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
Checked for plagiarism Yes
Review by Single anonymous peer review
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
Department of Neurosurgery, Jiangning Hospital Affiliated with Nanjing Medical University, Nanjing 211100, People’s Republic of China
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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