Protein kinase C isozyme distribution and down-regulation in relation to insulin-stimulated c-fos induction.
作者： D J Stumpo , P J Blackshear , D M Haupt
DOI: 10.1016/S0021-9258(17)31946-4
关键词:
摘要: Insulin can stimulate the expression of c-fos and other immediate early genes in many insulin-sensitive cell types. We found previously that this effect insulin was essentially normal cells which protein kinase C (PKC) down-regulated by 16 h exposure to microM phorbol 12-myristate 13-acetate (PMA). However, recent studies groups have suggested much response lost at least part remaining could be due a species PKC beta is resistant down-regulation. To resolve these discrepancies, we performed enzyme assays immunoblots on HIRc-B, H4IIEC3, BC3H-1 before after down-regulation with PMA. activity undetectable first two types down-regulation; addition, all three expressed isozymes than zeta were completely PMA exposure. Neither 1 nor 2 any cells, as determined immunoblotting isotype-specific antibodies. As our previous studies, c-Fos mRNA accumulation HIRc-B H4IIEC3 whereas re-added abolished. not PMA; considerations leave open possibility "atypical" isotypes play role action.
sci-hub.st 参考文章(36)
P J Blackshear, L A Witters, P R Girard, J F Kuo, S N Quamo, Growth factor-stimulated protein phosphorylation in 3T3-L1 cells. Evidence for protein kinase C-dependent and -independent pathways. Journal of Biological Chemistry. ,vol. 260, pp. 13304- 13315 ,(1985) , 10.1016/S0021-9258(17)38870-1
H. Nakanishi, K.A. Brewer, J.H. Exton, Activation of the zeta isozyme of protein kinase C by phosphatidylinositol 3,4,5-trisphosphate. Journal of Biological Chemistry. ,vol. 268, pp. 13- 16 ,(1993) , 10.1016/S0021-9258(18)54107-7
K.A. Heidenreich, S.P. Toledo, L.L. Brunton, M.J. Watson, S. Daniel-Issakani, B. Strulovici, Insulin stimulates the activity of a novel protein kinase C, PKC-epsilon, in cultured fetal chick neurons. Journal of Biological Chemistry. ,vol. 265, pp. 15076- 15082 ,(1990) , 10.1016/S0021-9258(18)77225-6
C Borner, S.N. Guadagno, W.W. Hsiao, D Fabbro, M Barr, I.B. Weinstein, Expression of four protein kinase C isoforms in rat fibroblasts. Differential alterations in ras-, src-, and fos-transformed cells. Journal of Biological Chemistry. ,vol. 267, pp. 12900- 12910 ,(1992) , 10.1016/S0021-9258(18)42360-5
D.L. Halsey, P.R. Girard, J.F. Kuo, P.J. Blackshear, Protein kinase C in fibroblasts. Characteristics of its intracellular location during growth and after exposure to phorbol esters and other mitogens. Journal of Biological Chemistry. ,vol. 262, pp. 2234- 2243 ,(1987) , 10.1016/S0021-9258(18)61644-8
D J Stumpo, P J Blackshear, Cellular expression of mutant insulin receptors interferes with the rapid transcriptional response to both insulin and insulin-like growth factor I. Journal of Biological Chemistry. ,vol. 266, pp. 455- 460 ,(1991) , 10.1016/S0021-9258(18)52456-X
D A McClain, H Maegawa, J Lee, T J Dull, A Ulrich, J M Olefsky, A mutant insulin receptor with defective tyrosine kinase displays no biologic activity and does not undergo endocytosis. Journal of Biological Chemistry. ,vol. 262, pp. 14663- 14671 ,(1987) , 10.1016/S0021-9258(18)47847-7
D H Spach, R A Nemenoff, P J Blackshear, Protein phosphorylation and protein kinase activities in BC3H-1 myocytes. Differences between the effects of insulin and phorbol esters. Journal of Biological Chemistry. ,vol. 261, pp. 12750- 12753 ,(1986) , 10.1016/S0021-9258(18)67156-X
S N Guadagno, C Borner, I B Weinstein, Altered regulation of a major substrate of protein kinase C in rat 6 fibroblasts overproducing PKC beta I. Journal of Biological Chemistry. ,vol. 267, pp. 2697- 2707 ,(1992) , 10.1016/S0021-9258(18)45936-4
W S Lai, D J Stumpo, P J Blackshear, Rapid insulin-stimulated accumulation of an mRNA encoding a proline-rich protein. Journal of Biological Chemistry. ,vol. 265, pp. 16556- 16563 ,(1990) , 10.1016/S0021-9258(17)46259-4