Dependence of soluble guanylyl cyclase activity on calcium signaling in pituitary cells

被引:26
作者
Andric, SA [1 ]
Kostic, TS [1 ]
Tomic, M [1 ]
Koshimizu, T [1 ]
Stojilkovic, SS [1 ]
机构
[1] NICHD, Sect Cellular Signalling, ERRB, NIH, Bethesda, MD 20892 USA
关键词
D O I
10.1074/jbc.M004406200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The role of nitric oxide (NO) in the stimulation of soluble guanylyl cyclase (sGC) is well established, but the mechanism by which the enzyme is inactivated during the prolonged NO stimulation has not been characterized. In this paper we studied the interactions between NO and intracellular Ca2+ in the control of sGC in rat anterior pituitary cells. Experiments were done in cultured cells, which expressed neuronal and endothelial NO synthases, and in cells with elevated NO levels induced by the expression of inducible NO synthase and by the addition of several NO donors. Basal sGC-dependent cGMP production was stimulated by the increase in NO levels in a time-dependent manner. In contrast, depolarization of cells by high K+ and Bay K 8644, an L-type Ca2+ channel agonist, inhibited sGC activity. Depolarization-induced down-regulation of sGC activity was also observed in cells with inhibited cGMP-dependent phosphodiesterases but not in cells bathed in Ca2+ deficient medium. This inhibition was independent from the pattern of Ca2+ signaling (oscillatory versus nonoscillatory) and NO levels, and was determined by averaged concentration of intracellular Ca2+. These results indicate that inactivation of sGC by intracellular Ca2+ serves as a negative feedback to break the stimulatory action of NO on enzyme activity in intact pituitary cells.
引用
收藏
页码:844 / 849
页数:6
相关论文
共 47 条
[1]   CYCLIC-NUCLEOTIDE PHOSPHODIESTERASES - FUNCTIONAL IMPLICATIONS OF MULTIPLE ISOFORMS [J].
BEAVO, JA .
PHYSIOLOGICAL REVIEWS, 1995, 75 (04) :725-748
[2]  
BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
[3]   Endothelial nitric-oxide synthase (type III) is activated and becomes calcium independent upon phosphorylation by cyclic nucleotide-dependent protein kinases [J].
Butt, E ;
Bernhardt, M ;
Smolenski, A ;
Kotsonis, P ;
Fröhlich, LG ;
Sickmann, A ;
Meyer, HE ;
Lohmann, SM ;
Schmidt, HHHW .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (07) :5179-5187
[4]   Involvement of phosphodiesterase-cGMP-PKG pathway in intracellular Ca2+ oscillations in pituitary GH3 cells [J].
Cataldi, M ;
Secondo, A ;
D'Alessio, A ;
Sarnacchiaro, F ;
Colao, AM ;
Amoroso, S ;
Di Renzo, GF ;
Annunziato, L .
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, 1999, 1449 (02) :186-193
[5]   Nitric oxide pumps up calcium signalling [J].
Charles, A .
NATURE CELL BIOLOGY, 1999, 1 (08) :E193-E195
[6]   L-type Ca2+ channels and K+ channels specifically modulate the frequency and amplitude of spontaneous Ca2+ oscillations and have distinct roles in prolactin release in GH3 cells [J].
Charles, AC ;
Piros, ET ;
Evans, CJ ;
Hales, TG .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (11) :7508-7515
[7]   ADENYLYL CYCLASES AND THE INTERACTION BETWEEN CALCIUM AND CAMP SIGNALING [J].
COOPER, DMF ;
MONS, N ;
KARPEN, JW .
NATURE, 1995, 374 (6521) :421-424
[8]   Guanylate cyclase and the .NO/cGMP signaling pathway [J].
Denninger, JW ;
Marletta, MA .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 1999, 1411 (2-3) :334-350
[9]   THE HUMAN PHOTORECEPTOR MEMBRANE GUANYLYL CYCLASE, RETGC, IS PRESENT IN OUTER SEGMENTS AND IS REGULATED BY CALCIUM AND A SOLUBLE ACTIVATOR [J].
DIZHOOR, AM ;
LOWE, DG ;
OLSHEVSKAYA, EV ;
LAURA, RP ;
HURLEY, JB .
NEURON, 1994, 12 (06) :1345-1352
[10]   ROLE OF NITRIC-OXIDE IN CONTROL OF PROLACTIN-RELEASE BY THE ADENOHYPOPHYSIS [J].
DUVILANSKI, BH ;
ZAMBRUNO, C ;
SEILICOVICH, A ;
PISERA, D ;
LASAGA, M ;
DIAZ, MD ;
BELOVA, N ;
RETTORI, V ;
MCCANN, SM .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (01) :170-174