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An involvement of oxidative stress in endoplasmic reticulum stress and its associated diseases

  • Bidur Bhandary
  • , Anu Marahatta
  • , Hyung Ryong Kim
  • , Han Jung Chae*
  • *Corresponding author for this work
  • Jeonbuk National University
  • Wonkwang University

Research output: Contribution to journalReview articlepeer-review

Abstract

The endoplasmic reticulum (ER) is the major site of calcium storage and protein folding. It has a unique oxidizing-folding environment due to the predominant disulfide bond formation during the process of protein folding. Alterations in the oxidative environment of the ER and also intra-ER Ca2+ cause the production of ER stress-induced reactive oxygen species (ROS). Protein disulfide isomerases, endoplasmic reticulum oxidoreductin-1, reduced glutathione and mitochondrial electron transport chain proteins also play crucial roles in ER stress-induced production of ROS. In this article, we discuss ER stress-associated ROS and related diseases, and the current understanding of the signaling transduction involved in ER stress.

Original languageEnglish
Pages (from-to)434-456
Number of pages23
JournalInternational Journal of Molecular Sciences
Volume14
Issue number1
DOIs
StatePublished - 2013.01

Keywords

  • Disulfide bond formation
  • ER associated oxidative stress
  • ER stress
  • ER stress associated disease
  • ERO-1a
  • Mitochondria electron transport chain
  • PDI

Quacquarelli Symonds(QS) Subject Topics

  • Computer Science & Information Systems
  • Engineering - Petroleum
  • Data Science
  • Engineering - Chemical
  • Chemistry
  • Biological Sciences

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