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Titolo:
Modulation of the murine peroxisome proliferator-activated receptor gamma 2 promoter activity by CCAAT/enhancer-binding proteins
Autore:
Elberg, G; Gimble, JM; Tsai, SY;
Indirizzi:
Baylor Coll Med, Dept Mol & Cellular Biol, Houston, TX 77030 USA Baylor Coll Med Houston TX USA 77030 Cellular Biol, Houston, TX 77030 USA Univ Oklahoma, Hlth Sci Ctr, Dept Surg, Oklahoma City, OK 73190 USA Univ Oklahoma Oklahoma City OK USA 73190 urg, Oklahoma City, OK 73190 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 36, volume: 275, anno: 2000,
pagine: 27815 - 27822
SICI:
0021-9258(20000908)275:36<27815:MOTMPP>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
INTERCELLULAR-ADHESION MOLECULE-1; NF-KAPPA-B; C/EBP-BETA; TRANSCRIPTION FACTOR; GENE-TRANSCRIPTION; MESSENGER-RNA; ADIPOCYTE DIFFERENTIATION; P21(WAF1/CIP1) GENE; ECTOPIC EXPRESSION; DNA-BINDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Tsai, SY Baylor Coll Med, Dept Mol & Cellular Biol, 1 Baylor Plaza, Houston, TX 77030 USA Baylor Coll Med 1 Baylor Plaza Houston TX USA 77030 TX 77030 USA
Citazione:
G. Elberg et al., "Modulation of the murine peroxisome proliferator-activated receptor gamma 2 promoter activity by CCAAT/enhancer-binding proteins", J BIOL CHEM, 275(36), 2000, pp. 27815-27822

Abstract

Peroxisome proliferator-activated receptor gamma (PPAR gamma) and CCAAT/enhancer-binding proteins (C/EBPs) are transcriptional regulators essential for adipocyte differentiation and function. Previous findings indicate that PPAR gamma 2 transcription is regulated by members of the C/EBP family. We demonstrate here that C/EBP alpha and C/EBP delta, but not C/EBP beta, induce the activity of the PPAR gamma 2 promoter in transiently transfected 3T3-L1 preadipocytes and bind to two juxtaposed low affinity C/EBP binding sites. Results obtained with chimeras containing interchanged C/EBP alpha-C/EBP beta N-terminal transactivation domain and C-terminal DNA binding dimerization domain indicate that the N-terminal part of C/EBP beta prevents it from binding to the PPAR gamma 2 promoter. Indeed, deletion mutants of C/EBP beta lacking the N-terminal part of the molecule are able to bind to the PPAR gamma 2 promoter. We further demonstrate that deletion of a region located between amino acids 184-212, upstream of the DNA binding domain, permitsC/EBP beta binding to the PPAR gamma 2 promoter, implicating an inhibitoryregion in C/EBP beta for modulating DNA binding specificity to the PPAR gamma 2 promoter. In summary, this study indicates that C/EBP beta but not C/EBP alpha or C/EBP delta is unable to bind to C/EBP binding sites in the mouse PPAR gamma 2 promoter. The lack of binding is due to a region N-terminal of the C/EBP beta DNA binding domain. Our findings illustrate a mechanismby which C/EBP isoforms differentially modulate the transactivation of thePPAR gamma 2 promoter.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 22:44:36