Abstract B051: Control of regulatory T (Treg) cell function by protein kinase C-eta (PKCη): A novel target for cancer immunotherapy

2016 ◽  
Author(s):  
Christophe Pedros ◽  
Kok-Fai Kong ◽  
Amnon Altman
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cancer Immunotherapy ◽  
Treg Cell ◽  
Cell Function ◽  
Kinase C ◽  
Novel Target ◽  
Treg Cell Function

Mechanism of Hepatic Heme Oxygenase-1 Induction by Isoflurane

2006 ◽  
Vol 104 (1) ◽  
pp. 101-109 ◽  
Author(s):  
Alexander Hoetzel ◽  
Daniel Leitz ◽  
Rene Schmidt ◽  
Eva Tritschler ◽  
Inge Bauer ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Phospholipase A2 ◽  
Heme Oxygenase ◽  
Kupffer Cell ◽  
Cell Function ◽  
Heme Oxygenase 1 ◽  
Gadolinium Chloride ◽  
Kinase C

Background The heme oxygenase pathway represents a major cell and organ protective system in the liver. The authors recently showed that isoflurane and sevoflurane up-regulate the inducible isoform heme oxygenase 1 (HO-1). Because the activating cascade remained unclear, it was the aim of this study to identify the underlying mechanism of this effect. Methods Rats were anesthetized with pentobarbital intravenously or with isoflurane per inhalation (2.3 vol%). Kupffer cell function was inhibited by dexamethasone or gadolinium chloride. Nitric oxide synthases were inhibited by either N(omega)-nitro-L-arginine methyl ester or S-methyl thiourea. N-acetyl-cysteine served as an antioxidant, and diethyldithiocarbamate served as an inhibitor of cytochrome P450 2E1. Protein kinase C and phospholipase A2 were inhibited by chelerythrine or quinacrine, respectively. HO-1 was analyzed in liver tissue by Northern blot, Western blot, immunostaining, and enzymatic activity assay. Results In contrast to pentobarbital, isoflurane induced HO-1 after 4-6 h in hepatocytes in the pericentral region of the liver. The induction was prevented in the presence of dexamethasone (P < 0.05) and gadolinium chloride (P < 0.05). Inhibition of nitric oxide synthases or reactive oxygen intermediates did not affect isoflurane-mediated HO-1 up-regulation. In contrast, chelerythrine (P < 0.05) and quinacrine (P < 0.05) resulted in a blockade of HO-1 induction. Conclusion The up-regulation of HO-1 by isoflurane in the liver is restricted to parenchymal cells and depends on Kupffer cell function. The induction is independent of nitric oxide or reactive oxygen species but does involve protein kinase C and phospholipase A2.

scholarly journals NF‐κB activation by protein kinase C isoforms and B‐cell function

EMBO Reports ◽  
2003 ◽  
Vol 4 (1) ◽  
pp. 31-36 ◽  
Author(s):  
Jorge Moscat ◽  
María T Diaz‐Meco ◽  
Paul Rennert
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
B Cell ◽  
Cell Function ◽  
B Cell Function ◽  
Kinase C ◽  
Protein Kinase C Isoforms

Two Interacting Signal Transduction Pathways Regulate Collecting Duct Water Transport

Physiology ◽  
1988 ◽  
Vol 3 (6) ◽  
pp. 235-241 ◽  
Author(s):  
Y Ando ◽  
HR Jacobson ◽  
MD Breyer
Keyword(s):  
Signal Transduction ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Cell Function ◽  
Collecting Duct ◽  
Signal Transduction Pathways ◽  
Phosphatidylinositol Bisphosphate ◽  
Kinase C ◽  
Arachidonate Metabolites

Receptor-mediated signal transduction occurs through phosphatidylinositol bisphosphate (PIP2) breakdown and activation of adenylate cyclase interacting to regulate cell function. Current studies suggest that hormone-stimulated PIP2 breakdown modulates the classic cyclic AMP-mediated hydrosmotic action of vasopressin through separate mechanisms attributable to activation of protein kinase C, elevation of intracellular Ca2+ concentration, and generation of arachidonate metabolites.

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.

scholarly journals Protein kinase C and T cell function

1997 ◽  
Vol 1358 (2) ◽  
pp. 113-126 ◽  
Author(s):  
Carolyn Keenan ◽  
Aideen Long ◽  
Dermot Kelleher
Keyword(s):  
Protein Kinase C ◽  
T Cell ◽  
Protein Kinase ◽  
Cell Function ◽  
Kinase C ◽  
T Cell Function

scholarly journals Induction of nitric oxide release by MRC OX-44 (anti-CD53) through a protein kinase C-dependent pathway in rat macrophages.

1994 ◽  
Vol 179 (4) ◽  
pp. 1119-1126 ◽  
Author(s):  
L Boscá ◽  
P A Lazo
Keyword(s):  
Nitric Oxide ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Membrane Proteins ◽  
Signaling Pathways ◽  
Cell Biology ◽  
Cell Function ◽  
Inositol Phosphates ◽  
Nitric Oxide Release ◽  
Kinase C

Many membrane proteins are implicated in the control of cell function by triggering specific signaling pathways. There is a new family of membrane proteins, defined by its structural motifs, which includes several lymphoid antigens, but lacks a function. To study its biological role, we determined which signaling pathways are affected by the CD53 antigen, a prototypic member of this family, in rat macrophages. Activation of CD53 by cross-linking results in an increase in inositol phosphates and diacylglycerol and in Ca2+ mobilization, which are insensitive to pertussis or cholera toxins. There is a translocation of protein kinase C to the membrane accompanied by nitric oxide (NO) release in macrophages. This effect is the result of the expression of the inducible nitric oxide synthase (iNOS), which is dependent on protein kinase C and protein synthesis. These results have linked a new receptor with a specific pathway of NO induction and thus have opened up a novel aspect of NO regulation in cell biology.

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