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 Lettjournal_title
FEBS lettersauthors
Ezumi Y,Takayama H,Okuma Mdoi
10.1016/0014-5793(95)01072-msubject
Has Abstractpub_date
1995-10-23 00:00:00pages
48-52issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(95)01072-Mjournal_volume
374pub_type
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