Literature DB >> 7517045

The identification of JAK2 tyrosine kinase as a signaling molecule for growth hormone.

C Carter-Su1, L S Argetsinger, G S Campbell, X Wang, J Ihle, B Witthuhn.   

Abstract

The intracellular pathways by which the binding of growth hormone (GH) to its receptor elicits its diverse effects have eluded investigators for many years. Studies showing that GH rapidly stimulates tyrosyl phosphorylation of cellular proteins, and that tyrosine kinase activity co-purifies with GH-GH receptor complexes, led us to hypothesize that activation by GH of a receptor-associated tyrosine kinase is an important early, and perhaps, initiating step in signal transduction by GH. Here, we review the work identifying JAK2 as a GH receptor-associated tyrosine kinase that is rapidly activated by ligand binding.

Entities:  

Mesh:

Substances:

Year:  1994        PMID: 7517045     DOI: 10.3181/00379727-206-43744

Source DB:  PubMed          Journal:  Proc Soc Exp Biol Med        ISSN: 0037-9727


  2 in total

1.  Bovine growth hormone induces oscillations in cytosolic free Ca2+ in single rat hepatocytes.

Authors:  I Marrero; A K Green; P H Cobbold; C J Dixon
Journal:  Biochem J       Date:  1996-01-15       Impact factor: 3.857

2.  MSM enhances GH signaling via the Jak2/STAT5b pathway in osteoblast-like cells and osteoblast differentiation through the activation of STAT5b in MSCs.

Authors:  Youn Hee Joung; Eun Joung Lim; Pramod Darvin; So Chung Chung; Ju Woong Jang; Kyung Do Park; Hak Kyo Lee; Heui Soo Kim; Taekyu Park; Young Mok Yang
Journal:  PLoS One       Date:  2012-10-11       Impact factor: 3.240

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.