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Titolo:
NADH oxidase activity of mitochondrial apoptosis-inducing factor
Autore:
Miramar, MD; Costantini, P; Ravagnan, L; Saraiva, LM; Haouzi, D; Brothers, G; Penninger, JM; Peleato, ML; Kroemer, G; Susin, SA;
Indirizzi:
Inst Gustave Roussy, CNRS, UMR 1599, F-94805 Villejuif, France Inst Gustave Roussy Villejuif France F-94805 , F-94805 Villejuif, France Univ Zaragoza, Dept Bioquim & Biol Mol & Celular, E-50009 Zaragoza, Spain Univ Zaragoza Zaragoza Spain E-50009 & Celular, E-50009 Zaragoza, Spain Univ Nova Lisboa, Inst Tecnol Quim & Biol, P-2780 Oeiras, Portugal Univ Nova Lisboa Oeiras Portugal P-2780 & Biol, P-2780 Oeiras, Portugal Univ Toronto, Dept Med Biophys & Immunol, Ontario Canc Inst, Toronto, ON M5G 2C1, Canada Univ Toronto Toronto ON Canada M5G 2C1 Inst, Toronto, ON M5G 2C1, Canada Univ Toronto, Dept Med Biophys & Immunol, Amgen Inst, Toronto, ON M5G 2C1,Canada Univ Toronto Toronto ON Canada M5G 2C1 n Inst, Toronto, ON M5G 2C1,Canada
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 19, volume: 276, anno: 2001,
pagine: 16391 - 16398
SICI:
0021-9258(20010511)276:19<16391:NOAOMA>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROGRAMMED CELL-DEATH; HYDROGEN-PEROXIDE; ESCHERICHIA-COLI; FACTOR AIF; PURIFICATION; SYSTEM; OXIDOREDUCTASE; FERREDOXIN; REDUCTASE; ENZYME;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
61
Recensione:
Indirizzi per estratti:
Indirizzo: Kroemer, G Inst Gustave Roussy, CNRS, UMR 1599, Pavillon Rech I,39 Rue Camille Desmoulins, F-94805 Villejuif, France Inst Gustave Roussy Pavillon Rech I,39 Rue Camille Desmoulins Villejuif France F-94805
Citazione:
M.D. Miramar et al., "NADH oxidase activity of mitochondrial apoptosis-inducing factor", J BIOL CHEM, 276(19), 2001, pp. 16391-16398

Abstract

Apoptosis-inducing factor (AIF) is a mitochondrial flavoprotein, which translocates to the nucleus during apoptosis and causes chromatin condensationand large scale DNA fragmentation. Here we report the biochemical characterization of AIF's redox activity. Natural AIF purified from mitochondria and recombinant AIF purified from bacteria (AIF Delta1-120) exhibit NADH oxidase activity, whereas superoxide anion (O-2(-)) is formed. AIF Delta1-120 is a monomer of 57 kDa containing 1 mol of noncovalently bound FAD/mol of protein. ApoATF Delta1-120, which lacks FAD, has no NADH oxidase activity. However, native AIF Delta1-120, apoAIF Delta1-120, and the reconstituted (FAD-containing) holoAIF Delta1-120 protein exhibit a similar apoptosis-inducing potential when microinjected into the cytoplasm of intact cells. inhibition of the redox function, by external addition of superoxide dismutase or covalent derivatization of FAD with diphenyleneiodonium, failed to affect the apoptogenic function of AIF Delta1-120 assessed on purified nuclei in a cell-free system. Conversely, blockade of the apoptogenic function of AIF Delta1-120 with the thiol reagent para-chloromercuriphenylsulfonic acid did not affect its NADH oxidase activity. Altogether, these data indicate that AIF has a marked oxidoreductase activity which can be dissociated from its apoptosis-inducing function.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/08/20 alle ore 09:01:05