FEBS Letters | |
Thrombopoietin, c‐Mpl ligand, induces tyrosine phosphorylation of Tyk2, JAK2, and STAT3, and enhances agonists‐induced aggregation in platelets in vitro | |
Takayama, Hiroshi1  Okuma, Minoru1  Ezumi, Yasuharu1  | |
[1] First Division, Department of Internal Medicine, Faculty of Medicine, Kyoto University, 54 Shogoin-Kawaramachi, Sakyo-ku, Kyoto 606, Japan | |
关键词: Thrombopoietin; Signal transduction; Protein-tyrosine kinase; Transcription factor; Platelet aggregation; Adenosine diphosphate; TPO; thrombopoietin; JAK; Janus tyrosine kinase; ASA; acetylsalicylic acid or aspirin; PRP; platelet-rich plasma; STAT; signal transducers and activators of transcription; | |
DOI : 10.1016/0014-5793(95)01072-M | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
We investigated in vitro effects of recombinant human thrombopoietin (TPO), or c-Mpl ligand, on human platelets. TPO induced rapid dose-dependent tyrosine phosphorylation of several proteins. We identified Janus tyrosine kinases, Tyk2 and JAK2, and a member of STAT (signal transducers and activators of transcription) family, STAT3, as the tyrosine-phosphorylated proteins in response to TPO. TPO by itself did not cause platelet aggregation and shape change, but augmented ADP-induced aggregation in a dose-dependent manner. Acetylsalicylic acid inhibited the secondary aggregation enhanced by TPO, but not the TPO-induced potentiation of the primary aggregation. TPO modulates platelet activation possibly through protein-tyrosine phosphorylation.
【 授权许可】
Unknown
【 预 览 】
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