, HL 63216, HL 56369] Funding Source: Medline
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-famlly 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 gamma-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 gamma-thrombin concentrations that cause secretion-dependent irreversible aggregation. Phosphorylation of Akt, a downstream effector of phosphatidylinositol 3-kinase, also requires a higher concentration of gamma-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. (C) 2002 by The American Society of Hematology.
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