Thrombopoietin, c-Mpl ligand, induces tyrosine phosphorylation of Tyk2, JAK2, and STAT3, and enhances agonists-induced aggregation in platelets in vitro.

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Ezumi Y,Takayama H,Okuma M

doi

10.1016/0014-5793(95)01072-m

subject

Has Abstract

pub_date

1995-10-23 00:00:00

pages

48-52

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(95)01072-M

journal_volume

374

pub_type

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