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Hypothermia Regulates Endoplasmic Reticulum (ER) Stress through the X-box Binding Protein-1 (XBP1) Gene Expression in PC12 Cells

  • Yoo, Bo-Kyung (Department of Anatomy & Cell Biology, College of Medicine, Chungnam National University) ;
  • Kwon, Kisang (Department of Biomedical Laboratory Science, College of Health & Welfare, Kyungwoon University) ;
  • Lee, Eun Ryeong (Department of Biomedical Laboratory Science, College of Health & Welfare, Kyungwoon University) ;
  • Kwon, O-Yu (Department of Anatomy & Cell Biology, College of Medicine, Chungnam National University)
  • Received : 2017.10.20
  • Accepted : 2017.12.08
  • Published : 2017.12.31

Abstract

Endoplasmic reticulum (ER) stress induces unfolded protein response (UPR) via inositol-requiring enzyme 1 (IRE1) activation, which sends a molecular signal for X box-binding protein 1 (XBP1) mRNA splicing in the cytosol. IRE1 endoribonuclease activity induces cleavage of XBP1 mRNA. The XBP1 mRNA is then ligated by an uncharacterized RNA ligase and translated to produce spliced XBP1 by 23 nt removed in which contains the PstI restriction enzyme site. The splicing of XBP1 mRNA can be detected by semiquantitative RT-PCR, and then splicing of XBP1 is a useful tool to measure the genetic variability in ER stress. In this study, we have estimated IRE1-dependent splicing of XBP1 mRNA under conditions of various hypothermia. The results indicated that hypothermia regulated ER stress. This study demonstrated that hypothermia is closely related to ER stress and may be useful for early diagnosis of ER-associated disease.

Keywords

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