Protein kinase C ? nuclear translocation mediates the occurrence of radioresistance in friend erythroleukemia cells

2002 ◽  
Vol 88 (1) ◽  
pp. 144-151 ◽  
Author(s):  
A. Cataldi ◽  
L. Centurione ◽  
R. Di Pietro ◽  
M. Rapino ◽  
D. Bosco ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Nuclear Translocation ◽  
Kinase C ◽  
Erythroleukemia Cells ◽  
Friend Erythroleukemia Cells

Protein kinase C β from Friend erythroleukemia cells is associated with chromatin and DNA

1995 ◽  
Vol 151 (2) ◽  
pp. 107-111 ◽  
Author(s):  
Conrad M. Mallia ◽  
James R. Jeter ◽  
Alan P. Fields ◽  
Russell B. Wilson ◽  
Barbara S. Beckman
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Kinase C ◽  
Erythroleukemia Cells ◽  
Friend Erythroleukemia Cells

Subnanomolar concentration of VIP induces the nuclear translocation of protein kinase C in neonatal rat cortical astrocytes

1994 ◽  
Vol 39 (4) ◽  
pp. 355-363 ◽  
Author(s):  
Z. Oláh ◽  
Cs. Lehel ◽  
W. B. Anderson ◽  
D. E. Brenneman ◽  
D. v. Agoston
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Nuclear Translocation ◽  
Neonatal Rat ◽  
Kinase C ◽  
Cortical Astrocytes

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.

Inhibition of T cell apoptosis by IFN-β rapidly reverses nuclear translocation of protein kinase C-δ

1999 ◽  
Vol 29 (8) ◽  
pp. 2603-2612 ◽  
Author(s):  
Dagmar Scheel-Toellner ◽  
Darrell Pilling ◽  
Arne N. Akbar ◽  
Deborah Hardie ◽  
Giovanna Lombardi ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
T Cell ◽  
Protein Kinase ◽  
Cell Apoptosis ◽  
Nuclear Translocation ◽  
T Cell Apoptosis ◽  
Kinase C

Nuclear localization of protein kinase C-α induces thyroid hormone receptor-α1 expression in the cardiomyocyte

2006 ◽  
Vol 290 (1) ◽  
pp. H381-H389 ◽  
Author(s):  
Agnes Kenessey ◽  
Elizabeth Ann Sullivan ◽  
Kaie Ojamaa
Keyword(s):  
Protein Kinase C ◽  
Thyroid Hormone ◽  
Protein Kinase ◽  
Nuclear Localization ◽  
Hormone Receptor ◽  
Nuclear Translocation ◽  
Thyroid Hormone Receptor ◽  
Neonatal Rat ◽  
Cardiac Phenotype ◽  
Kinase C

Maladaptive cardiac hypertrophy results in phenotypic changes in several genes that are thyroid hormone responsive, suggesting that thyroid hormone receptor (TR) function may be altered by cellular kinases, including protein kinase C (PKC) isozymes that are activated in pathological hypertrophy. To investigate the role of PKC signaling in regulating TR function, cultured neonatal rat ventricular myocytes were transduced with adenovirus (Ad) expressing wild-type (wt) or kinase-inactive (dn) PKCα or constitutively active (ca) PKCδ and PKCε. Overexpression of wtPKCα, but not caPKCδ or caPKCε, induced a 28-fold increase ( P < 0.001) in TRα1 protein in the nuclear compartment and a smaller increase in the cytosol. Furthermore, TRα1 mRNA was increased 55-fold ( P < 0.001). This effect of PKCα was dependent on its kinase activity because dnPKCα was without effect. Phorbol 12-myristate 13-acetate (PMA) induced nuclear translocation of endogenous PKCα and Ad-wtPKCα concomitantly with an increase in nuclear TRα1 protein. In contrast, PMA-induced nuclear translocation of dnPKCα resulted in a decrease of TRα1. The increase in TRα1 protein in Ad-wtPKCα-transduced cardiomyocytes was not the result of a reduced rate of protein degradation, nor was the half-life of TRα1 mRNA prolonged, suggesting a PKCα-mediated effect on TRα transcription. Although phosphorylation of ERK1/2 was increased in Ad-wtPKCα-transduced cells, inhibition of phospho-ERK did not change TRα1 expression. PKCα overexpression in cardiomyocytes caused marked repression of triiodothyronine (T3)-responsive genes, α-myosin heavy chain, and the sarcoplasmic reticulum calcium-activated adenosinetriphosphatase SERCA2. Treatment with T3 for 4 h resulted in significant reductions of PKCα in nuclear and cytosolic compartments, and decreased TRα1 mRNA and protein, with normalization of phenotype. These results implicate PKCα as a regulator of TR function and suggest that nuclear localization of PKCα may control transcription of the TRα gene, and consequently, affect cardiac phenotype.

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