Anionic amphiphile-independent activation of the phagocyte NADPH oxidase in a cell-free system by p47(phox) and p67(phox), both in C terminally truncated forms. Implication for regulatory Src homology 3 domain-mediated interactions

Kenichiro Hata, Takashi Ito, Koichiro Takeshige, Hideki Sumimoto

研究成果: ジャーナルへの寄稿記事

66 引用 (Scopus)

抄録

Anionic amphiphiles, such as arachidonate, activate the superoxide- producing phagocyte NADPH oxidase in a cell-free system with human neutrophil membrane, which contains cytochrome b558 comprising gp91(phox) and p22(phox), and three cytosolic proteins: p47(phox) and p67(phox), each harboring two SH3 domains, and the small GTPase Rac. Here we show that, even without the amphiphiles, the oxidase is activated in vitro by a C terminally truncated p47(phox), retaining the N-terminal and the two SH3 domains, and the N terminus of p67(phox). When either truncated p47(phox) or p67(phox) is replaced by the respective full-length one, the activation absolutely requires the amphiphiles. The results indicate that both p47(phox) and p67(phox) are the primary targets of the amphiphiles, and that their C- terminal regions play negative regulatory roles. We also find that the truncated p47(phox), but not the full-length one, can bind to p22(phox), a binding required for the oxidase activation. The N-terminal SH3 domain of p47(phox) is responsible for the binding not only to p22(phox), but also to the p47(phox) C terminus. Thus the SH3 domain is accessible in the active p47(phox), but is normally masked in the full-length one probably via intramolecularly interacting with the C terminus. The present findings support our previous proposal of regulatory SH3 domain-mediated interactions.

元の言語英語
ページ(範囲)4232-4236
ページ数5
ジャーナルJournal of Biological Chemistry
273
発行部数7
DOI
出版物ステータス出版済み - 2 13 1998

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Amphiphiles
src Homology Domains
Cell-Free System
NADPH Oxidase
Phagocytes
Chemical activation
Oxidoreductases
neutrophil cytosol factor 67K
4-ethoxymethylene-2-phenyl-2-oxazoline-5-one
Monomeric GTP-Binding Proteins
Superoxides
Neutrophils
Membranes

All Science Journal Classification (ASJC) codes

  • Biochemistry

これを引用

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title = "Anionic amphiphile-independent activation of the phagocyte NADPH oxidase in a cell-free system by p47(phox) and p67(phox), both in C terminally truncated forms. Implication for regulatory Src homology 3 domain-mediated interactions",
abstract = "Anionic amphiphiles, such as arachidonate, activate the superoxide- producing phagocyte NADPH oxidase in a cell-free system with human neutrophil membrane, which contains cytochrome b558 comprising gp91(phox) and p22(phox), and three cytosolic proteins: p47(phox) and p67(phox), each harboring two SH3 domains, and the small GTPase Rac. Here we show that, even without the amphiphiles, the oxidase is activated in vitro by a C terminally truncated p47(phox), retaining the N-terminal and the two SH3 domains, and the N terminus of p67(phox). When either truncated p47(phox) or p67(phox) is replaced by the respective full-length one, the activation absolutely requires the amphiphiles. The results indicate that both p47(phox) and p67(phox) are the primary targets of the amphiphiles, and that their C- terminal regions play negative regulatory roles. We also find that the truncated p47(phox), but not the full-length one, can bind to p22(phox), a binding required for the oxidase activation. The N-terminal SH3 domain of p47(phox) is responsible for the binding not only to p22(phox), but also to the p47(phox) C terminus. Thus the SH3 domain is accessible in the active p47(phox), but is normally masked in the full-length one probably via intramolecularly interacting with the C terminus. The present findings support our previous proposal of regulatory SH3 domain-mediated interactions.",
author = "Kenichiro Hata and Takashi Ito and Koichiro Takeshige and Hideki Sumimoto",
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T1 - Anionic amphiphile-independent activation of the phagocyte NADPH oxidase in a cell-free system by p47(phox) and p67(phox), both in C terminally truncated forms. Implication for regulatory Src homology 3 domain-mediated interactions

AU - Hata, Kenichiro

AU - Ito, Takashi

AU - Takeshige, Koichiro

AU - Sumimoto, Hideki

PY - 1998/2/13

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N2 - Anionic amphiphiles, such as arachidonate, activate the superoxide- producing phagocyte NADPH oxidase in a cell-free system with human neutrophil membrane, which contains cytochrome b558 comprising gp91(phox) and p22(phox), and three cytosolic proteins: p47(phox) and p67(phox), each harboring two SH3 domains, and the small GTPase Rac. Here we show that, even without the amphiphiles, the oxidase is activated in vitro by a C terminally truncated p47(phox), retaining the N-terminal and the two SH3 domains, and the N terminus of p67(phox). When either truncated p47(phox) or p67(phox) is replaced by the respective full-length one, the activation absolutely requires the amphiphiles. The results indicate that both p47(phox) and p67(phox) are the primary targets of the amphiphiles, and that their C- terminal regions play negative regulatory roles. We also find that the truncated p47(phox), but not the full-length one, can bind to p22(phox), a binding required for the oxidase activation. The N-terminal SH3 domain of p47(phox) is responsible for the binding not only to p22(phox), but also to the p47(phox) C terminus. Thus the SH3 domain is accessible in the active p47(phox), but is normally masked in the full-length one probably via intramolecularly interacting with the C terminus. The present findings support our previous proposal of regulatory SH3 domain-mediated interactions.

AB - Anionic amphiphiles, such as arachidonate, activate the superoxide- producing phagocyte NADPH oxidase in a cell-free system with human neutrophil membrane, which contains cytochrome b558 comprising gp91(phox) and p22(phox), and three cytosolic proteins: p47(phox) and p67(phox), each harboring two SH3 domains, and the small GTPase Rac. Here we show that, even without the amphiphiles, the oxidase is activated in vitro by a C terminally truncated p47(phox), retaining the N-terminal and the two SH3 domains, and the N terminus of p67(phox). When either truncated p47(phox) or p67(phox) is replaced by the respective full-length one, the activation absolutely requires the amphiphiles. The results indicate that both p47(phox) and p67(phox) are the primary targets of the amphiphiles, and that their C- terminal regions play negative regulatory roles. We also find that the truncated p47(phox), but not the full-length one, can bind to p22(phox), a binding required for the oxidase activation. The N-terminal SH3 domain of p47(phox) is responsible for the binding not only to p22(phox), but also to the p47(phox) C terminus. Thus the SH3 domain is accessible in the active p47(phox), but is normally masked in the full-length one probably via intramolecularly interacting with the C terminus. The present findings support our previous proposal of regulatory SH3 domain-mediated interactions.

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