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Heat Shock Cognate Protein 70 Enhanced Integrin β1 Mediated Invasion in Cancer Cells

Authors Sun G, Cao Y, Guo J, Li M, Dai Y

Received 23 October 2019

Accepted for publication 11 December 2019

Published 11 February 2020 Volume 2020:12 Pages 981—991

DOI https://doi.org/10.2147/CMAR.S235791

Checked for plagiarism Yes

Review by Single-blind

Peer reviewer comments 2

Editor who approved publication: Professor Bilikere Dwarakanath


Guan Sun, 1,* Ying Cao, 2,* Jun Guo, 1 Min Li, 3,* Yuyu Dai 4

1Department of Neurosurgery, Yancheng City No.1 People’s Hospital, The Fourth Affiliated Hospital of Nantong University, Yancheng, People’s Republic of China; 2Department of Ear-Nose-Throat, The Second People’s Hospital of Huai’an, Huai’an Affiliated Hospital of Xuzhou Medical University, Huai’an, People’s Republic of China; 3Department of Neurosurgery, Jiangning Hospital Affiliated with Nanjing Medical University, Nanjing, People’s Republic of China; 4Department of Neurosurgery, Yancheng Third People’s Hospital, Yancheng, People’s Republic of China

*These authors contributed equally to this work

Correspondence: Yuyu Dai
Department of Neurosurgery, Yancheng Third People’s Hospital, Yancheng 224001, People’s Republic of China
Email daiyuyu1981@163.com
Min Li
Department of Neurosurgery, Jiangning Hospital Affiliated with Nanjing Medical University, Nanjing 211100, People’s Republic of China
Email sbn133@163.com

Purpose: Glioblastoma is one of the most common malignant cancers worldwide. In our previous work, we have shown that heat shock cognate protein 70 (Hsc70) functions as a positive growth regulator in glioma. We investigated the role of Hsc70 in integrin β 1 mediated invasion of glioma cells.
Methods: In order to investigate whether the down-regulation of Hsc70 would affect the expression of integrin β 1 subunit, HeLa cells were transiently transfected with Hsc70-AS or pcDNA3.0 vectors and the down-regulation of Hsc70 was confirmed by Western blotting. Human brain glioma U87 cells were stably transfected with Hsc70-AS or pcDNA3.0 vectors to further elucidate the relationship between Hsc70 and integrin β 1 in human glioma cells. Cellular localization of integrin β 1 was detected using immunofluorescence confocal microscopy analysis.
Results: Here we reported that down-regulation of the expression of Hsc70 in U87 cells by transfection with antisense cDNA specifically increased the expression of cell surface integrin β 1 without changing its mRNA. Meanwhile, the integrin β 1 125-kD mature form increased while 105-kD precursor form decreased when Hsc70 was down-regulated. Mechanically, the U87 cells transfected with antisense cDNA of Hsc70 decreased the Golgi localization of integrin β 1, strengthened its interaction with integrin α 5 subunit, and enhanced the adhesion ability to fibronectin (FN) and the phosphorylation level of focal adhesion kinase (FAK).
Conclusion: Overall, these results suggested that the down-regulation of Hsc70 expression could promote the expression of cell surface integrin β 1 and subsequently inhibit glioma invasion phenotype.

Keywords: Hsc70, integrin β 1, glioma, focal adhesion kinase, invasion

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