Heat shock protein 27 phosphorylation in the proliferation and apoptosis of human umbilical vein endothelial cells induced by high glucose through the phosphoinositide 3‑kinase/Akt and extracellular signal‑regulated kinase 1/2 pathways.

In the present study, the effect of the heat shock protein 27 (HSP27) signaling pathway on the proliferation and apoptosis of human umbilical vein endothelial cells (HUVECs) induced by high glucose (HG) was investigated. HUVEC proliferation in the indicated conditions was measured by the alamarBlue® assay. Apoptosis in HUVECs cultured with HG was analyzed by an Annexin V‑fluorescein isothiocyanate/propidium iodide apoptosis detection kit. HSP27 activity was evaluated by western blotting with specific phospho‑HSP27 antibody. HUVEC proliferation induced by HG was observed to be reduced by the HSP27 inhibitor quercetin in a concentration‑dependent manner, with a concomitant increase in apoptosis. The phosphorylation of HSP27 induced by HG was blocked by the specific phosphoinositide 3‑kinase (PI3K) inhibitor LY294002 and the specific extracellular signal‑regulated kinase (ERK) 1/2 inhibitor U0126 in a concentration‑dependent manner, with peak inhibition rates of 62.6 and 56.1%, respectively. LY294002 and U0126 also reduced HUVEC proliferation with a concomitant increase in apoptotic rate. In conclusion, HSP27 phosphorylation is important in mediating the proliferation and apoptosis of HUVECs induced by high glucose, and PI3K/Akt and ERK1/2 are important signaling pathways that contribute to HSP27 phosphorylation.