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

Abstract：

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.

journal_name

J Hepatol

journal_title

Journal of hepatology

authors

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

doi

10.1016/j.jhep.2007.01.039

subject

Has Abstract

pub_date

2007-07-01 00:00:00

pages

93-102

issue

1

eissn

0168-8278

issn

1600-0641

pii

S0168-8278(07)00116-X

journal_volume

47

pub_type

杂志文章

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