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Titolo:
THE CAMP-RESPONSE-ELEMENT-BINDING PROTEIN INTERACTS, BUT FOS PROTEIN DOES NOT INTERACT, WITH THE PROENKEPHALIN ENHANCER IN RAT STRIATUM
Autore:
KONRADI C; KOBIERSKI LA; NGUYEN TV; HECKERS S; HYMAN SE;
Indirizzi:
MASSACHUSETTS GEN HOSP,MOLEC & DEV NEUROSCI LAB BOSTON MA 02114 MASSACHUSETTS GEN HOSP,DEPT PSYCHIAT BOSTON MA 02114 HARVARD UNIV,SCH MED BOSTON MA 02114 HARVARD UNIV,SCH MED,PROGRAM NEUROSCI BOSTON MA 02115 BETH ISRAEL HOSP,DEPT NEUROL BOSTON MA 02215
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 15, volume: 90, anno: 1993,
pagine: 7005 - 7009
SICI:
0027-8424(1993)90:15<7005:TCPIBF>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
CYCLIC-AMP; C-FOS; GENE-EXPRESSION; MESSENGER-RNA; STRIATOPALLIDAL NEURONS; ENKEPHALIN; TRANSCRIPTION; HALOPERIDOL; INCREASE; AP-1;
Keywords:
AP-1 PROTEINS; HALOPERIDOL;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
28
Recensione:
Indirizzi per estratti:
Citazione:
C. Konradi et al., "THE CAMP-RESPONSE-ELEMENT-BINDING PROTEIN INTERACTS, BUT FOS PROTEIN DOES NOT INTERACT, WITH THE PROENKEPHALIN ENHANCER IN RAT STRIATUM", Proceedings of the National Academy of Sciences of the United Statesof America, 90(15), 1993, pp. 7005-7009

Abstract

The proenkephalin gene is a well-studied model of transcription factor-target gene interaction in the nervous system and has been proposed as a regulatory target of the protein product of the immediate-early gene c-fos. This regulatory mechanism has been proposed, in part, because the cAMP response element 2 (CRE-2) site, the key DNA regulatory element within the proenkephalin second-messenger-inducible enhancer, avidly binds AP-1 proteins, including Fos, in vitro. However, we observea dissociation in the time course of activation of c-fos and proenkephalin mRNA in rat striatum after administration of the dopamine D2 receptor antagonist haloperidol. This result prompted us to investigate the composition of protein complexes in striatal nuclear extracts that bind to the CRE-2 site. Even though our striatal nuclear extracts had substantial basal and haloperidol-inducible AP-1-binding activities that contained Fos, we could not detect Fos in complexes bound to the CRE-2 element. Instead, as determined by antibody supershift analysis, we detect CRE-binding protein (CREB)-like proteins binding to CRE-2 in both basal and haloperidol-stimulated conditions. Finally, we show that haloperidol induces CREB protein phosphorylation in striatum.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 15:11:05