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Titolo:
A soluble NH2-terminally truncated catalytically active form of rat cytochrome P450 2E1 targeted to liver mitochondria
Autore:
Neve, EPA; Ingelman-Sundberg, M;
Indirizzi:
Karolinska Inst, Natl Inst Environm Med, Div Mol Toxicol, S-17177 Stockholm, Sweden Karolinska Inst Stockholm Sweden S-17177 icol, S-17177 Stockholm, Sweden
Titolo Testata:
FEBS LETTERS
fascicolo: 2, volume: 460, anno: 1999,
pagine: 309 - 314
SICI:
0014-5793(19991029)460:2<309:ASNTCA>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
ENDOPLASMIC-RETICULUM MEMBRANE; SACCHAROMYCES-CEREVISIAE; PROTEIN IMPORT; RETENTION; REGION; SIGNAL; CYTOCHROME-P-450(SCC); TRANSLOCATION; DEGRADATION; SUFFICIENT;
Keywords:
mitochondrial import; chlorzoxazone; cDNA transfection; adrenodoxin; ethanol; oxidative stress; cytochrome P450 2E1;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Neve, EPA Karolinska Inst, Natl Inst Environm Med, Div Mol Toxicol, Box 210, S-17177Stockholm, Sweden Karolinska Inst Box 210 Stockholm Sweden S-17177 ckholm, Sweden
Citazione:
E.P.A. Neve e M. Ingelman-Sundberg, "A soluble NH2-terminally truncated catalytically active form of rat cytochrome P450 2E1 targeted to liver mitochondria", FEBS LETTER, 460(2), 1999, pp. 309-314

Abstract

The role of the NH2-terminus of cytochrome P450 2E1 (CYP2E1) in intracellular targeting was investigated. Tao NH2-terminal CYP2E1 mutants, Delta(2-29)2E1, lacking the transmembrane domain, and N(++)2E1, having Ala2Lys and Val3Arg substitutions, were generated and expressed in the H2.35 mouse hepatoma cell line. In cells transfected with both constructs, a 40 kDa fragment of CYP2E1 (Delta 2E1) was found to he localized to mitochondria as evidenced from immunofluorescence microscopy and subcellular fractionation studies. Delta 2E1 was shown to be a soluble protein localized inside the mitochondria, displayed catalytic activity when reconstituted with adrenodoxin and adrenodoxin reductase, and was also present in mitochondria isolated from rat liver. It is concluded that in the absence of the hydrophobic NH2-terminal sequence, a putative mitochondrial import signal is exposed which targetsCYP2E1 to this organelle where it is further processed. (C) 1999 Federation of European Biochemical Societies.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/03/20 alle ore 20:06:43