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Titolo:
Assembly of the neutrophil respiratory burst oxidase: A direct interactionbetween p67(PHOX) and cytochrome b(558)
Autore:
Dang, PMC; Cross, AR; Babior, BM;
Indirizzi:
Scripps Clin & Res Inst, Dept Mol & Expt Med, La Jolla, CA 92037 USA Scripps Clin & Res Inst La Jolla CA USA 92037 Med, La Jolla, CA 92037 USA
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 6, volume: 98, anno: 2001,
pagine: 3001 - 3005
SICI:
0027-8424(20010313)98:6<3001:AOTNRB>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHAGOCYTE NADPH OXIDASE; CELL-FREE SYSTEM; INHIBIT SUPEROXIDE GENERATION; FLAVOCYTOCHROME B(558); ACTIVATION DOMAIN; BINDING SITE; P47(PHOX); SUBUNIT; P40(PHOX); PHOSPHORYLATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
23
Recensione:
Indirizzi per estratti:
Indirizzo: Babior, BM Scripps Clin & Res Inst, Dept Mol & Expt Med, La Jolla, CA 92037 USA Scripps Clin & Res Inst La Jolla CA USA 92037 la, CA 92037 USA
Citazione:
P.M.C. Dang et al., "Assembly of the neutrophil respiratory burst oxidase: A direct interactionbetween p67(PHOX) and cytochrome b(558)", P NAS US, 98(6), 2001, pp. 3001-3005

Abstract

Activation of the phagocyte NADPH oxidase complex requires the assembly ofthe cytosolic factors p47(PHOX), P67(PHOX), P40(PHOX), and Rad or Rac2, with the membrane-bound cytochrome b(558) Whereas the interaction of p47(PHOX) with cytochrome b(558) is well established, an interaction between p67(PHOX) and cytochrome b(558) has never been investigated. We report here a direct interaction between p67(PHOX) and cytochrome b(558) First, labeled p67(PHOX) recognizes a 91-kDa band in specific: granules from a normal patient but not from a cytochrome b(558)-deficient patient. Second, p67(PHOX) bindsto cytochrome b(558) that has been bound to nitrocellulose. Third, GTP-p67(PHOX) bound to glutathione agarose is able to pull down cytochrome b(558). Rac1-GTP or Rac1-GDP increased the binding of p67(PHOX) to cytochrome b(558), suggesting that at least one of the oxidase-retated functions of Rad isto promote the interaction between p67(PHOX) and cytochrome b(558).

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/10/20 alle ore 11:54:21