scholarly journals Cellular control of renin secretion

1999 ◽  
Vol 202 (3) ◽  
pp. 219-225
Author(s):  
A. Kurtz ◽  
C. Wagner
Keyword(s):  
Protein Kinase ◽  
Inhibitory Action ◽  
Second Messengers ◽  
Present Knowledge ◽  
Renin Secretion ◽  
Protein Kinase G ◽  
Juxtaglomerular Cells ◽  
Kinase C ◽  
Cl Channels ◽  
Cellular Control

Renin secretion at the level of renal juxtaglomerular cells appears to be controlled mainly by classic second messengers such as Ca2+, cyclic AMP and cyclic GMP, which in turn exert their effects through oppositely acting protein kinases and probably also by affecting the activity of ion channels in the plasma membrane. Thus, protein kinase A stimulates renin secretion, whilst protein kinase C and protein kinase G II inhibit renin secretion. Moreover, Cl- channels could be involved in the mediation of the inhibitory action of Ca2+ on renin secretion. This review summarizes our present knowledge about the possible actions of these kinases in renal juxtaglomerular cells and considers pathways in the organ control of renin secretion.

Cytochrome P-450 metabolites in endothelin-stimulated cardiac hormone secretion

2004 ◽  
Vol 286 (5) ◽  
pp. R888-R893 ◽  
Author(s):  
Sook Jeong Lee ◽  
Carol S. Landon ◽  
Stanley J. Nazian ◽  
John R. Dietz
Keyword(s):  
Protein Kinase ◽  
Inhibitory Action ◽  
Ventricular Myocytes ◽  
Hormone Secretion ◽  
Neonatal Rat ◽  
Kinase C ◽  
Neonatal Rat Ventricular Myocytes ◽  
Cytochrome P 450 ◽  
Kinase A

We examined the role of cytochrome P-450-arachidonate (CYP450-AA) metabolites in endothelin-1 (ET-1)-stimulated atrial natriuretic peptide (ANP) and pro-ANP-(1-30) secretion from the heart. 17-Octadecynoic acid (17-ODYA, 10-5 M) significantly inhibited ANP secretion stimulated by ET-1 (10-8 M) in the isolated perfused rat atria and inhibited pro-ANP-(1-30) secretion stimulated by ET-1 (10-8 M) or 20-hydroxyeicosatetraenoic acid in cultured neonatal rat ventricular myocytes (NRVM). In NRVM, 17-ODYA significantly ( P < 0.05) increased secretion of cAMP but had no significant effect on the secretion of cGMP from NRVM. Staurosporine, an inhibitor of protein kinase C, completely blocked the inhibitory action of 17-ODYA, whereas a protein kinase A inhibitor, H-89 (5 × 10-5 M), did not significantly attenuate the effects of 17-ODYA. The results show that the inhibitory action of 17-ODYA on ET-1-augmented ANP secretion is mediated through cAMP and suggest that CYP450-AA may play an important role in ET-1-induced cardiac hormone secretion.

Do Calcium-Activated Chloride Channels Control Renin Secretion?

Physiology ◽  
1990 ◽  
Vol 5 (2) ◽  
pp. 43-46 ◽  
Author(s):  
A Kurtz
Keyword(s):  
Chloride Channels ◽  
Renin Secretion ◽  
Volume Control ◽  
Juxtaglomerular Cells ◽  
Epithelioid Cells ◽  
Intracellular Ca ◽  
Cl Channels

The rate of renin secretion from renal juxtaglomerular epithelioid cells appears to be inversely correlated to intracellular Ca activity. Such a dependency of renin secretion on Ca activity could be controlled by Ca-activated Cl channels that may be involved in the volume control of juxtaglomerular cells.

Lifespan regulation of conventional protein kinase C isotypes

2007 ◽  
Vol 35 (5) ◽  
pp. 1043-1045 ◽  
Author(s):  
D. Carmena ◽  
A. Sardini
Keyword(s):  
Signal Transduction ◽  
Plasma Membrane ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Second Messengers ◽  
Therapeutic Strategies ◽  
Kinase C ◽  
Signalling Network ◽  
Pkc Protein Kinase C ◽  
Lifespan Regulation

Plasma membrane translocation, following allosteric binding of second messengers, initiates the signal transduction process mediated by cPKC [conventional PKC (protein kinase C)] isotypes. Mechanisms regulating the lifespan of the active enzyme such as its phosphorylation, internalization, dephosphorylation and degradation are key elements of the signalling network. The understanding of such mechanisms is essential for the design of therapeutic strategies targeting PKC isoenzymes.

Cyclic GMP and protein kinase G inhibit the quantal transmitter release induced by protein kinase C

1988 ◽  
Vol 4 (3) ◽  
pp. 263-266 ◽  
Author(s):  
Dimitrie D. Brǎnişteanu ◽  
Laurenţiu M. Popescu ◽  
Dumitru D. Brǎnişteanu ◽  
Ion D. Haulicǎ
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cyclic Gmp ◽  
Transmitter Release ◽  
Protein Kinase G ◽  
Kinase C ◽  
Quantal Transmitter Release

Erythropoietin and testicular steroidogenesis: the role of second messengers

1995 ◽  
Vol 132 (1) ◽  
pp. 103-108 ◽  
Author(s):  
Carlo Foresta ◽  
Roberto Mioni ◽  
Paola Bordon ◽  
Francesco Gottardello ◽  
Andrea Nogara ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Leydig Cells ◽  
Second Messengers ◽  
Indirect Evidence ◽  
Calcium Flux ◽  
Dependent Manner ◽  
Kinase C ◽  
Testicular Steroidogenesis

Foresta C, Mioni R, Bordon P, Gottardello F, Nogara A, Rossato M. Erythropoietin and testicular steroidogenesis: the role of second messengers. Eur J Endocrinol 1995;132:103–8. ISSN 0804–4643 It has been demonstrated that erythropoietin (EPO) influences rat and human Leydig cell steroidogenesis, stimulating testosterone production through a direct and specific receptor-mediated mechanism. The aim of this study was to investigate the mechanism by which recombinant human erythropoietin (rHuEPO) exerts its stimulatory effect on rat Leydig cells. Recombinant human EPO did not induce, at any dose tested (10−10 to 10−13 mol/l), an increase in either cAMP or cGMP, suggesting that in Leydig cells the effect of rHuEPO does not involve the adenylate or guanylate–cyclase systems. The role of transmembrane calcium flux in rHuEPO-stimulated steroidogenesis was studied by evaluating the effect of calcium channel blocker, verapamil, and by the 45Ca2+ uptake method. Verapamil did not influence rHuEPO-induced testosterone secretion and rHuEPO did not modify calcium recycling, indicating that calcium transmembrane flux is not involved in the rHuEPO effect. The protein kinase C inhibitor staurosporine (10, 30, 100 and 300 nmol/l) inhibited rHuEPO-stimulated testicular steroidogenesis in a dose-dependent manner. This indirect evidence suggests that the stimulatory effect of rHuEPO on rat Leydig cells may involve protein kinase C activation. Carlo Foresta, Institute of Internal Medicine, Via Ospedale Civile 105, 35128 Padova, Italy

Activation of cellular protein kinase C and mode of inhibitory action of phospholipid-interacting compounds

1985 ◽  
Vol 130 (2) ◽  
pp. 654-661 ◽  
Author(s):  
Yuko Uratsuji ◽  
Hiroyuki Nakanishi ◽  
Yoshihumi Takeyama ◽  
Akira Kishimoto ◽  
Yasutomi Nishizuka
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Inhibitory Action ◽  
Cellular Protein ◽  
Kinase C

Regulation of Renin Secretion and Renin Synthesis by Second Messengers in Isolated Mouse Juxtaglomerular Cells

1991 ◽  
Vol 1 (2) ◽  
pp. 98-110 ◽  
Author(s):  
Roberto Delia Bruna ◽  
Florence Pinet ◽  
Pierre Corvol ◽  
Armin Kurtz
Keyword(s):  
Second Messengers ◽  
Renin Secretion ◽  
Juxtaglomerular Cells ◽  
Renin Synthesis

Protein Kinase C Does Not Mediate the Inhibitory Action of Lead on Vitamin D3-Dependent Production of Osteocalcin in Osteoblastic Bone Cells

2002 ◽  
Vol 178 (2) ◽  
pp. 109-116 ◽  
Author(s):  
Partow Guity ◽  
Michael J. McCabe ◽  
David K. Pitts ◽  
Ronald P. Santini ◽  
Joel G. Pounds
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Vitamin D3 ◽  
Inhibitory Action ◽  
Bone Cells ◽  
Kinase C

Ceramide-induced vasorelaxation An inhibitory action on protein kinase C

1999 ◽  
Vol 33 (5) ◽  
pp. 415-421 ◽  
Author(s):  
Douglas G. Johns ◽  
Jong-Shiaw Jin ◽  
Dixon W. Wilde ◽  
R.Clinton Webb
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Inhibitory Action ◽  
Kinase C
Sign in / Sign up

Export Citation Format

Share Document