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Hyperphosphorylated p47-phox lost the ability to activate NADPH oxidase in guinea pig neutrophils.
Yamaguchi, M; Saeki, S; Yamane, H; Okamura, N; Ishibashi, S.
Afiliação
  • Yamaguchi M; Department of Physiological Chemistry, Hiroshima University School of Medicine, Japan.
Biochem Biophys Res Commun ; 216(1): 203-8, 1995 Nov 02.
Article em En | MEDLINE | ID: mdl-7488090
p47-phox is one of the cytosolic activation factors of NADPH oxidase in neutrophils and known to translocate to plasma membranes and function by protein kinase C-phosphorylation. In cytosol fraction, prepared from calyculin A-treated neutrophils, the activity of cytosolic factor to activate NADPH oxidase was more reduced than that from PMA-treated cells. But, p47-phox did not translocate to the membranes, even if p47-phox was hyperphosphorylated in the calyculin A-treated neutrophils. Such hyperphosphorylated p47-phox seemed to lose the activity to constitute NADPH oxidase complex.
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fosfoproteínas / NADH NADPH Oxirredutases / NADPH Desidrogenase / Neutrófilos Limite: Animals Idioma: En Revista: Biochem Biophys Res Commun Ano de publicação: 1995 Tipo de documento: Article País de afiliação: Japão País de publicação: Estados Unidos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fosfoproteínas / NADH NADPH Oxirredutases / NADPH Desidrogenase / Neutrófilos Limite: Animals Idioma: En Revista: Biochem Biophys Res Commun Ano de publicação: 1995 Tipo de documento: Article País de afiliação: Japão País de publicação: Estados Unidos