Protein kinase C-mediated phosphorylation in intact cells

作者: Lee A. Witters , Perry J. Blackshear

DOI: 10.1016/0076-6879(87)41087-2

关键词:

摘要: Publisher Summary The calcium- and phospholipid-dependent protein kinase (protein C) is widely distributed in the tissues of mammals other organisms. Diacylglycerol greatly increases affinity for both calcium phospholipid. Agonist-induced turnover membrane inositol phospholipid taken as evidence potential C activation. Based on this criterion alone, activation suggested to be involved signal transducing cascade several agonists, such thyrotropin-releasing hormone. This chapter describes application four techniques that are applied a variety cell systems address these criteria. These include use phorbol esters diacylglycerols modulate intracellular C, description ubiquitous phosphoprotein serves an important reporter intact cells, creation cells deficient assay permits measurement activity crude tissue extracts.

参考文章(42)
B Glynn, J Colliton, J McDermott, L A Witters, Assay of protein kinase C with an N-bromosuccinimide-cleavage fragment of histone H1. Biochemical Journal. ,vol. 231, pp. 489- 492 ,(1985) , 10.1042/BJ2310489
R Ballester, O M Rosen, Fate of immunoprecipitable protein kinase C in GH3 cells treated with phorbol 12-myristate 13-acetate. Journal of Biological Chemistry. ,vol. 260, pp. 15194- 15199 ,(1985) , 10.1016/S0021-9258(18)95721-2
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
A. Kishimoto, Y. Takai, T. Mori, U. Kikkawa, Y. Nishizuka, Activation of calcium and phospholipid-dependent protein kinase by diacylglycerol, its possible relation to phosphatidylinositol turnover. Journal of Biological Chemistry. ,vol. 255, pp. 2273- 2276 ,(1980) , 10.1016/S0021-9258(19)85886-6
D K Werth, I Pastan, Vinculin phosphorylation in response to calcium and phorbol esters in intact cells. Journal of Biological Chemistry. ,vol. 259, pp. 5264- 5270 ,(1984) , 10.1016/S0021-9258(17)42984-X
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
J G Hovis, D J Stumpo, D L Halsey, P J Blackshear, Effects of Mitogens on Ornithine Decarboxylase Activity and Messenger RNA Levels in Normal and Protein Kinase C-deficient NIH-3T3 Fibroblasts* Journal of Biological Chemistry. ,vol. 261, pp. 10380- 10386 ,(1986) , 10.1016/S0021-9258(18)67535-0
R J Davis, B R Ganong, R M Bell, M P Czech, Structural requirements for diacylglycerols to mimic tumor-promoting phobol diester action on the epidermal growth factor receptor. Journal of Biological Chemistry. ,vol. 260, pp. 5315- 5322 ,(1985) , 10.1016/S0021-9258(18)89024-X
C Cochet, G N Gill, J Meisenhelder, J A Cooper, T Hunter, C-kinase phosphorylates the epidermal growth factor receptor and reduces its epidermal growth factor-stimulated tyrosine protein kinase activity. Journal of Biological Chemistry. ,vol. 259, pp. 2553- 2558 ,(1984) , 10.1016/S0021-9258(17)43389-8