Abstract
Heat shock protein 27 (HSP27) is a multifunctional protein that undergoes significant changes in its expression and phosphorylation in response to shear stress stimuli, suggesting that it may be involved in mechanotransduction. However, the mechanism of HSP27 affecting tumor cell migration under shear stress is still not clear. In this study, HSP27-enhanced cyan fluorescent protein (ECFP) and HSP27-Ypet plasmids are constructed to visualize the self-polymerization of HSP27 in living cells based on fluorescence resonance energy transfer technology. The results show that shear stress induces polar distribution of HSP27 to regulate the dynamic structure at the cell leading edge. Shear stress also promotes HSP27 depolymerization to small molecules and then regulates polar actin accumulation and focal adhesion kinase (FAK) polar activation, which further promotes tumor cell migration. This study suggests that HSP27 plays an important role in the regulation of shear stress-induced HeLa cell migration, and it also provides a theoretical basis for HSP27 as a potential drug target for metastasis.
Highlights
Metastasis, the most fatal characteristic of malignant tumors, accounts for more than 90% of tumor-related mortalities [1]
Lambert et al have proposed that Heat shock protein 27 (HSP27) forms stable dimers through the α-crystallin domain that further multimerize through intermolecular interactions mediated by the phosphorylation of a sensitive
The results indicate that overexpression of HSP27 and inhibition of HSP27 phosphorylation phosphorylation can attenuate shear-stress-induced can attenuate shear-stress-induced
Summary
Metastasis, the most fatal characteristic of malignant tumors, accounts for more than 90% of tumor-related mortalities [1]. Cancer cells first separate from the primary tumor and degrade host stroma and intravasate into the blood and/or lymphatic vasculature. These cells extravasate from endothelium tissues and invade parenchyma tissues of the distant organ [2]. It has been reported that hemodynamic shear stress stimulates migration of tumor cells as well as their extravasation by increasing cellular oxidative levels [4]. It alters the interactions of tumor cells and improves their viability and proliferation [5,6]. Some reports have shown that low shear stress may endow tumor cell migration ability via activating the focal adhesion kinase (FAK)-extracellular regulated protein kinases
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