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Growth hormone induces tyrosine phosphorylation of annexin I in rat osteosarcoma cells.

Authors: Salles, JP  Netelenbos, JC  Slootweg, MC 
Citation: Salles JP, etal., Endocrinology. 1996 Oct;137(10):4358-62.
Pubmed: (View Article at PubMed) PMID:8828496
DOI: Full-text: DOI:10.1210/endo.137.10.8828496

GH induces phosphorylation of a number of cellular proteins, of which several have now been identified, such as mitogen-activated protein kinase, insulin receptor substrate-1, and members of the JAK kinase and STAT families of proteins. However, other phosphorylated proteins remain unidentified. Growth factors and cytokines, including epidermal growth factor, insulin, pp60v-scr, and angiotensin II, induce a rapid phosphorylation of annexin I, a 35-kDa member of the annexin family of Ca2+ and phospholipid-binding proteins. The osteoblast-like rat osteosarcoma cell-line UMR-106.01, in which GH acts as a mitogen via a high affinity GH receptor, was used as a model for GH-induced protein phosphorylation. It is demonstrated by immunoblotting and immunoprecipitation techniques that GH induces the phosphorylation of annexin I on tyrosine residues. This phosphorylation is dose and time dependent. Induction of annexin I phosphorylation is delayed compared with that of JAK2. These results identify annexin I as a protein that becomes tyrosine phosphorylated under the influence of GH and show that phosphorylation of annexin I is a general phenomenon that follows activation of a cell by hormones or cytokines.


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CRRD Object Information
CRRD ID: 2306953
Created: 2009-05-12
Species: All species
Last Modified: 2009-05-12
Status: ACTIVE


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