Cell death or survival against oxidative stress

Non Miyata; Kanji Okumoto; Yukio Fujiki

doi:10.1007/978-981-13-2233-4_20

Cell death or survival against oxidative stress

Non Miyata, Kanji Okumoto, Yukio Fujiki

Research output: Chapter in Book/Report/Conference proceeding › Chapter

1 Citation (Scopus)

Abstract

Peroxisomes contain anabolic and catabolic enzymes including oxidases that produce hydrogen peroxide as a by-product. Peroxisomes also contain catalase to metabolize hydrogen peroxide. It has been recognized that catalase is localized to cytosol in addition to peroxisomes. A recent study has revealed that loss of VDAC2 shifts localization of BAK, a pro-apoptotic member of Bcl-2 family, from mitochondria to peroxisomes and cytosol, thereby leading to release of peroxisomal matrix proteins including catalase to the cytosol. A subset of BAK is localized to peroxisomes even in wild-type cells, regulating peroxisomal membrane permeability and catalase localization. The cytosolic catalase potentially acts as an antioxidant to eliminate extra-peroxisomal hydrogen peroxide.

Original language	English
Title of host publication	Subcellular Biochemistry
Publisher	Springer New York
Pages	463-471
Number of pages	9
DOIs	https://doi.org/10.1007/978-981-13-2233-4_20
Publication status	Published - 2018

Publication series

Name	Subcellular Biochemistry
Volume	89
ISSN (Print)	0306-0225

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology
Cell Biology
Cancer Research

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1007/978-981-13-2233-4_20

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title = "Cell death or survival against oxidative stress",

abstract = "Peroxisomes contain anabolic and catabolic enzymes including oxidases that produce hydrogen peroxide as a by-product. Peroxisomes also contain catalase to metabolize hydrogen peroxide. It has been recognized that catalase is localized to cytosol in addition to peroxisomes. A recent study has revealed that loss of VDAC2 shifts localization of BAK, a pro-apoptotic member of Bcl-2 family, from mitochondria to peroxisomes and cytosol, thereby leading to release of peroxisomal matrix proteins including catalase to the cytosol. A subset of BAK is localized to peroxisomes even in wild-type cells, regulating peroxisomal membrane permeability and catalase localization. The cytosolic catalase potentially acts as an antioxidant to eliminate extra-peroxisomal hydrogen peroxide.",

author = "Non Miyata and Kanji Okumoto and Yukio Fujiki",

note = "Funding Information: We thank the supports: MEXT KAKENHI grant JP26116007 and JSPS KAKENHI grants JP24247038, JP25112518, JP25116717, JP15K14511, JP15K21743, JP17H03675, and grants from the Takeda Science Foundation, the Naito Foundation, the Japan, Foundation for Applied Enzymology, and the Novartis Foundation (Japan) for the Promotion of Science. Funding Information: Acknowledgements We thank the supports: MEXT KAKENHI grant JP26116007 and JSPS KAKENHI grants JP24247038, JP25112518, JP25116717, JP15K14511, JP15K21743, JP17H03675, and grants from the Takeda Science Foundation, the Naito Foundation, the Japan, Foundation for Applied Enzymology, and the Novartis Foundation (Japan) for the Promotion of Science. Publisher Copyright: {\textcopyright} Springer Nature Singapore Pte Ltd. 2018. Copyright: Copyright 2018 Elsevier B.V., All rights reserved.",

year = "2018",

doi = "10.1007/978-981-13-2233-4_20",

language = "English",

series = "Subcellular Biochemistry",

publisher = "Springer New York",

pages = "463--471",

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AU - Miyata, Non

AU - Okumoto, Kanji

AU - Fujiki, Yukio

N1 - Funding Information: We thank the supports: MEXT KAKENHI grant JP26116007 and JSPS KAKENHI grants JP24247038, JP25112518, JP25116717, JP15K14511, JP15K21743, JP17H03675, and grants from the Takeda Science Foundation, the Naito Foundation, the Japan, Foundation for Applied Enzymology, and the Novartis Foundation (Japan) for the Promotion of Science. Funding Information: Acknowledgements We thank the supports: MEXT KAKENHI grant JP26116007 and JSPS KAKENHI grants JP24247038, JP25112518, JP25116717, JP15K14511, JP15K21743, JP17H03675, and grants from the Takeda Science Foundation, the Naito Foundation, the Japan, Foundation for Applied Enzymology, and the Novartis Foundation (Japan) for the Promotion of Science. Publisher Copyright: © Springer Nature Singapore Pte Ltd. 2018. Copyright: Copyright 2018 Elsevier B.V., All rights reserved.

PY - 2018

Y1 - 2018

N2 - Peroxisomes contain anabolic and catabolic enzymes including oxidases that produce hydrogen peroxide as a by-product. Peroxisomes also contain catalase to metabolize hydrogen peroxide. It has been recognized that catalase is localized to cytosol in addition to peroxisomes. A recent study has revealed that loss of VDAC2 shifts localization of BAK, a pro-apoptotic member of Bcl-2 family, from mitochondria to peroxisomes and cytosol, thereby leading to release of peroxisomal matrix proteins including catalase to the cytosol. A subset of BAK is localized to peroxisomes even in wild-type cells, regulating peroxisomal membrane permeability and catalase localization. The cytosolic catalase potentially acts as an antioxidant to eliminate extra-peroxisomal hydrogen peroxide.

AB - Peroxisomes contain anabolic and catabolic enzymes including oxidases that produce hydrogen peroxide as a by-product. Peroxisomes also contain catalase to metabolize hydrogen peroxide. It has been recognized that catalase is localized to cytosol in addition to peroxisomes. A recent study has revealed that loss of VDAC2 shifts localization of BAK, a pro-apoptotic member of Bcl-2 family, from mitochondria to peroxisomes and cytosol, thereby leading to release of peroxisomal matrix proteins including catalase to the cytosol. A subset of BAK is localized to peroxisomes even in wild-type cells, regulating peroxisomal membrane permeability and catalase localization. The cytosolic catalase potentially acts as an antioxidant to eliminate extra-peroxisomal hydrogen peroxide.

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ER -

Cell death or survival against oxidative stress

Abstract

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UN SDGs

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