Cell type- and region-specific expression of protein kinase C-substrate mRNAs in the cerebellum of the macaque monkey

2003 ◽  
Vol 467 (2) ◽  
pp. 135-149 ◽  
Author(s):  
Noriyuki Higo ◽  
Takao Oishi ◽  
Akiko Yamashita ◽  
Keiji Matsuda ◽  
Motoharu Hayashi
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Macaque Monkey ◽  
Cell Type ◽  
Specific Expression ◽  
Kinase C

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 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.

scholarly journals Protein kinase C βII regulates Akt phosphorylation on Ser-473 in a cell type- and stimulus-specific fashion. Vol. 279 (2004) 47720-47725

2005 ◽  
Vol 280 (9) ◽  
pp. 8628
Author(s):  
Yuko Kawakami ◽  
Hajime Nishimoto ◽  
Jiro Kitaura ◽  
Mari Maeda-Yamamoto ◽  
Roberta M. Kato ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Type ◽  
Akt Phosphorylation ◽  
Kinase C ◽  
A Cell
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