THROMBOPOIETIN, C-MPL LIGAND, INDUCES TYROSINE PHOSPHORYLATION OF TYK2, JAK2, AND STAT3, AND ENHANCES AGONISTS-INDUCED AGGREGATION IN PLATELETS IN-VITRO

被引：132

作者：

EZUMI, Y ^{[1
]}

TAKAYAMA, H ^{[1
]}

OKUMA, M ^{[1
]}

机构：

[1] KYOTO UNIV,FAC MED,DEPT INTERNAL MED,DIV 1,SAKYO KU,KYOTO 606,JAPAN

来源：

FEBS LETTERS | 1995年 / 374卷 / 01期

关键词：

THROMBOPOIETIN; SIGNAL TRANSDUCTION; PROTEIN-TYROSINE KINASE; TRANSCRIPTION FACTOR; PLATELET AGGREGATION; ADENOSINE DIPHOSPHATE;

D O I：

10.1016/0014-5793(95)01072-M

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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.

引用

页码：48 / 52

页数：5

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