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Titolo:
SELENIUM-DEPENDENT GLUTATHIONE PEROXIDASE-GI IS A MAJOR GLUTATHIONE-PEROXIDASE ACTIVITY IN THE MUCOSAL EPITHELIUM OF RODENT INTESTINE
Autore:
ESWORTHY RS; SWIDEREK KM; HO YS; CHU FF;
Indirizzi:
CITY HOPE NATL MED CTR,DEPT MED ONCOL,1500 E DUARTE RD DUARTE CA 91010 CITY HOPE NATL MED CTR,DEPT MED ONCOL & THERAPEUT RES DUARTE CA 91010 CITY HOPE NATL MED CTR,BECKMAN RES INST,DIV IMMUNOL DUARTE CA 91010 WAYNE STATE UNIV,INST TOXICOL DETROIT MI 48201
Titolo Testata:
Biochimica et biophysica acta (G). General subjects
fascicolo: 2, volume: 1381, anno: 1998,
pagine: 213 - 226
SICI:
0304-4165(1998)1381:2<213:SGPIAM>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
TANDEM MASS-SPECTROMETRY; PEPTIDE MIXTURES; GSHPX-GI; EXPRESSION; PROTEINS; FORM; GPX2;
Keywords:
GLUTATHIONE PEROXIDASE; ISOENZYME; INTESTINE; MUCOSA; SELENIUM; MASS SPECTROMETRY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
28
Recensione:
Indirizzi per estratti:
Citazione:
R.S. Esworthy et al., "SELENIUM-DEPENDENT GLUTATHIONE PEROXIDASE-GI IS A MAJOR GLUTATHIONE-PEROXIDASE ACTIVITY IN THE MUCOSAL EPITHELIUM OF RODENT INTESTINE", Biochimica et biophysica acta (G). General subjects, 1381(2), 1998, pp. 213-226

Abstract

Gpx2 mRNA, encoding a selenium-dependent glutathione peroxidase (GPX-GI), has been found to be highly expressed in the gastrointestinal tract (GI) mucosal epithelium. In this study, we show that GPX-GI is produced in the mucosal epithelium of the adult rat GI tract and that the activity levels are comparable to that from GPX-1. Post-mitochondrial supernatant GPX activity from the mucosal epithelium of the complete length of the small intestine was partially purified. A sample enrichedfor putative GPX-GI was fractionated by SDS-polyacrylamide gel electrophoresis. Polypeptides of 21 kDa and 22 kDa were digested with trypsin. After resolving the tryptic peptides by high pressure liquid chromatography (HPLC), the major peaks were analyzed for their amino acid sequence by Microflow-HPLC-Tandem Mass Spectrometry and automated Edman degradation sequencing. Both methods revealed that the 21-kDa sample contained rat GPX-GI determined by the sequence homology with the deduced mouse GPX-GI polypeptide sequence. Rat GPX-1 was also detected in the samples. AntiGPX-GI and antiGPX-1 antibodies were used to determinethe distribution of the respective isoenzyme activities along the length of the intestine and with respect to the crypt to villus axis in rats. GPX-GI and GPX-1 activities were uniformly distributed in the middle and lower GI tract and with respect to the crypt to villus axis. GPX-GI activity accounted nearly the same percentage of the total GPX activity as GPX-1 in all of the these compartments. Studies on the distal ileum segment of wildtype and Gpx1 gene knockout mice showed that GPX-GI activity was also at parity with GPX-1 in the mucosal epitheliumof this segment. (C) 1998 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 12:53:58