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Titolo:
Participation of cytosolic protein phosphatase in regulation of NADPH oxidase in polymorphonuclear leukocytes
Autore:
Kawakami, N; Takemasa, H; Okamura, N; Hayakawa, T; Shimohama, S; Fujimoto, S;
Indirizzi:
KyotoJapanmaceut Univ, Dept Environm Biochem, Yamashima Ku, Kyoto 6078414,Kyoto Pharmaceut Univ Kyoto Japan 6078414 , Yamashima Ku, Kyoto 6078414, Hiroshimaapanv, Sch Med, Dept Physiol Chem, Minami Ku, Hiroshima 7340037, J Hiroshima Univ Hiroshima Japan 7340037 , Minami Ku, Hiroshima 7340037, J Natl Inst Hlth Sci, Div Biol Chem & Biol, Setagaya Ku, Tokyo 1588501, Japan Natl Inst Hlth Sci Tokyo Japan 1588501 Setagaya Ku, Tokyo 1588501, Japan Kyoto Univ, Fac Med, Dept Neurol, Kyoto 6068507, Japan Kyoto Univ Kyoto Japan 6068507 ac Med, Dept Neurol, Kyoto 6068507, Japan
Titolo Testata:
BIOLOGICAL & PHARMACEUTICAL BULLETIN
fascicolo: 6, volume: 22, anno: 1999,
pagine: 556 - 560
SICI:
0918-6158(199906)22:6<556:POCPPI>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
CHRONIC GRANULOMATOUS-DISEASE; RESPIRATORY BURST OXIDASE; GUINEA-PIG NEUTROPHILS; KINASE-C; ACTIVATION; PHOSPHORYLATION; TRANSLOCATION; MEMBRANE;
Keywords:
polymorphonuclear leukocyte; NADPH oxidase; calyculin A; protein phosphatase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
21
Recensione:
Indirizzi per estratti:
Indirizzo: Kawakami, N KyotoJapanmaceut Univ, Dept Environm Biochem, Yamashima Ku, Kyoto 6078414, Kyoto Pharmaceut Univ Kyoto Japan 6078414 Ku, Kyoto 6078414,
Citazione:
N. Kawakami et al., "Participation of cytosolic protein phosphatase in regulation of NADPH oxidase in polymorphonuclear leukocytes", BIOL PHAR B, 22(6), 1999, pp. 556-560

Abstract

Calyculin A, a protein phosphatase inhibitor, enhanced phorbol 12-myristate 13-acetate (PMA)-induced superoxide anion (O-2(-)) production and translocation of the cytosolic NADPH oxidase factor, p47phox, to the plasma membrane in guinea pig polymorphonuclear leukocytes (PMNs). When PMNs were treated with 1-(5-isoquinoline-sulfonyl)-3-methyl-piperazine (H-7), a protein kinase C (PKC) inhibitor, after exposure to PMA, inhibition of O-2(-) production and of translocation of p47phox to the membrane fraction in PMA-stimulated PMNs were observed. When calyculin A was added to the PMA-stimulated PMNs after the addition of H-7, O-2(-) production was again observed and translocation of p47phox to the membrane fraction also occurred. The activity ofNADPH oxidase, the amount of p47phox and the level of phosphorylation of p47phox in the membrane fraction prepared from PMA-stimulated PMNs, were reduced by the addition of the cytosol fraction from unstimulated PMNs. These reductions were attenuated by calyculin A. These results indicate that the active form of NADPH oxidase in PMNs can be reconstituted after the active complex of the enzyme has disappeared once, and that one of the mechanisms of regulation of this enzyme activity involves the phosphorylation of p47phox in the cyotosol and dephosphorylation of phosphorylated p47phox in the NADPH oxidase complex by protein kinase: and protein phosphatase, respectively.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/04/20 alle ore 12:06:33