HSP60 mediates AKT/mTOR signaling to promote the progression of colorectal cancer.

Colorectal cancer (CRC) is a relatively common malignant tumor in the digestive system, and its prevention and treatment remain a challenging issue. The migration and invasion of CRC leads to significantly poor prognosis. Heat shock protein 60 (HSP60) is a mitochondrial chaperone that maintains the stability of mitochondrial proteins and plays an important functional role in the progression of most tumors. However, the functional role of HSP60 in the migration and invasion of CRC is still not understood. Therefore, this study investigated the expression of HSP60 in CRC tissues by using public databases, and the effect of HSP60 on the migration and invasion of CRC cells through functional experiments. The results showed that HSP60 was highly expressed in CRC tissues. Overexpression of HSP60 promotes the migration and invasion of CRC cells, enhances the stress and morphological changes of the cellular fibrin skeleton. However, shRNA knockdown HSP60 expression inhibited the progression of CRC cells and reduced the stress ability of fibrin. Moreover, public databases showed that there was a clear correlation between HSP60 and AKT in CRC tissues. Overexpression of HSP60 increased the expression levels of p-AKT and p-mTOR proteins, while knocking down HSP60 achieved the opposite result. Further used of BGT226 (20 nm), a dual inhibitor of the AKT/mTOR pathway, inhibited the migration and invasive movement of CRC cells induced by HSP60 overexpression. Furthermore, in vivo experiments further showed that overexpression of HSP60 promoted tumor growth. These results indicate that HSP60 is highly expressed in CRC tissues. Overexpression of HSP60 promotes the progression of CRC cells. This may be related to HSP60 overexpression activating AKT/mTOR signaling. These data suggest that HSP60 may be used as another important molecular target for the prevention and treatment of CRC.