English  |  正體中文  |  简体中文  |  Items with full text/Total items : 27248/39091
Visitors : 2415990      Online Users : 64
RC Version 4.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
Scope Adv. Search
LoginUploadHelpAboutAdminister

Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/26846

Title: XBP-1, a key regulator of unfolded protein response, activates transcription of IGF1 and Akt phosphorylation in zebrafish embryonic cell line
Authors: Meng-Chuen Hu;Hong-Yi Gong;Gen-Hwa Lin;Shao-Yang Hu;Mark Hung-Chih Chen;Shin-Jie Huang;Ching-Fong Liao;Jen-Leih Wu
Contributors: 國立臺灣海洋大學:水產養殖學系
Keywords: XBP-1;Unfolded protein response;ER stress;IGF1;Akt;Anti-apoptosis;Zebrafish
Date: 2007-08-03
Issue Date: 2011-10-21T02:19:04Z
Publisher: Biochemical and Biophysical Research Communications
Abstract: Abstract:The unfolded protein response (UPR) is a conserved and adaptive cellular response to increase cell survival during ER stress. XBP-1 spliced form (XBP-1S) generated by IRE1 endoribonuclease is a key transcriptional regulator in UPR to activate genes involved in protein folding and degradation to restore ER function. Although Akt activation was suggested to be a pro-survival pathway activated during ER stress, the signal to trigger Akt is still not clear. In this study, we report IGF1 transcription and Akt phosphorylation are enhanced in XBP-1S stably overexpressed clone of zebrafish embryonic cell line (ZF4). In addition, zebrafish IGF1 intron1 with predicted UPRE (XBP-1S binding sites) and ERSE (ATF6/XBP-1S binding site) linked with basal promoter could be activated by XBP-1S, not by XBP-1 unspliced form (XBP-1U). Furthermore, we demonstrate that expression of endogenous IGF1 is transiently induced as XBP-1 splicing during ER stress in parallel to ER chaperone GRP78/Hspa5 and ER resided E3 ubiquitin ligase Synoviolin in ZF4 cells by quantitative PCR. Our results suggest zebrafish XBP-1S not only activates genes responsible for protein folding, transporting, glycosylation and ER associated degradation but also activates anti-apoptosis signal via IGF1/Akt pathway in unfolded protein response to cope with ER stress.
Relation: 359(3), pp.778-783
URI: http://ntour.ntou.edu.tw/handle/987654321/26846
Appears in Collections:[水產養殖學系] 期刊論文

Files in This Item:

File Description SizeFormat
index.html0KbHTML356View/Open


All items in NTOUR are protected by copyright, with all rights reserved.

 


著作權政策宣告: 本網站之內容為國立臺灣海洋大學所收錄之機構典藏,無償提供學術研究與公眾教育等公益性使用,請合理使用本網站之內容,以尊重著作權人之權益。
網站維護: 海大圖資處 圖書系統組
DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - Feedback