Protein kinase C-mediated down-regulation of MDR3 mRNA expression in Chang liver cells11Abbreviations: MDR, multidrug resistance; P-gp, P-glycoprotein; PCR, polymerase chain reaction; PMA, phorbol 12-myristate 13-acetate; 4α-PDD, 4α-phorbol 12,13-didecanoate; and PKC, protein kinase C.

2001 ◽  
Vol 61 (11) ◽  
pp. 1339-1345
Author(s):  
Shinya Wakusawa∗ ◽  
Ritsuko Ikeda ◽  
Yuhta Shiono ◽  
Hisao Hayashi
Keyword(s):  
Polymerase Chain Reaction ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Chain Reaction ◽  
Kinase C ◽  
P Glycoprotein ◽  
Pkc Protein Kinase C ◽  
Polymerase Chain ◽  
Chang Liver ◽  
Mdr Multidrug Resistance

scholarly journals Identification of specific sites in human P-glycoprotein phosphorylated by protein kinase C.

1993 ◽  
Vol 268 (7) ◽  
pp. 4592-4595 ◽  
Author(s):  
T.C. Chambers ◽  
J. Pohl ◽  
R.L. Raynor ◽  
J.F. Kuo
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Kinase C ◽  
P Glycoprotein

scholarly journals Protein kinase C regulation of p-glycoprotein-mediated xenobiotic secretion in renal proximal tubule

1998 ◽  
Vol 275 (5) ◽  
pp. F785-F795 ◽  
Author(s):  
David S. Miller ◽  
Caroline R. Sussman ◽  
J. Larry Renfro
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Proximal Tubule ◽  
Kinase Inhibitors ◽  
Primary Cultures ◽  
Renal Proximal Tubule ◽  
Protein Kinase Inhibitors ◽  
Drug Accumulation ◽  
Kinase C ◽  
P Glycoprotein

Fluorescence microscopy, fluorescent substrates [daunomycin and a fluorescent cyclosporin A (CSA) derivative] and digital image analysis were used to examine the role of protein kinase C (PKC) in the control of p-glycoprotein in killifish renal proximal tubules. PKC activators, phorbol ester (phorbol 12-myristate 13-acetate, PMA) and dioctylglycerol, reduced luminal drug accumulation, and protein kinase inhibitors, staurosporine and 1-(5-isoquinolinylsulfonyl)-2-methylpiperazine (H-7), increased luminal accumulation; a PMA analog that does not activate PKC was without effect. PMA effects were blocked by staurosporine. The increase in luminal fluorescence caused by staurosporine was blocked by the p-glycoprotein substrate, CSA, indicating that this component of transport was indeed mediated by p-glycoprotein. Neither PMA, dioctylglycerol, nor protein kinase inhibitors altered cellular drug accumulation. Finally, in primary cultures of flounder proximal tubule cells, PMA decreased transepithelial [3H]daunomycin secretion. This pharmacological approach demonstrates that in teleost renal proximal tubule, p-glycoprotein-mediated xenobiotic secretion is negatively correlated with changes in PKC activity, a finding that conflicts with results from studies using mammalian tumor cells that express p-glycoprotein.

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.

Regulation of exocytosis by protein kinase C

2005 ◽  
Vol 33 (6) ◽  
pp. 1341-1344 ◽  
Author(s):  
A. Morgan ◽  
R.D. Burgoyne ◽  
J.W. Barclay ◽  
T.J. Craig ◽  
G.R. Prescott ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Types ◽  
Neuroendocrine Cells ◽  
Protein Targets ◽  
Site Specific ◽  
Regulated Exocytosis ◽  
Kinase C ◽  
Pkc Protein Kinase C

PKC (protein kinase C) has been known for many years to modulate regulated exocytosis in a wide variety of cell types. In neurons and neuroendocrine cells, PKC regulates several different stages of the exocytotic process, suggesting that these multiple actions of PKC are mediated by phosphorylation of distinct protein targets. In recent years, a variety of exocytotic proteins have been identified as PKC substrates, the best characterized of which are SNAP-25 (25 kDa synaptosome-associated protein) and Munc18. In the present study, we review recent evidence suggesting that site-specific phosphorylation of SNAP-25 and Munc18 by PKC regulates distinct stages of exocytosis.

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