English  |  正體中文  |  简体中文  |  Items with full text/Total items : 92472/107804 (86%)
Visitors : 19144962      Online Users : 403
RC Version 6.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
Scope Tips:
  • please add "double quotation mark" for query phrases to get precise results
  • please goto advance search for comprehansive author search
  • Adv. Search
    HomeLoginUploadHelpAboutAdminister Goto mobile version

    Please use this identifier to cite or link to this item: http://asiair.asia.edu.tw/ir/handle/310904400/16126

    Title: Peptidyl-prolyl cis/trans isomerase PIN1 is critical for the regulation of PKB/Akt stability and activation phosphorylation
    Authors: Liao, Y.;Wei, Y;Zhou, Z;Yang, J-Y;Dai, C;Chen, Y-J;Agarwal, N.K;Sarbassov, D;Shi, D;Yu, D;洪明奇;Hung, Mien-Chie
    Contributors: 生物科技學系
    Keywords: PKB/Akt;Pin1;peptidyl-prolyl cis/trans isomerase;breast cancer
    Date: 2009
    Issue Date: 2012-11-23 17:08:53 (UTC+8)
    Abstract: The serine/threonine protein kinase B (PKB, also known as Akt) plays a pivotal role in diverse cellular functions. Elevated expression of activated Akt has been detected in a wide variety of human cancers; however, the mechanism of Akt protein stability regulation remains unclear. In this study, we showed a strong correlation between the expression levels of an oncogenic peptidyl-prolyl cis/trans isomerase Pin1 and levels of Akt phosphorylation at S473 in multiple cancer types (P<0.0001). Akt-pS473 status combined with Pin1 expression levels predicted a poorer prognosis than did either one alone in patients with breast cancer (P = 0.0052). We further showed that Pin1 regulated Akt stability and phosphorylation on S473 through the phosphorylated Thr-Pro motifs of Akt. These motifs are conserved evolutionary and are required for the maintenance of Akt stability and its interaction with Pin1. In addition, repressing Pin1 expression through either homologue Pin1 knockout or small interfering RNA-mediated knockingdown compromised its ability to protect Akt from degradation. Our results show how Akt protein stability is regulated by the peptidyl-prolyl cis/trans isomerase Pin1 and highlight the importance of this oncogenic network in human disease pathogenesis.
    Relation: ONCOGENE,28(26),2436–2445.
    Appears in Collections:[生物科技學系] 期刊論文

    Files in This Item:

    File Description SizeFormat

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

    DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - Feedback