Induction of c-fos and zif/268 gene expression in rat striatal neurons, following stimulation of D1-like dopamine receptors, involves protein kinase A and protein kinase C

Neuroscience ◽  
1995 ◽  
Vol 68 (1) ◽  
pp. 97-106 ◽  
Author(s):  
C.S. Simpson ◽  
B.J. Morris
Keyword(s):  
Gene Expression ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Dopamine Receptors ◽  
Striatal Neurons ◽  
Kinase C ◽  
Kinase A ◽  
Stimulation Of

Mechanisms of PTH-induced rise in cytosolic calcium in adult rat hepatocytes

1994 ◽  
Vol 267 (5) ◽  
pp. G754-G763 ◽  
Author(s):  
M. Klin ◽  
M. Smogorzewski ◽  
H. Khilnani ◽  
M. Michnowska ◽  
S. G. Massry
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
G Protein ◽  
Cytosolic Calcium ◽  
Amino Terminal ◽  
Kinase C ◽  
Dose Dependent ◽  
Kinase A ◽  
Stimulation Of

Available data indicate that the liver is a target organ for parathyroid hormone (PTH) and that this effect is most likely mediated by PTH-induced calcium entry into hepatocytes. The present study examined the effects of both PTH-(1-84) and its amino-terminal fragment [PTH-(1-34)] on cytosolic calcium concentration ([Ca2+]i) of hepatocytes and explored the cellular pathways that mediate this potential action of PTH. Both moieties of PTH produced a dose-dependent rise in [Ca2+]i, but the effect of PTH-(1-84) was greater (P < 0.01) than an equimolar amount of PTH-(1-34). This effect required calcium in the medium and was totally [PTH-(1-34)] or partially [PTH-(1-84)] blocked by PTH antagonist ([Nle8,18,Tyr34]bPTH-(7-34)-NH2] and by verapamil or nifedipine. Sodium or chloride channel blockers did not modify this effect. 12-O-tetradecanoylphorbol 13-acetate (TPA), an activator of protein kinase C, dibutyryl adenosine 3',5'-cyclic monophosphate (DBcAMP), and G protein activator also produced a dose-dependent rise in [Ca2+]i. Staurosporine abolished the effect of TPA, and both staurosporine and calphostin C partially inhibited the effect of PTH. Staurosporine and verapamil together produced greater inhibition of PTH action than each alone. Rp-cAMP, a competitive inhibitor of cAMP binding to the R subunit of protein kinase A, and N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide (H-89), a protein kinase A inhibitor, blocked the effect of both DBcAMP and PTH, but the effect of these agents was greater (P < 0.01) on DBcAMP action. G protein inhibitor and pertussis toxin partially blocked the action of PTH. The data indicate that 1) PTH increases [Ca2+]i of hepatocytes; 2) this action of the hormone is receptor mediated; 3) the predominant pathway for this PTH action is the stimulation of a G protein-adenylate cyclase-cAMP system, which then leads to stimulation of a calcium transport system inhibitable by verapamil or nifedipine or activation of L-type calcium channels; 4) activation of protein kinase C is also involved; and 5) the PTH-induced rise in [Ca2+]i is due, in major parts, to movement of extracellular calcium into the cell.

scholarly journals Ghrelin induces clock gene expression in the liver of goldfishin vitrovia protein kinase C and protein kinase A pathways

2017 ◽  
Vol 220 (7) ◽  
pp. 1295-1306 ◽  
Author(s):  
Aída Sánchez-Bretaño ◽  
Ayelén M. Blanco ◽  
Ángel L. Alonso-Gómez ◽  
María J. Delgado ◽  
Olivier Kah ◽  
...  
Keyword(s):  
Gene Expression ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Clock Gene ◽  
Clock Gene Expression ◽  
Kinase C ◽  
Kinase A

Distinct voltage-dependent regulation of a heart-delayed IK by protein kinases A and C

1991 ◽  
Vol 261 (6) ◽  
pp. C1081-C1090 ◽  
Author(s):  
K. B. Walsh ◽  
R. S. Kass
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Dependent Protein Kinase ◽  
Kinase C ◽  
Voltage Dependent ◽  
Dependent Protein ◽  
Kinetics Of ◽  
Kinase A ◽  
Stimulation Of

We have investigated the effects of stimulation of adenosine 3',5'-cyclic monophosphate-dependent protein kinase (protein kinase A) and Ca(2+)-diacylglycerol-dependent protein kinase (protein kinase C) on the delayed rectifier K+ current (IK) in guinea pig ventricular cells using a whole cell arrangement of the patch-clamp procedure. Stimulation of either protein kinase C or A resulted in enhanced IK activity. Augmentation of IK observed during stimulation of protein kinase A occurred in a markedly voltage-dependent manner, with the largest increases occurring at potentials near the threshold for IK activation. Enhancement of IK during stimulation of protein kinase C followed a different pattern, with minimal effects of the enzyme near IK threshold. Neither protein kinase A nor C altered the kinetics of IK activation, although both kinases slightly changed the kinetics of deactivation. Both kinases increased IK maximal conductance, but the effects of each kinase on the voltage-dependence of activation differed. Protein kinase A shifted IK activation toward more negative voltages but did not affect the slope of the activation curve. Protein kinase C, in contrast, changed the slope of the IK activation curve, with only a small effect on the half-maximal voltage of activation. These contrasting effects on the voltage dependence of IK activation are consistent with actions of the kinases at distinct sites on or near the IK channel protein.

scholarly journals Stimulation of the ERK Pathway by GTP-loaded Rap1 Requires the Concomitant Activation of Ras, Protein Kinase C, and Protein Kinase A in Neuronal Cells

2002 ◽  
Vol 278 (7) ◽  
pp. 4778-4785 ◽  
Author(s):  
Tristan Bouschet ◽  
Virgili Perez ◽  
Céline Fernandez ◽  
Joël Bockaert ◽  
Alain Eychene ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Neuronal Cells ◽  
Erk Pathway ◽  
Ras Protein ◽  
Kinase C ◽  
Kinase A ◽  
Stimulation Of

scholarly journals Global Profiles of Gene Expression Induced by Adrenocorticotropin in Y1 Mouse Adrenal Cells

Endocrinology ◽  
2006 ◽  
Vol 147 (5) ◽  
pp. 2357-2367 ◽  
Author(s):  
Bernard P. Schimmer ◽  
Martha Cordova ◽  
Henry Cheng ◽  
Andrew Tsao ◽  
Andrew B. Goryachev ◽  
...  
Keyword(s):  
Gene Expression ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Adrenal Cortex ◽  
Structural Integrity ◽  
Adrenal Cells ◽  
Kinase C ◽  
Genome Wide ◽  
Kinase A

ACTH regulates the steroidogenic capacity, size, and structural integrity of the adrenal cortex through a series of actions involving changes in gene expression; however, only a limited number of ACTH-regulated genes have been identified, and these only partly account for the global effects of ACTH on the adrenal cortex. In this study, a National Institute on Aging 15K mouse cDNA microarray was used to identify genome-wide changes in gene expression after treatment of Y1 mouse adrenocortical cells with ACTH. ACTH affected the levels of 1275 annotated transcripts, of which 46% were up-regulated. The up-regulated transcripts were enriched for functions associated with steroid biosynthesis and metabolism; the down- regulated transcripts were enriched for functions associated with cell proliferation, nuclear transport and RNA processing, including alternative splicing. A total of 133 different transcripts, i.e. only 10% of the ACTH-affected transcripts, were represented in the categories above; most of these had not been described as ACTH-regulated previously. The contributions of protein kinase A and protein kinase C to these genome-wide effects of ACTH were evaluated in microarray experiments after treatment of Y1 cells and derivative protein kinase A-defective mutants with pharmacological probes of each pathway. Protein kinase A-dependent signaling accounted for 56% of the ACTH effect; protein kinase C-dependent signaling accounted for an additional 6%. These results indicate that ACTH affects the expression profile of Y1 adrenal cells principally through cAMP- and protein kinase A- dependent signaling. The large number of transcripts affected by ACTH anticipates a broader range of actions than previously appreciated.

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