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Titolo:
Thrombin induces the release of the Y-box protein dbpB from mRNA: A mechanism of transcriptional activation
Autore:
Stenina, OI; Shaneyfelt, KM; DiCorleto, PE;
Indirizzi:
Cleveland Clin Fdn, Lerner Res Inst, Dept Cell Biol, Cleveland, OH 44195 USA Cleveland Clin Fdn Cleveland OH USA 44195 l Biol, Cleveland, OH 44195 USA
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 13, volume: 98, anno: 2001,
pagine: 7277 - 7282
SICI:
0027-8424(20010619)98:13<7277:TITROT>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
MESSENGER-RIBONUCLEOPROTEIN PARTICLES; MAJOR CORE PROTEIN; COLD SHOCK DOMAIN; ENDOTHELIAL-CELLS; XENOPUS-OOCYTES; BINDING PROTEIN; SOMATIC-CELLS; RNA; TRANSLATION; PHOSPHORYLATION;
Keywords:
DNA-binding protein B; endothelium; platelet-derived growth factor; RNA-binding proteins;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: DiCorleto, PE Cleveland Clin Fdn, Lerner Res Inst, Dept Cell Biol, 9500 Euclid Ave, Cleveland, OH 44195 USA Cleveland Clin Fdn 9500 Euclid Ave Cleveland OH USA 44195 SA
Citazione:
O.I. Stenina et al., "Thrombin induces the release of the Y-box protein dbpB from mRNA: A mechanism of transcriptional activation", P NAS US, 98(13), 2001, pp. 7277-7282

Abstract

We have recently demonstrated that thrombin induces expression of the platelet-derived growth factor B-chain gene in endothelial cells (EC) through activation of the Y-box binding protein DNA-binding protein B (dbpB). We nowpresent evidence that dbpB is activated by a novel mechanism: proteolytic cleavage leading to release from mRNA, nuclear translocation, and inductionof thrombin-responsive genes. Cytosolic, full-length dbpB (50 kDa) was rapidly cleaved to a 30-kDa species upon thrombin stimulation of EC. This truncated, "active" dbpB exhibited nuclear localization and binding affinity for the thrombin response element sequence, which is distinct from the Y-box sequence. Oligo(dT) affinity chromatography revealed that cytosolic dbpB from control EC. but not active dbpB from thrombin-treated EC, was bound to mRNA. Latent dbpB immunoprecipitated from cytosolic extracts of control EC was activated by ribonuclease treatment. Furthermore, when EC cytosolic extracts were subjected to Nycodenz gradient centrifugation. latent dbpB fractionated with mRNA, whereas active dbpB fractionated with free proteins. The cytosolic retention domain of dbpB, which we localized to the region 247-267, was proteolytically cleaved during its activation. In contrast to full-length dbpB, truncated dbpB stimulated platelet-derived growth factor B-chain and tissue factor promoter activity by over 5-fold when transiently cotransfected with reporter constructs. These results suggest a novel mode of transcription factor activation in which an agonist causes release from mRNA of a latent transcription factor leading to its transport to the nucleus and its regulation of target gene expression.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 14:52:35