Expression and phosphorylation of insulin receptor substrate 1 during rat liver regeneration

作者: Y. Sasaki , X.F. Zhang , M. Nishiyama , J. Avruch , J.R. Wands

DOI: 10.1016/S0021-9258(18)53541-9

关键词:

摘要: Insulin has been shown to be important for normal liver regeneration occur. The mechanisms whereby insulin may exert its effects on hepatocyte growth, however, are still unknown. rat and human receptor substrate 1 (IRS-1) is a specific target molecule the beta subunit kinase will bind signal transducing molecules containing Src homology 2 domains through multiple tyrosyl phosphorylation (TP) sites. This investigation examined how IRS-1 involved in action during growth induced by two-thirds partial hepatectomy. TP of was strikingly enhanced prior major wave DNA synthesis at 24 h; protein mRNA expression increased parallel lesser extent after subunit, which enhances activity toward IRS-1, association with IRS-1. Finally, phosphatidylinositol 3-kinase, one domains, associated following vivo. These observations suggest that play an role transmitting intracellular regulators growth.

参考文章(29)
Masaki Nishiyama, Jack R. Wands, Cloning and increased expression of an insulin receptor substrate - 1-like gene in human hepatocellular carcinoma Biochemical and Biophysical Research Communications. ,vol. 183, pp. 280- 285 ,(1992) , 10.1016/0006-291X(92)91640-C
A. Ullrich, J. R. Bell, E. Y. Chen, R. Herrera, L. M. Petruzzelli, T. J. Dull, A. Gray, L. Coussens, Y.-C. Liao, M. Tsubokawa, A. Mason, P. H. Seeburg, C. Grunfeld, O. M. Rosen, J. Ramachandran, Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes Nature. ,vol. 313, pp. 756- 761 ,(1985) , 10.1038/313756A0
J Meyerovitch, P Rothenberg, Y Shechter, S Bonner-Weir, C R Kahn, Vanadate normalizes hyperglycemia in two mouse models of non-insulin-dependent diabetes mellitus. Journal of Clinical Investigation. ,vol. 87, pp. 1286- 1294 ,(1991) , 10.1172/JCI115131
Lewis C Cantley, Kurt R Auger, Christopher Carpenter, Brian Duckworth, Andrea Graziani, Rosana Kapeller, Stephen Soltoff, Oncogenes and signal transduction Cell. ,vol. 64, pp. 281- 302 ,(1991) , 10.1016/0092-8674(91)90639-G
E. Fischer, H Charbonneau, N. Tonks, Protein tyrosine phosphatases: a diverse family of intracellular and transmembrane enzymes Science. ,vol. 253, pp. 401- 406 ,(1991) , 10.1126/SCIENCE.1650499
Y. Ebina, E. Araki, M. Taira, F. Shimada, M. Mori, C. S. Craik, K. Siddle, S. B. Pierce, R. A. Roth, W. J. Rutter, Replacement of lysine residue 1030 in the putative ATP-binding region of the insulin receptor abolishes insulin- and antibody-stimulated glucose uptake and receptor kinase activity Proceedings of the National Academy of Sciences of the United States of America. ,vol. 84, pp. 704- 708 ,(1987) , 10.1073/PNAS.84.3.704
O. Rosen, After insulin binds. Science. ,vol. 237, pp. 1452- 1458 ,(1987) , 10.1126/SCIENCE.2442814
C. Koch, D Anderson, M. Moran, C Ellis, T Pawson, SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins. Science. ,vol. 252, pp. 668- 674 ,(1991) , 10.1126/SCIENCE.1708916
Kunliang Guan, Steven S Broyles, Jack E Dixon, None, A Tyr/Ser protein phosphatase encoded by vaccinia virus. Nature. ,vol. 350, pp. 359- 362 ,(1991) , 10.1038/350359A0
Xiao Jian Sun, Paul Rothenberg, C. Ronald Kahn, Jonathan M Backer, Eiichi Araki, Peter A Wilden, Deborah A Cahill, Barry J Goldstein, Morris F White, Structure of the insulin receptor substrate IRS-1 defines a unique signal transduction protein. Nature. ,vol. 352, pp. 73- 77 ,(1991) , 10.1038/352073A0