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Titolo:
TRANSCRIPTIONAL REGULATION OF THE BOVINE CYP17 GENE BY CAMP
Autore:
LUND J; BAKKE M; MELLGREN G; MOROHASHI KI; DOSKELAND SO;
Indirizzi:
UNIV BERGEN,DEPT ANAT & CELL BIOL,ARSTADVEIEN 19 N-5009 BERGEN NORWAY HUDDINGE UNIV HOSP,KAROLINSKA INST,DEPT MED NUTR S-14186 HUDDINGE SWEDEN KYUSHU UNIV,DEPT MOL BIOL FUKUOKA 812 JAPAN
Titolo Testata:
Steroids
fascicolo: 1, volume: 62, anno: 1997,
pagine: 43 - 45
SICI:
0039-128X(1997)62:1<43:TROTBC>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
RECEPTOR SUPERFAMILY; RESPONSIVE SEQUENCE; PROTEIN; TARGET; MEMBER;
Keywords:
17-ALPHA-HYDROXYLASE; P450C17; SF-1; COUP-TF; CAMP;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
12
Recensione:
Indirizzi per estratti:
Citazione:
J. Lund et al., "TRANSCRIPTIONAL REGULATION OF THE BOVINE CYP17 GENE BY CAMP", Steroids, 62(1), 1997, pp. 43-45

Abstract

The transcription of steroid hydroxylase genes is controlled by ACTH and cAMP in the adrenal cortex. In most instances the regulation appears to rely on transcription factors traditionally not associated with cAMP-dependent gene expression. For the non-traditional factors it remains necessary to elucidate the coupling of increases in intracellularcAMP and cAMP-dependent protein kinase (PKA) activity to the functionof these proteins. The bovine CYP17 gene, which encodes the steroid 17 alpha-hydroxylase, contains two discrete DNA elements within its promoter and upstream region (CRS1 and CRS2) that individually can confercAMP responsiveness. The CRS1 element is a target for PKA signalling and for negative regulation via the protein kinase C signal transduction pathway. The homeodomain protein Pbx1 enhances CRS1-dependent transcription, but additional CRS1-binding proteins remain to be identified. Furthermore it is not known how PKA regulates the activity of Pbx1 or its possible binding partners. Closer to the promoter, the nuclear orphan receptors SF-I and COUP-TF have overlapping binding sires in CRS2 and they bind in a mutually exclusive manner with very similar affinities; 8 and 10 nM, respectively. SF-1 stimulates whereas COUP-TF inhibits transcription from the bovine CYP17 promoter. Together, the data suggest that cAMP-dependent control of the amounts of the activator SF-I vs. the repressor COUP-TF could influence CRS2-dependent transcription. In addition, PKA may influence the phosphorylation of SF-I, thus ino-easing its activity. In vitro, PKA will elicit phosphorylation of SF-1. However, although SF-1 can be immunoprecipitated from adrenocortical cells as a phosphroprotein, we have not been able to show cAMP-dependent increase in net phosphorylation in intact cells. More careful examination of individual phosphorylation sites in SF-1 may still reveal hormone- and cAMP-induced phosphorylation of SF-1. (C) 1997 by Elsevier Science Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/09/20 alle ore 15:43:41