Regulation of tumor invasion and metastasis in protein kinase C epsilon-transformed NIH3T3 fibroblasts

2002 ◽  
Vol 85 (4) ◽  
pp. 785-797 ◽  
Author(s):  
Souvenir D. Tachado ◽  
Mark W. Mayhew ◽  
Ginger G. Wescott ◽  
Tonia L. Foreman ◽  
Crystal D. Goodwin ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Tumor Invasion ◽  
Invasion And Metastasis ◽  
Kinase C ◽  
Protein Kinase C Epsilon

scholarly journals INHIBITION OF PROTEIN KINASE C EPSILON CAUSES CILIATED BOVINE BRONCHIAL CELL DETACHMENT

2006 ◽  
Vol 32 (8) ◽  
pp. 349-362 ◽  
Author(s):  
Rebecca E. Slager ◽  
Joseph H. Sisson ◽  
Jaqueline A. Pavlik ◽  
Jennifer K. Johnson ◽  
Jeremy R. Nicolarsen ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Detachment ◽  
Kinase C ◽  
Protein Kinase C Epsilon

scholarly journals Protein kinase C epsilon is involved in ionizing radiation induced bystander response in human cells

2009 ◽  
Vol 41 (12) ◽  
pp. 2413-2421 ◽  
Author(s):  
Burong Hu ◽  
Bo Shen ◽  
Yanrong Su ◽  
Charles R. Geard ◽  
Adayabalam S. Balajee
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Ionizing Radiation ◽  
Human Cells ◽  
Kinase C ◽  
Protein Kinase C Epsilon ◽  
Bystander Response ◽  
Radiation Induced

scholarly journals Design and synthesis of protein kinase C epsilon selective diacylglycerol lactones (DAG-lactones)

2015 ◽  
Vol 90 ◽  
pp. 332-341 ◽  
Author(s):  
Jihyae Ann ◽  
Suyoung Yoon ◽  
Jisoo Baek ◽  
Da Hye Kim ◽  
Nancy E. Lewin ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Design And Synthesis ◽  
Kinase C ◽  
Protein Kinase C Epsilon

scholarly journals Protein Kinase C Epsilon Deletion in Adipose Tissue, but Not in Liver, Improves Glucose Tolerance

2019 ◽  
Vol 29 (1) ◽  
pp. 183-191.e7 ◽  
Author(s):  
Amanda E. Brandon ◽  
Bing M. Liao ◽  
Barbara Diakanastasis ◽  
Benjamin L. Parker ◽  
Katy Raddatz ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Glucose Tolerance ◽  
Kinase C ◽  
Protein Kinase C Epsilon

scholarly journals Novel Small-Molecule Inhibitors of Protein Kinase C Epsilon Reduce Ethanol Consumption in Mice

2018 ◽  
Vol 84 (3) ◽  
pp. 193-201 ◽  
Author(s):  
Angelo Blasio ◽  
Jingyi Wang ◽  
Dan Wang ◽  
Florence P. Varodayan ◽  
Matthew B. Pomrenze ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Small Molecule ◽  
Small Molecule Inhibitors ◽  
Ethanol Consumption ◽  
Kinase C ◽  
Protein Kinase C Epsilon

Non-TypeableHaemophilus influenzaeDecreases Cilia Beating Via Protein Kinase C Epsilon.

2009 ◽  
Author(s):  
TA Wyatt ◽  
JH Sisson ◽  
JM DeVasure ◽  
JA Pavlik ◽  
DA Yanov ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Kinase C ◽  
Protein Kinase C Epsilon

Effects of calponin on force generation by single smooth muscle cells

1996 ◽  
Vol 270 (5) ◽  
pp. H1858-H1863 ◽  
Author(s):  
A. Horowitz ◽  
O. Clement-Chomienne ◽  
M. P. Walsh ◽  
T. Tao ◽  
H. Katsuyama ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Smooth Muscle Cells ◽  
Smooth Muscle Cell ◽  
Contractile Force ◽  
Actin Binding ◽  
Aortic Smooth Muscle ◽  
Kinase C ◽  
Protein Kinase C Epsilon

Although the actin-binding and actomyosin adenosinetriphosphatase (ATPase) inhibitory properties of calponin are well documented in vitro, its function in the smooth muscle cell has not been elucidated. To address this question, we utilized the ferret aortic smooth muscle cell, which shows a protein kinase C-dependent contraction even at pCa (-log [Ca2+]) 9.0 in the absence of a change in myosin light chain phosphorylation. Force was recorded from single, briefly permeabilized cells stimulated via a Ca(2+)-independent pathway by either phenylephrine or the epsilon isoenzyme of protein kinase C. Treatment of stimulated cells with wild-type recombinant calponin reduced steady-state contractile force by 45-60%. When calponin application preceded protein kinase C epsilon treatment, contraction was completely suppressed. On the other hand, calponin phosphorylated at Ser175 or mutant calponin with a Ser175 ⇢ Ala replacement had no effect on contractile force. A peptide corresponding to Leu166-Gly194 of calponin, which included an actin-binding domain but excluded the actomyosin ATPase inhibitory region, was synthesized. Treatment of aortic smooth muscle cells with this peptide triggered a concentration-dependent contraction, presumably by alleviating the inhibitory effect of endogenous calponin. A control peptide with a scrambled sequence of the same residues produced no detectable contractile response. Although other interpretations are possible, these results are consistent with the view that calponin participates in thin filament-mediated regulation of smooth muscle contraction and that it may be part of a Ca(2+)-independent pathway downstream of protein kinase C epsilon.

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