scholarly journals Inhibitory Effect of Calcium-binding Protein Regucalcin on Protein Kinase C Activity in Rat Renal Cortex Cytosol.

1998 ◽  
Vol 21 (4) ◽  
pp. 315-318 ◽  
Author(s):  
Hideyuki KUROTA ◽  
Masayoshi YAMAGUCHI
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Calcium Binding ◽  
Renal Cortex ◽  
Binding Protein ◽  
Inhibitory Effect ◽  
Calcium Binding Protein ◽  
Kinase C ◽  
Protein Kinase C Activity

Autoregulation of muscarinic and gastrin receptors on gastric parietal cells

1989 ◽  
Vol 256 (2) ◽  
pp. G356-G363 ◽  
Author(s):  
T. Chiba ◽  
S. K. Fisher ◽  
B. W. Agranoff ◽  
T. Yamada
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Parietal Cell ◽  
Phorbol Esters ◽  
Cell Function ◽  
Inhibitory Effect ◽  
Parietal Cells ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Inositol Phospholipids

In previous studies we demonstrated that parietal cell stimulation with gastrin and carbamoylcholine (carbachol) is accompanied by increased turnover of membrane inositol phospholipids. We conducted the present studies to examine whether membrane-associated protein kinase C activity is enhanced as a consequence of these events and to explore the role of this enzyme in regulating parietal cell function. We observed that carbachol and gastrin dose dependently increased membrane-associated protein kinase C activity while histamine did not. Furthermore, compounds such as phorbol esters and diacylglycerol, which are known to be direct stimulants of protein kinase C activity, also stimulated parietal cell aminopyrine uptake. In contrast, the phorbol ester 12-O-tetradecanoylphorbol-13-acetate and the synthetic diacylglycerol 1-oleoyl-2-acetyl-sn-glycerol inhibited both aminopyrine uptake and membrane inositol phospholipid turnover in parietal cells induced by carbachol and gastrin. The inhibitory effect appeared to result from reduction in the quantity of muscarinic and gastrin receptors without alterations in their specific affinities. These data suggest that protein kinase C mediates stimulation of parietal cells by gastrin and carbachol but also activates an autoregulatory mechanism via downregulation of muscarinic and gastrin receptors.

Caerulein-induced NF-κB/Rel activation requires both Ca2+ and protein kinase C as messengers

1999 ◽  
Vol 277 (3) ◽  
pp. G678-G686 ◽  
Author(s):  
Yusuke Tando ◽  
Hana Algül ◽  
Martin Wagner ◽  
Hans Weidenbach ◽  
Guido Adler ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Nuclear Translocation ◽  
Inhibitory Effect ◽  
Binding Activity ◽  
Atpase Inhibitor ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Intracellular Ca ◽  
Iκbα Degradation

The eukaryotic transcription factor NF-κB/Rel is activated by a large variety of stimuli. We have recently shown that NF-κB/Rel is induced during the course of caerulein pancreatitis. Here, we show that activation of NF-κB/Rel by caerulein, a CCK analog, requires increasing intracellular Ca2+ levels and protein kinase C activation. Caerulein induces a dose-dependent increase of nuclear NF-κB/Rel binding activity in pancreatic lobules, which is paralleled by degradation of IκBα. IκBβ was only slightly affected by caerulein treatment. Consistent with an involvement of Ca2+, the endoplasmic reticulum-resident Ca2+-ATPase inhibitor thapsigargin activated NF-κB/Rel in pancreatic lobules. The intracellular Ca2+ chelator TMB-8 prevented IκBα degradation and subsequent nuclear translocation of NF-κB/Rel induced by caerulein. BAPTA-AM was less effective. Cyclosporin A, a Ca2+/calmodulin-dependent protein phosphatase (PP2B) inhibitor, decreased caerulein-induced NF-κB/Rel activation and IκBα degradation. The inhibitory effect of bisindolylmaleimide suggests that protein kinase C activity is also required for caerulein-induced NF-κB/Rel activation. These data suggest that Ca2+- as well as protein kinase C-dependent mechanisms are required for caerulein-induced NF-κB/Rel activation.

scholarly journals Involvement of calcium-sensitive phospholipid-dependent protein kinase in control of acid secretion by isolated rat parietal cells

1985 ◽  
Vol 232 (2) ◽  
pp. 609-611 ◽  
Author(s):  
N G Anderson ◽  
P J Hanson
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Acid Secretion ◽  
Phorbol Esters ◽  
Inhibitory Effect ◽  
Dependent Protein Kinase ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Dependent Protein ◽  
Isolated Rat

The relative potency with which phorbol esters inhibited histamine-stimulated aminopyrine accumulation (an index of acid secretion) paralleled that which has been established for the activation of purified protein kinase C. The inhibitory effect of 1-oleoyl-2-acetylglycerol on aminopyrine accumulation stimulated by various secretagogues was similar to that of 12-O-tetradecanoylphorbol 13-acetate. Protein kinase C activity was present in a parietal-cell-enriched fraction. In conclusion, protein kinase C could be involved in mechanisms regulating gastric acid secretion.

Inhibitory Effect of Annexin V on Protein Kinase C Activity in Mesangial Cell Lysates

1995 ◽  
Vol 232 (3) ◽  
pp. 865-872 ◽  
Author(s):  
Bernard Rothhut ◽  
Thierry Dubois ◽  
Denis Feliers ◽  
Francoise Russo-Marie ◽  
Jean-Paul Oudinet
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Mesangial Cell ◽  
Annexin V ◽  
Inhibitory Effect ◽  
Cell Lysates ◽  
Kinase C ◽  
Protein Kinase C Activity

scholarly journals Granulocyte-macrophage colony-stimulating factor: signals for its mRNA accumulation

Blood ◽  
1989 ◽  
Vol 74 (4) ◽  
pp. 1314-1320 ◽  
Author(s):  
K Yamato ◽  
Z El-Hajjaoui ◽  
JF Kuo ◽  
HP Koeffler
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Binding Protein ◽  
Mesenchymal Cells ◽  
Colony Stimulating Factor ◽  
Gm Csf ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Cellular Pathways ◽  
Stimulating Factor

Abstract Granulocyte-monocyte colony-stimulating factor (GM-CSF) is an important hematopoietic growth factor. Mesenchymal cells produce abundant GM-CSF in response to tumor necrosis factor alpha (TNF). We wished to determine (1) what cellular pathways enhanced levels of GM-CSF mRNA, and (2) if TNF used any of these pathways. Modulation in levels of GM- CSF mRNA in human fibroblasts (WI-38) was studied by using Northern blot analysis. Markedly increased levels of GM-CSF mRNA occurred in these cells after exposure to sodium fluoride (NaF) and the effect of NaF was slightly enhanced by aluminum chloride; these results suggest that accumulation of GM-CSF mRNA can occur by activating a G-binding protein. Stimulators of protein kinase C dramatically increased levels of GM-CSF mRNA; however, blockade of protein kinase C activity did not attenuate accumulation of GM-CSF mRNA stimulated by TNF and NaF. Exposure to ouabain increased levels of GM-CSF mRNA and this effect was prominently enhanced in the presence of low concentrations of extracellular K+ and was almost abolished in high concentrations of extracellular K+. A monovalent ionophore (monensin) also increased levels of GM-CSF mRNA. Both ouabain and monensin can increase intracellular Ca++ concentration (Cai++) through Na+-Ca++ exchange. A calcium channel blocker (diltiazem) blocked the increased levels of GM- CSF mRNA mediated by ouabain, but could not block the stimulation mediated by TNF alpha. Ca++ ionophores also increased levels of GM-CSF mRNA and rapidly increased levels of Cai++. TNF did not increase Cai++ and, moreover, was able to stimulate accumulation of GM-CSF mRNA in the absence of extracellular Ca++. Taken together, we have found that several different cellular pathways can lead to prominent accumulation of GM-CSF mRNA in mesenchymal cells including (1) activation of protein kinase C, (2) increase in Cai++, and (3) stimulation of G-binding protein. Our studies show that TNF appears to increase levels of GM-CSF mRNA independent of protein kinase C activity or levels of Cai++.

FKBP, the binding protein for the immunosuppressive drug, FK-506, is not an inhibitor of protein kinase C activity

1991 ◽  
Vol 180 (2) ◽  
pp. 846-852 ◽  
Author(s):  
John Cryan ◽  
Shirley H.Y. Hung ◽  
Gregory Wiederrecht ◽  
Nolan H. Sigal ◽  
John J. Siekierka
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Binding Protein ◽  
Immunosuppressive Drug ◽  
Fk 506 ◽  
Kinase C ◽  
Protein Kinase C Activity

scholarly journals Lycopene depresses glutamate release through inhibition of voltage-dependent Ca2+ entry and protein kinase C in rat cerebrocortical nerve terminals

2018 ◽  
Vol 96 (5) ◽  
pp. 479-484 ◽  
Author(s):  
Cheng-Wei Lu ◽  
Chi-Feng Hung ◽  
Wei-Horng Jean ◽  
Tzu-Yu Lin ◽  
Shu-Kuei Huang ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Glutamate Release ◽  
Inhibitory Effect ◽  
Nerve Terminals ◽  
Protein Kinase C Inhibitors ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Voltage Dependent ◽  
Intracellular Ca

Lycopene is a natural dietary carotenoid that was reported to exhibit a neuroprotective profile. Considering that excitotoxicity and cell death induced by glutamate are involved in many brain disorders, the effect of lycopene on glutamate release in rat cerebrocortical nerve terminals and the possible mechanism involved in such effect was investigated. We observed here that lycopene inhibited 4-aminopyridine (4-AP)-evoked glutamate release and intrasynaptosomal Ca2+ concentration elevation. The inhibitory effect of lycopene on 4-AP-evoked glutamate release was markedly reduced in the presence of the Cav2.2 (N-type) and Cav2.1 (P/Q-type) channel blocker ω-conotoxin MVIIC, but was insensitive to the intracellular Ca2+-release inhibitors dantrolene and CGP37157. Furthermore, in the presence of the protein kinase C inhibitors GF109203X and Go6976, the action of lycopene on evoked glutamate release was prevented. These results are the first to suggest that lycopene inhibits glutamate release from rat cortical synaptosomes by suppressing presynaptic Ca2+ entry and protein kinase C activity.

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