Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/66036
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Type: Journal article
Title: Subtilase cytotoxin activates MAP kinases through PERK and IRE1 branches of the unfolded protein response
Author: Zhao, Y.
Tian, T.
Huang, T.
Nakajima, S.
Saito, Y.
Takahashi, S.
Yao, J.
Paton, A.
Paton, J.
Kitamura, M.
Citation: Toxicological Sciences, 2011; 120(1):79-86
Publisher: Oxford Univ Press
Issue Date: 2011
ISSN: 1096-6080
1096-0929
Statement of
Responsibility: 
Yang Zhao, Tian Tian, Tao Huang, Shotaro Nakajima, Yukinori Saito, Shuhei Takahashi, Jian Yao, Adrienne W. Paton, James C. Paton, and Masanori Kitamura
Abstract: Recent reports suggested involvement of mitogen-activated protein (MAP) kinases in the pathogenesis of Shiga toxin–induced hemolytic uremic syndrome (HUS). In the present study, we investigated a role for subtilase cytotoxin (SubAB), a possible trigger for HUS, in the regulation of MAP kinases. Treatment of cells with SubAB caused phosphorylation of c-Jun NH2-terminal kinase, extracellular signal-regulated kinase (ERK), and p38 MAP kinase. It was associated with activation of activator protein 1 (AP-1) and induction of AP-1–dependent transcription. SubAB induced the unfolded protein response (UPR) and consequently caused MAP kinase activation. SubAB led to induction of three major branches of the UPR, and the protein kinase–like endoplasmic reticulum kinase and inositol-requiring ER-to-nucleus signal kinase 1 pathways were responsible for the activation of MAP kinases. These results elucidated the potential of SubAB to trigger MAP kinase pathways via the UPR, which may contribute to the pathogenesis of Shiga toxin–induced HUS.
Keywords: Cell Line; Epithelial Cells; Animals; Rats; Subtilisins; Protein-Serine-Threonine Kinases; eIF-2 Kinase; Mitogen-Activated Protein Kinases; Escherichia coli Proteins; Membrane Proteins; Transcription Factor AP-1; Blotting, Western; Transfection; Enzyme Activation; Unfolded Protein Response
Rights: © The Author 2010. Published by Oxford University Press on behalf of the Society of Toxicology. All rights reserved.
RMID: 0020110958
DOI: 10.1093/toxsci/kfq368
Appears in Collections:Molecular and Biomedical Science publications

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