Overexpression of Hsc70 promotes proliferation, migration, and invasion of human glioma cells

Abstract

Migration and invasion are often recognized as the main reasons for the high recurrence and death rates of glioma and limit the efficacy of surgery and other antitumor therapies. In this study, we found over activation of heat shock cognate protein 70 (Hsc70) in human glioma specimens, which was closely related to glioma grade. We investigated whether Hsc70 induced the migration and invasion of glioma cells. Wound healing and transwell migration assay were used to determine the migration and invasion ability of human glioma U251 and U87 cells, in which the expression of Hsc70 was knocked down by small interfering RNA.Western blot analysis was performed to determine the expression of FAK-Src signaling in malignant glioma cells. The results showed that Hsc70 deficiency significantly retarded migration and invasion and reduced the phosphorylation of FAK, Src, and Pyk2 in U251 and U87 cells. Overall, our results indicate that the migration and invasion capacity of human brain glioma cells is at least partly induced by Hsc70-dependent activation of FAK-Src signaling.

Overexpression of heat shock protein 70 inhibits epithelial-mesenchymal transition and cell migration induced by transforming growth factor-β in A549 cells

“…There was evidence that HSP70 was involved in the process of cell migration. In glioma, overexpression of HSP70 can promote cell migration (Sun et al 2019). Conversely, in HeLa cells, silencing HSP70 gene expression promotes cell migration (Kasioumi et al 2019).…”

Impact of Polyallylamine Hydrochloride on Gene Expression and Karyotypic Stability of Multidrug Resistant Transformed Cells

“…It has been shown that enhanced expression of HSP70 is accompanied with activation of mesenchymal markers N-cadherin, MMP2, SNAIL, and vimentin and promotes metastasis of breast cancer [ 53 ]. Overexpression of HSC70 stimulates glioma cell proliferation, migration, and invasion through phosphorylation and activation of FAK, Src, and Pyk2 [ 54 ]. GRP78, a resident protein in the endoplasmic reticulum (ER), is also overexpressed in various tumor cells.…”

Heat Shock Proteins: Agents of Cancer Development and Therapeutic Targets in Anti-Cancer Therapy

“…Furthermore, HSC70 overexpression enhances the glioma cell proliferation, migration, and invasion through phosphorylation and activation of FAK, Src, and Pyk2. [55]. As extensively studied in relation to cancer, Mortalin is overexpressed in a variety of tumors, including breast, pancreatic, lung, and ovarian cancers, and it is associated with multiple processes of carcinogenesis, which include the inactivation of tumor suppressor p53, deregulation of apoptosis, activation of EMT, and induction of cancer cell stemness.…”