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KMID : 0603820060120040435
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Journal of Experimental & Biomedical Science
2006 Volume.12 No. 4 p.435 ~ p.438
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Induction of ER-stress by Heat Shock in the Thyrocytes
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Kwon Ki-Sang
Kwon O-Yu
Yang Young-Mo
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Abstract
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In eukaryotes, ER stress induces UPR (unfolded protein response) via IRE1 activation which sends a molecular signal for XBP1 mRNA splicing in the cytosol. During this mRNA splicing, 23 nt removed in which contains PstI site and then resulting XBP1 product is not digested with PstI restriction enzyme. In this study, using this XBP1 mRNA splicing mechanism, the effect of heat shock on thyrocytes is studied, because heat shock response in the thyrocytes needs more study to understand thyroid physiology under alternative environments. ER inducible drugs (tunicamycin, DTT, Ca {2+} ionopore A23187, BFA) induce ER stress in the thyrocytes. From 3 hours after heat shock, ER stress is induced and which is reversible when heat shock is without. While Ca {2+} ionopore A23187 is reversible from ER stress by washing out the drug, thapsigagin is irreversible. Other ER inducible drugs are not so sensitive to ER stress repairing. XBP1 mRNA splicing in a cell is very available method to detect ER stress. It needs only a small quantity of total RNA and processing also very easy.
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KEYWORD
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ER stress, XBP1 mRNA splicing, Thyrocytes
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