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Signal transduction by the peptide which mimics the activity of thrombopoietin
Author(s) -
Kimura Tatsuya,
Kaburaki Hiroshi,
Tsujino Tomomi,
Watanabe Yoshinari,
Kato Hideo
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800202292
Subject(s) - thrombopoietin , janus kinase 2 , phosphorylation , thrombopoietin receptor , stat5 , tyrosine phosphorylation , signal transduction , chemistry , microbiology and biotechnology , haematopoiesis , receptor , agonist , tyrosine kinase , janus kinase , biology , cancer research , biochemistry , stem cell
Thrombopoietin (TPO) plays a central role in megakaryopoiesis and platelet production. It is a ligand for c‐mpl, which is a member of the hematopoietic receptor superfamily. We have recently identified several human c‐mpl binding peptides which are distinct from TPO, from phage random peptide libraries. PK1M is one of these peptides and is an agonist of c‐mpl which is TPO receptor. We show here that PK1M induces the tyrosine phosphorylation of the Janus kinase 2 (JAK2) and the activation of the signal transducer and activation of transcription 5 (STAT5) in TPO‐dependent cells like TPO.