Biomedical Science Letters (대한의생명과학회지)
- Volume 11 Issue 2
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- Pages.249-252
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- 2005
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- 1738-3226(pISSN)
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- 2288-7415(eISSN)
Development of Rapid Detection Method for Unfolded Protein Response in the Mammalian Cells
- Kwon Kisang (Department of Anatomy, College of Medicine, Chungnam National University) ;
- Goo Tae Won (Department of Sericulture and Entomology, National Institute of Agricultural Science and Technology) ;
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Kwon O-Yu
(Department of Anatomy, College of Medicine, Chungnam National University)
- Published : 2005.06.01
Abstract
The mammalian unfolded protein response (UPR) protects the cell. against the stress of unfolded or misfolded proteins in the endoplasmic reticulum (ER). It has recently demonstrated that IRE1, PERK, ATF6, and X-box protein 1 (XBP-l) directly or indirectly participate in this process. Upon accumulation of unfolded/misfolded proteins in the ER lumen, release of BiP from Ire1p permits dimerization and autophosphorylation to activate its kinase and endoribonulease activities to initiate XBP-1 mRNA splicing. Spliced XBP-1 mRNA removed middle part of 23 bp and encodes a potent transcription factor, XBP-l protein that binds to the unfolded protein response element (UPRE) or endoplasmic reticulum stress element (ERSE) sequence of many UPR target genes and produces several kind of ER chaperones. In this study, we described both the result and the detailed experimental procedures of XBP-1 mRNA splicing induced by ER stress, this result might help to elucidate the roles of the UPR and early diagnosis in a number of human diseases involving endoplasmic reticulum storage disease (ERSD).
Keywords
- Unfolded protein response (UPR);
- Endoplasmic reticulum (ER);
- X-box protein 1 (XBP-l);
- Endoplasmic reticulum storage disease (ERSD)