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Clin Exp Pharmacol Physiol. 2015 Oct;42(10):1092-7. doi: 10.1111/1440-1681.12457.

HSP60 overexpression increases the protein levels of the p110α subunit of  phosphoinositide 3-kinase and c-Myc.

Author information

1
Department of Radiotherapy, Zhejiang Cancer Hospital, Hangzhou, China.
2
Institute of Ageing Research, School of Medicine, Hangzhou Normal University, Hangzhou, China.
3
Genome Research Centre, National Yang-Ming University, Taipei, Taiwan.
4
Research Centre for Tumor Medical Science, Graduate Institute of Cancer Biology, China Medical University, Taichung, Taiwan.

Abstract

Heat shock protein 60 (HSP60) is a chaperone protein which plays an essential role in facilitating the folding of many newly synthesized proteins to reach their native forms. Increased HSP60 expression is observed in various types of human cancers. However, proteins induced by HSP60 to mediate transformation remain largely unknown. Here we show that HSP60 overexpression increases the protein levels of the p110α subunit of phosphoinositide 3-kinase (PI3K). The amino acid domain 288-383 of HSP60 is used to increase the protein levels. Overexpression of HSP60 also induces the levels of phosphorylated Akt. In addition, the amino acid domain 288-383 of HSP60 is used to induce c-Myc expression. Finally, a mono-ubiquitinated form of β-catenin has a higher activity to activate β-catenin downstream targets compared to wild-type β-catenin. These results indicate that HSP60 overexpression induces the levels or activity of multiple oncogenic proteins to mediate transformation.

KEYWORDS:

Heat shock protein 60 (HSP60); c-Myc; p110α; transformation

PMID:
26174078
DOI:
10.1111/1440-1681.12457
[Indexed for MEDLINE]

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