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G-protein and tyrosine kinase receptor cross-talk in rat aortic smooth muscle cells: thrombin- and angiotensin II-induced tyrosine phosphorylation of insulin receptor substrate-1 and insulin-like growth factor 1 receptor.

Authors: Du, J  Sperling, LS  Marrero, MB  Phillips, L  Delafontaine, P 
Citation: Du J, etal., Biochem Biophys Res Commun. 1996 Jan 26;218(3):934-9.
Pubmed: (View Article at PubMed) PMID:8579617
DOI: Full-text: DOI:10.1006/bbrc.1996.0165

Insulin-like growth factor I is an autocrine/paracrine factor for vascular smooth muscle cells and is required for angiotensin II- and thrombin-induced mitogenesis. The insulin-like growth factor I-triggered signaling pathway involves autophosphorylation of the beta-subunit of its tyrosine kinase receptor and phosphorylation of insulin receptor substrate-1, the latter providing binding sites for proteins with src homology-2 domains. In rat aortic smooth muscle cells we observed that both angiotensin II and thrombin induced rapid tyrosine phosphorylation of insulin receptor substrate-1. Our results also demonstrated that these mitogens rapidly stimulated phosphorylation of the insulin-like growth factor 1 receptor beta-chain. These data demonstrate a novel interaction between the G-protein coupled angiotensin II and thrombin receptors and the tyrosine-kinase insulin-like growth factor I receptor.

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CRRD Object Information
CRRD ID: 10046011
Created: 2015-07-01
Species: All species
Last Modified: 2015-07-01
Status: ACTIVE



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