Abstract:
:Inducible heat shock protein 70 (HSP70; also known as HSPA1 or HSP72) is implicated in cancer. As a stress‑inducible heat shock protein, HSP70 is highly expressed in a variety of cancers and correlates with metastasis, chemotherapy resistance and tumor prognosis. The present study demonstrated that suppression of HSP70 through the specific inhibitor pifithrin‑µ or by HSP70 knockdown enhanced cisplatin‑induced apoptosis in HGC‑27 gastric cancer cells. By contrast, upregulation of HSP70 through transfection of a HSP70 overexpressing plasmid decreased cisplatin‑induced HGC‑27 cell apoptosis. In exploring the underlying molecular mechanisms, the present results revealed that HSP70 antagonized cisplatin‑induced HGC‑27 cell apoptosis by regulating the mitogen‑activated protein kinase (MAPK) signaling pathway. In addition, suppressing the MAPK pathway enhanced cisplatin‑induced HGC‑27 cell apoptosis. Collectively, the present findings suggest that inhibition of HSP70 expression enhanced the sensitivity of HGC‑27 cells to cisplatin via the MAPK signaling pathway, and that HSP70 may serve as a potential therapeutic target in gastric cancer.
journal_name
Int J Mol Medjournal_title
International journal of molecular medicineauthors
Sheng L,Tang T,Liu Y,Ma Y,Wang Z,Tao H,Zhang Y,Qi Zdoi
10.3892/ijmm.2018.3789subject
Has Abstractpub_date
2018-10-01 00:00:00pages
2089-2097issue
4eissn
1107-3756issn
1791-244Xjournal_volume
42pub_type
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journal_title:International journal of molecular medicine
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