scholarly journals Regulation of cell type specific expression of a putative protein kinase C (pkcA) in Dictyostelium discoideum

2017 ◽  
Vol 145 ◽  
pp. S140-S141
Author(s):  
Umachandran Shalini ◽  
Wasima Mohamed ◽  
Ramamurthy Baskar
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Dictyostelium Discoideum ◽  
Cell Type ◽  
Specific Expression ◽  
Putative Protein ◽  
Kinase C ◽  
Cell Type Specific Expression ◽  
Cell Type Specific ◽  
Putative Protein Kinase

scholarly journals Cell type-specific expression of protein kinase C isozymes in the rabbit cerebellum.

1988 ◽  
Vol 263 (10) ◽  
pp. 4523-4526 ◽  
Author(s):  
H Hidaka ◽  
T Tanaka ◽  
K Onoda ◽  
M Hagiwara ◽  
M Watanabe ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Type ◽  
Specific Expression ◽  
Kinase C ◽  
Cell Type Specific Expression ◽  
Cell Type Specific

scholarly journals The Acidic Region and Conserved Putative Protein Kinase C Phosphorylation Site in Nef Are Important for SIV Replication in Rhesus Macaques

Virology ◽  
1999 ◽  
Vol 257 (1) ◽  
pp. 138-155 ◽  
Author(s):  
Silke Carl ◽  
A.John Iafrate ◽  
Sabine M. Lang ◽  
Christiane Stahl-Hennig ◽  
Eva M. Kuhn ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Rhesus Macaques ◽  
Phosphorylation Site ◽  
Putative Protein ◽  
Kinase C ◽  
Acidic Region ◽  
Putative Protein Kinase

Differential effects of putative protein kinase C inhibitors on contraction of rat aortic smooth muscle

1993 ◽  
Vol 264 (4) ◽  
pp. H1300-H1306 ◽  
Author(s):  
Y. Shimamoto ◽  
H. Shimamoto ◽  
C. Y. Kwan ◽  
E. E. Daniel
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Kinases ◽  
Induced Response ◽  
Dependent Manner ◽  
Contractile Responses ◽  
Putative Protein ◽  
Calphostin C ◽  
Kinase C ◽  
Putative Protein Kinase

We investigated effects of three kinds of putative protein kinase C (PKC) inhibitors, calphostin C, 1-(5-isoquinolinesulfonyl)-2-methylpiperazine (H-7), and stauro-sporine, on aortic muscle contractions induced by KCl, phenylephrine, 12-O-tetradecanoylphorbol-13-acetate (TPA), and phorbol 12, 13-dibutyrate (PDBu). Calphostin C noncompetitively inhibited TPA-induced contractions in a concentration-dependent manner. At 10(-6) M, calphostin C completely abolished responses to TPA and also effectively inhibited PDBu-induced contractions. Such a concentration of calphostin C had no effect on KCl-induced contractions but decreased the maximal tension of phenylephrine-induced response curve by 35.3 +/- 6.6% H-7 (10(-5) M had little effect on TPA-induced contraction but significantly inhibited contractile responses to phenylephrine and KCl. Staurosporine (10(-8) M, 3 x 10(-8) M) inhibited contractile responses to KCl, phenylephrine, and TPA. We suggest that staurosporine and H-7, which are known to act on the catalytic domain of PKC carrying high degree of sequence homology with other protein kinases, are relatively nonselective for PKC. On the other hand, calphostin C acting on the regulatory domain of PKC, which is distinct from other protein kinases, may serve as a relatively more selective PKC inhibitor.

scholarly journals Phospholipase C-eta Enzymes as Putative Protein Kinase C and Ca2+ Signalling Components in Neuronal and Neuroendocrine Tissues

2007 ◽  
Vol 86 (4) ◽  
pp. 243-248 ◽  
Author(s):  
Alan J. Stewart ◽  
Kevin Morgan ◽  
Colin Farquharson ◽  
Robert P. Millar
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phospholipase C ◽  
Putative Protein ◽  
Kinase C ◽  
Putative Protein Kinase

Role of a geminivirus AV2 protein putative protein kinase C motif on subcellular localization and pathogenicity

2008 ◽  
Vol 135 (1) ◽  
pp. 115-124 ◽  
Author(s):  
R.V. Chowda-Reddy ◽  
Fidelis Achenjang ◽  
Christian Felton ◽  
Marie T. Etarock ◽  
Marie-Therese Anangfac ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Subcellular Localization ◽  
Putative Protein ◽  
Kinase C ◽  
Putative Protein Kinase

scholarly journals Gene- and cell-type-specific effects of signal transduction cascades on metal-regulated gene transcription appear to be independent of changes in the phosphorylation of metal-response-element-binding transcription factor-1

2004 ◽  
Vol 382 (1) ◽  
pp. 33-41 ◽  
Author(s):  
Huimin JIANG ◽  
Kai FU ◽  
Glen K. ANDREWS
Keyword(s):  
Transcription Factor ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Kinases ◽  
Cell Type ◽  
Specific Effects ◽  
Kinase C ◽  
Cell Type Specific ◽  
Transcription Factor 1

Post-translational modification of MTF-1 (metal-response-element-binding transcription factor-1) was suggested to play a role in its metalloregulatory functions. In the present study, pulse labelling and two-dimensional electrophoresis–Western blotting were used to demonstrate that, although MTF-1 is highly modified in vivo, its phosphorylation level does not rapidly change in response to metals, nor does its overall modification pattern. Recombinant MTF-1 was found to serve as an in vitro substrate for casein kinase II, c-Jun N-terminal kinase and protein kinase C, but inhibition of these kinases in vivo did not significantly change the modification pattern of MTF-1. Northern blotting revealed that inhibitors of casein kinase II and c-Jun N-terminal kinase severely attenuate the metal-induced transcription of the native chromatin-packaged metallothionein-I and zinc transporter-1 genes, whereas protein kinase C inhibitors exerted gene- and cell-type-specific effects on the metal regulation and basal expression of these two genes. A chromatin immunoprecipitation assay was used to demonstrate that none of these inhibitors prevent the metal-dependent recruitment of MTF-1 to the MT-I promoter. In brief, results of the present study suggest that protein kinases may not alter the phosphorylation state of MTF-1 during the rapid-response phase to metals, nor do they regulate the metal-dependent formation of a stable MTF-1–chromatin complex. Instead, protein kinases may exert their interdependent effects on metal-induced gene expression by acting on cofactors that interact with MTF-1.

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