Regulated expression of the tyrosine hydroxylase gene by membrane depolarization. Identification of the responsive element and possible second messengers.
作者： E.L. Sabban , E.J. Kilbourne , B.B. Nankova , E.J. Lewis , A McMahon
DOI: 10.1016/S0021-9258(18)42553-7
关键词:
摘要: Prolonged depolarization has been used as a model of adaptive changes in the expression various proteins, such ion channels and neurotransmitter biosynthetic enzymes, response to increased trans-synaptic activity nervous system. In depolarized PC12 cells, tyrosine hydroxylase (TH) mRNA levels severalfold (Kilbourne, E. J., Sabban, L. (1990) Mol. Brain Res. 8, 121-127). this study, membrane caused an increase reporter gene chloramphenicol acetyltransferase (CAT), under transcriptional control 5' region rat TH gene. These results indicate that leads transcription Protein kinase C inhibitors had no effect on induction by depolarization, well formation CAT upstream The responsive element was mapped containing cAMP element. This also calcium ionophore, ionomycin. Interestingly, combined treatment with analogs greater than either alone levels, cells transfected plasmid
sci-hub.st 参考文章(53)
S. Vyas, N. Faucon Biguet, J. Mallet, Transcriptional and post-transcriptional regulation of tyrosine hydroxylase gene by protein kinase C. The EMBO Journal. ,vol. 9, pp. 3707- 3712 ,(1990) , 10.1002/J.1460-2075.1990.TB07583.X
Lloyd A. Greene, John M. Aletta, Adriana Rukenstein, Steven H. Green, [18] PC12 pheochromocytoma cells: culture, nerve growth factor treatment, and experimental exploitation Peptide Growth Factors - Part B. ,vol. 147, pp. 207- 216 ,(1987) , 10.1016/0076-6879(87)47111-5
E L Sabban, L A Greene, M Goldstein, Mechanism of biosynthesis of soluble and membrane-bound forms of dopamine beta-hydroxylase in PC12 pheochromocytoma cells. Journal of Biological Chemistry. ,vol. 258, pp. 7812- 7818 ,(1983) , 10.1016/S0021-9258(18)32251-8
M K Stachowiak, H K Jiang, A M Poisner, R K Tuominen, J S Hong, Short and long term regulation of catecholamine biosynthetic enzymes by angiotensin in cultured adrenal medullary cells. Molecular mechanisms and nature of second messenger systems. Journal of Biological Chemistry. ,vol. 265, pp. 4694- 4702 ,(1990) , 10.1016/S0021-9258(19)39618-8
D.D. Ginty, D. Glowacka, D.S. Bader, H. Hidaka, J.A. Wagner, Induction of immediate early genes by Ca2+ influx requires cAMP-dependent protein kinase in PC12 cells. Journal of Biological Chemistry. ,vol. 266, pp. 17454- 17458 ,(1991) , 10.1016/S0021-9258(19)47394-8
F L Hall, P Fernyhough, D N Ishii, P R Vulliet, Suppression of nerve growth factor-directed neurite outgrowth in PC12 cells by sphingosine, an inhibitor of protein kinase C. Journal of Biological Chemistry. ,vol. 263, pp. 4460- 4466 ,(1988) , 10.1016/S0021-9258(18)68948-3
F Hefti, H Gnahn, ME Schwab, H Thoenen, Induction of tyrosine hydroxylase by nerve growth factor and by elevated K+ concentrations in cultures of dissociated sympathetic neurons The Journal of Neuroscience. ,vol. 2, pp. 1554- 1566 ,(1982) , 10.1523/JNEUROSCI.02-11-01554.1982
E J Lewis, A W Tank, N Weiner, D M Chikaraishi, Regulation of tyrosine hydroxylase mRNA by glucocorticoid and cyclic AMP in a rat pheochromocytoma cell line. Isolation of a cDNA clone for tyrosine hydroxylase mRNA. Journal of Biological Chemistry. ,vol. 258, pp. 14632- 14637 ,(1983) , 10.1016/S0021-9258(17)43909-3
Raymond F. Chen, Removal of Fatty Acids from Serum Albumin by Charcoal Treatment Journal of Biological Chemistry. ,vol. 242, pp. 173- 181 ,(1967) , 10.1016/S0021-9258(19)81445-X
M E Greenberg, L A Greene, E B Ziff, Nerve growth factor and epidermal growth factor induce rapid transient changes in proto-oncogene transcription in PC12 cells. Journal of Biological Chemistry. ,vol. 260, pp. 14101- 14110 ,(1985) , 10.1016/S0021-9258(17)38689-1