Erythropoietin increases c-myc mRNA by a protein kinase C-dependent pathway.
作者： A J Sytkowski , S C Bailey , R Spangler
DOI: 10.1016/S0021-9258(17)35223-7
关键词: MAP kinase kinase kinase 、 Cyclin-dependent kinase 2 、 SOCS2 、 MAP2K7 、 ASK1 、 Biochemistry 、 Cell biology 、 Mitogen-activated protein kinase kinase 、 c-Raf 、 Biology 、 Protein kinase A
摘要: The peptide hormone erythropoietin is a major regulator of red blood cell production. While development has been studied intensively, little known about the intracellular signaling events that follow binding to its receptor on target cell. We report here erythropoietin-induced activation immediate early gene c-myc requires protein kinase C and causes rapid phosphorylation substrate, p80. Our results also argue for modulation activity second signal transduction element in addition C.
sci-hub.st 参考文章(40)
C Godson, B A Weiss, P A Insel, Differential activation of protein kinase C alpha is associated with arachidonate release in Madin-Darby canine kidney cells. Journal of Biological Chemistry. ,vol. 265, pp. 8369- 8372 ,(1990) , 10.1016/S0021-9258(19)38894-5
F L Huang, Y Yoshida, J R Cunha-Melo, M A Beaven, K P Huang, Differential down-regulation of protein kinase C isozymes. Journal of Biological Chemistry. ,vol. 264, pp. 4238- 4243 ,(1989) , 10.1016/S0021-9258(19)84988-8
M Faucher, N Gironès, Y A Hannun, R M Bell, R J Davis, Regulation of the epidermal growth factor receptor phosphorylation state by sphingosine in A431 human epidermoid carcinoma cells. Journal of Biological Chemistry. ,vol. 263, pp. 5319- 5327 ,(1988) , 10.1016/S0021-9258(18)60718-5
S Narindrasorasak, A Brickenden, E Ball, B D Sanwal, Regulation of protein kinase C by cyclic adenosine 3':5'-monophosphate and a tumor promoter in skeletal myoblasts. Journal of Biological Chemistry. ,vol. 262, pp. 10497- 10501 ,(1987) , 10.1016/S0021-9258(18)60988-3
H Zhang, N E Buckley, K Gibson, S Spiegel, Sphingosine stimulates cellular proliferation via a protein kinase C-independent pathway. Journal of Biological Chemistry. ,vol. 265, pp. 76- 81 ,(1990) , 10.1016/S0021-9258(19)40197-X
Tatsuya Tamaoki, Hisayo Nomoto, Isami Takahashi, Yuzuru Kato, Makoto Morimoto, Fusao Tomita, Staurosporine, a potent inhibitor of phospholipid/Ca++dependent protein kinase. Biochemical and Biophysical Research Communications. ,vol. 135, pp. 397- 402 ,(1986) , 10.1016/0006-291X(86)90008-2
D Mary, J F Peyron, P Auberger, C Aussel, M Fehlmann, Modulation of T cell activation by differential regulation of the phosphorylation of two cytosolic proteins. Implication of both Ca2+ and cyclic AMP-dependent protein kinases. Journal of Biological Chemistry. ,vol. 264, pp. 14498- 14502 ,(1989) , 10.1016/S0021-9258(18)71706-7
Y A Hannun, C R Loomis, A H Merrill, R M Bell, Sphingosine inhibition of protein kinase C activity and of phorbol dibutyrate binding in vitro and in human platelets Journal of Biological Chemistry. ,vol. 261, pp. 12604- 12609 ,(1986) , 10.1016/S0021-9258(18)67133-9
L A Witters, B P Glynn, L Wen, P J Blackshear, Protein kinase C-stimulated phosphorylation in vitro of a Mr 80,000 protein phosphorylated in response to phorbol esters and growth factors in intact fibroblasts. Distinction from protein kinase C and prominence in brain. Journal of Biological Chemistry. ,vol. 261, pp. 1459- 1469 ,(1986) , 10.1016/S0021-9258(17)36115-X
C R Loomis, R M Bell, Sangivamycin, a Nucleoside Analogue, Is a Potent Inhibitor of Protein Kinase C Journal of Biological Chemistry. ,vol. 263, pp. 1682- 1692 ,(1988) , 10.1016/S0021-9258(19)77930-7