scholarly journals DNA Binding of TEA/ATTS Domain Factors Is Regulated by Protein Kinase C Phosphorylation in Human Choriocarcinoma Cells

2001 ◽  
Vol 276 (26) ◽  
pp. 23464-23470 ◽  
Author(s):  
Shi-Wen Jiang ◽  
Maoqing Dong ◽  
Miguel A. Trujillo ◽  
Laurence J. Miller ◽  
Norman L. Eberhardt
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Dna Binding ◽  
Kinase C ◽  
Choriocarcinoma Cells ◽  
Human Choriocarcinoma Cells

FGF inactivates myogenic helix-loop-helix proteins through phosphorylation of a conserved protein kinase C site in their DNA-binding domains

Cell ◽  
1992 ◽  
Vol 71 (7) ◽  
pp. 1181-1194 ◽  
Author(s):  
Li Li ◽  
Jumin Zhou ◽  
Guy James ◽  
Robin Heller-Harrison ◽  
Michael P. Czech ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Dna Binding ◽  
Dna Binding Domains ◽  
Helix Loop Helix ◽  
Binding Domains ◽  
Kinase C

scholarly journals Regulation of the Sequence-specific DNA Binding Function of p53 by Protein Kinase C and Protein Phosphatases

1995 ◽  
Vol 270 (10) ◽  
pp. 5405-5411 ◽  
Author(s):  
Ivone Takenaka ◽  
Francine Morin ◽  
Bernd R. Seizinger ◽  
Nikolai Kley
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Dna Binding ◽  
Protein Phosphatases ◽  
Kinase C ◽  
Binding Function

Regulation of 11β-hydroxysteroid dehydrogenase type 2 activity and mRNA in human choriocarcinoma cells

1996 ◽  
Vol 16 (3) ◽  
pp. 269-275 ◽  
Author(s):  
M M Pasquarette ◽  
P M Stewart ◽  
M L Ricketts ◽  
K Imaishi ◽  
J I Mason
Keyword(s):  
Protein Kinase ◽  
Northern Blot Analysis ◽  
Hydroxysteroid Dehydrogenase ◽  
Dependent Manner ◽  
Human Trophoblast ◽  
Kinase C ◽  
Cytotrophoblastic Cell ◽  
Choriocarcinoma Cells ◽  
Human Choriocarcinoma Cells

ABSTRACT The type 2 isoform of 11 β-hydroxysteroid dehydrogenase (11β-HSD2), which catalyzes the conversion of cortisol to hormonally inactive cortisone in man, is principally expressed in the placenta and mineralocorticoid target tissues, kidney and colon. To date, few studies have addressed the regulation of this novel 11β-HSD2 isoform. We have characterized the nature and regulation of the 11β-HSD activity expressed in a human cytotrophoblastic cell line, the JEG-3 choriocarcinoma cell. The 11β-HSD activity in JEG-3 cell homogenates required NAD+ as cofactor with NADP ineffective and demonstrated a high affinity for cortisol (apparent Km 31 nm). Incubation of JEG-3 cells with forskolin and dibutyryl cyclic AMP increased 11β-HSD2 activity several-fold in a time-dependent manner, while treatment with phorbol ester had little, if any, effect on 11β-HSD2 activity. Northern blot analysis of RNA isolated from JEG-3 cells after these treatments demonstrated a marked increase in a 1·9 kb 11β-HSD2 mRNA species in cells treated with forskolin for 24 h. We conclude that 11β-HSD2 is regulated by activation of the protein kinase A pathway, but not the protein kinase C pathway in human choriocarcinoma cells, and that this regulation occurs at a pretranslational level. JEG-3 cells provide an excellent model for further studies on the regulation of 11β-HSD2 gene expression in human trophoblast tissue.

Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity

Cell ◽  
1991 ◽  
Vol 64 (3) ◽  
pp. 573-584 ◽  
Author(s):  
William J. Boyle ◽  
Tod Smeal ◽  
Libert H.K. Defize ◽  
Peter Angel ◽  
James R. Woodgett ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Dna Binding ◽  
Binding Activity ◽  
Dna Binding Activity ◽  
Kinase C
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