Cell membrane gp96 facilitates HER2 dimerization and serves as a novel target in breast cancer. Issue 3 (8th January 2015)

• Record Type: Journal Article
• Authors: Li, Xin; Sun, Lu; Hou, Junwei; Gui, Mingming; Ying, Jianming; Zhao, Hong; Lv, Ning; Meng, Songdong
• Is Part Of: International journal of cancer. Volume 137:Issue 3(2015:Aug. 01)
• Page Start: 512
• Page End: 524
• Publication Date: 2015-01-08
• Subjects: Cancer -- Periodicals; Cancer -- Prevention -- Periodicals; 616.994
• DOI: 10.1002/ijc.29405
• Languages: English
• ISSNs: 0020-7136

Abstract

<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>HER2 receptor dimerization is a critical step in the HER2 activation process. Here, we demonstrated that heat shock protein gp96 on cell membrane interacts with HER2, facilitates HER2 dimerization and promotes cell proliferation. Cell membrane gp96 levels were observed to correlate with HER2 phosphorylation in primary breast tumors. Finally, we provide evidence that targeting gp96 with a specific monoclonal antibody led to decreased cell growth and increased apoptosis <italic>in vitro</italic>, and suppression of tumor growth <italic>in vivo</italic>. Our work represents a new therapeutic strategy for inhibiting HER2 signaling in cancer.</p> </abstract>