Selective activation of rabbit ovarian protein kinase isozymes in rabbit ovarian follicles and corpora lutea.
作者： M. Hunzicker-Dunn
DOI: 10.1016/S0021-9258(18)43251-6
关键词: Human chorionic gonadotropin 、 Isozyme 、 Endocrinology 、 In vitro 、 Enzyme 、 Intracellular 、 Internal medicine 、 Estrous cycle 、 In vivo 、 Biology 、 Protein kinase A
摘要: The magnitude of activation the type I and II forms cAMP-dependent protein kinase was investigated in estrous follicles corpora lutea (CL) obtained from ovaries control rabbits injected acutely with human chorionic gonadotropin (hCG). To this end, a chromatographic technique which permitted quantitative evaluation vivo activational state two cAmP-dependent developed verified. Results revealed that untreated rabbits, 15% soluble kinase, all exists as isozyme, is activated. Intravenous administration single bolus hCG promoted concentration-dependent (in 10 min) isozyme. In CL control, 4-day pseudopregnant 32% total form 68% form. Both types are approximately 10% dissociated rabbits. Upon intravenous hCG, only further activated min). Dissociation dependent upon time concentration hCG. Preferential also demonstrable vitro studies using exogenous cAMP. These data suggest physiological intracellular mediator acute cAMP-regulated, hCG-triggered functions rabbit ovarian isozyme while it enzyme
sci-hub.st 参考文章(47)
H.R. LINDNER, A. TSAFRIRI, U. ZOR, Y. KOCH, S. BAUMINGER, A. BARNEA, M.E. LIEBERMAN, Gonadotropin action on cultured Graafian follicles: induction of maturation division of the mammalian oocyte and differentiation of the luteal cell. Recent Progress in Hormone Research. ,vol. 30, pp. 79- 138 ,(1974) , 10.1016/B978-0-12-571130-2.50007-9
S S Taylor, M J Zoller, A R Kerlavage, Structural comparisons of cAMP-dependent protein kinases I and II from porcine skeletal muscle. Journal of Biological Chemistry. ,vol. 254, pp. 2408- 2412 ,(1979) , 10.1016/S0021-9258(17)30237-5
W.K. Palmer, J.M. McPherson, D.A. Walsh, Critical controls in the evaluation of cAMP-dependent protein kinase activity ratios as indices of hormonal action. Journal of Biological Chemistry. ,vol. 255, pp. 2663- 2666 ,(1980) , 10.1016/S0021-9258(19)85786-1
J.S. Hayes, L.L. Brunton, S.E. Mayer, Selective activation of particulate cAMP-dependent protein kinase by isoproterenol and prostaglandin E1. Journal of Biological Chemistry. ,vol. 255, pp. 5113- 5119 ,(1980) , 10.1016/S0021-9258(19)70757-1
J D Corbin, S L Keely, C R Park, The distribution and dissociation of cyclic adenosine 3':5'-monophosphate-dependent protein kinases in adipose, cardiac, and other tissues. Journal of Biological Chemistry. ,vol. 250, pp. 218- 225 ,(1975) , 10.1016/S0021-9258(19)42003-6
E W Gerner, M Costa, D H Russell, Cell cycle-specific activity of type I and type II cyclic adenosine 3':5'-monophosphate-dependent protein kinases in Chinese hamster ovary cells. Journal of Biological Chemistry. ,vol. 251, pp. 3313- 3319 ,(1976) , 10.1016/S0021-9258(17)33439-7
P C Lee, D Radloff, J S Schweppe, R A Jungmann, Testicular protein kinases. Characterization of multiple forms and ontogeny. Journal of Biological Chemistry. ,vol. 251, pp. 914- 921 ,(1976) , 10.1016/S0021-9258(17)33780-8
J D Corbin, S L Keely, Characterization and regulation of heart adenosine 3':5'-monophosphate-dependent protein kinase isozymes. Journal of Biological Chemistry. ,vol. 252, pp. 910- 918 ,(1977) , 10.1016/S0021-9258(19)75184-9
James P. Harwood, Maria L. Dufau, Marco Conti, Kevin J. Catt, Regulation of Luteinizing Hormone Receptors and Adenylate Cyclase Activity by Gonadotrophin in the Rat Ovary Molecular Pharmacology. ,vol. 13, pp. 1024- 1032 ,(1977)
P H Sugden, L A Holladay, E M Reimann, J D Corbin, Purification and characterization of the catalytic subunit of adenosine 3':5'-cyclic monophosphate-dependent protein kinase from bovine liver Biochemical Journal. ,vol. 159, pp. 409- 422 ,(1976) , 10.1042/BJ1590409