Oxidative stress induces the endoplasmic reticulum stress and facilitates inclusion formation in cultured cells.

Oxidative stress induces the endoplasmic reticulum stress and facilitates inclusion formation in cultured cells. Research Abstract Details 

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Oxidative stress induces the endoplasmic reticulum stress and facilitates inclusion formation in cultured cells. Abstract Text:

Shinichiro Hanada,Masaru Harada,Hiroto Kumemura,M Bishr Omary,Hironori Koga,Takumi Kawaguchi,Eitaro Taniguchi,Takafumi Yoshida,Takao Hisamoto,Chikatoshi Yanagimoto,Michiko Maeyama,Takato Ueno,Michio Sata,

BACKGROUND/AIMS: The precise mechanism of formation and significance of Mallory bodies (MBs) are poorly understood. The endoplasmic reticulum (ER) is the organelle responsible for proper folding and elimination of unfolded proteins. Therefore, failure of this function increases defective proteins in the cell. METHODS: We examined the effects of oxidative stress on induction of ER stress and keratin 8 and 18 (K8/18)-containing inclusion formation in cultured human hepatoma cells and hepatocytes by immunofluorescence and immunoblot analyses. RESULTS: Generation of H(2)O(2) was detected in glucose oxidase (GO)-treated cells by 2',7'-dichlorodihydrofluorescein diacetate and co-treatment with GO and acetyl-leucyl-leucyl-norleucinal (ALLN), a proteasome inhibitor, induced formation of extensive keratin inclusions that were inhibited by pre-treatment with N-acetyl-cysteine. These inclusions shared similar features with MBs by immunofluorescence analysis. Electron microscopy showed that these structures appeared near the nuclei, surrounded by filamentous structures. GO and ALLN upregulated the expression of ER stress markers, however, 4-phenylbutyrate, a chemical chaperone, reduced formation of inclusions and expression of the ER stress markers. CONCLUSIONS: The oxidative stress coupled with limited inhibition of the proteasome induces dysfunction of the ER and results in inclusion formation in cultured cells. This suggests that ER stress plays a role in MB formation in liver disease.

Oxidative stress induces the endoplasmic reticulum stress and facilitates inclusion formation in cultured cells. Publishing Authors By Initials

S Hanada,M Harada,H Kumemura,M Bishr Omary,H Koga,T Kawaguchi,E Taniguchi,T Yoshida,T Hisamoto,C Yanagimoto,M Maeyama,T Ueno,M Sata,

For similar cells: cells, cultured: tumor cells, cultured research abstracts see: cells: cells, cultured: tumor cells, cultured research

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Oxidative stress induces the endoplasmic reticulum stress and facilitates inclusion formation in cultured cells. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Journal of hepatology

VOLUME: 47

Page Numbers: 93-102

Journal Abbreviation: J. Hepatol.

ISSN: 0168-8278

DAY: 8

MONTH: 03

YEAR: 2007

Oxidative stress induces the endoplasmic reticulum stress and facilitates inclusion formation in cultured cells. Information

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LANGUAGE: eng

NlmUniqueID: 8503886

Oxidative stress induces the endoplasmic reticulum stress and facilitates inclusion formation in cultured cells. Keywords Mesh Terms:

KEYWORDS: Tumor Cells, Cultured

MESH TERMS: antagonists & inhibitors

Chemical & Substance for Abstract: Oxidative stress induces the endoplasmic reticulum stress and facilitates inclusion formation in cultured cells. Information

Substance Name: Proteasome Endopeptidase Complex

Registry Number: EC 3.4.25.1

Grant and Affiliation Information for Oxidative stress induces the endoplasmic reticulum stress and facilitates inclusion formation in cultured cells.

AFFILIATION: Department of Medicine, Kurume University School of Medicine, and Research Center for Innovative Cancer Therapy, and Center of the 21st Century COE Program for Medical Science, Kurume University, Kurume, Japan. hanadas@med.kurume-u.ac.jp

Country: England

AGENCY: United States NIDDK

GRANT: DK52951

ACRONYM: DK

MEDLINETA: J Hepatol

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