QIN Lei, XU Ke, ZHANG Chun-Guang, CHU Han, DENG Shi-Fan, ZHANG Jian-Bin, YANG Hua, HONG Liang, ZHANG Gui-Feng, SUN Chao, PU Lei
The aim of this study was to investigate the impact of overexpressing 70-kD heat shock proteins (Hsp70) on glycolysis in C2C12 cells during myogenesis and adipogenesis. Using C2C12 cells as the research material, adenovirus was used to overexpress the Hsp70 gene, and changes in the expression of glycolytic genes were detected using fluorescence quantitative PCR and Western blotting techniques. The study indicated that during C2C12 cell myogenic differentiation, the expression trend of the Hsp70 gene was consistent with that of Gsk3β, Pkm, Prkag3, Pfkm, and Hk-2 genes, suggesting a relationship between Hsp70 and the glycolytic pathway during myogenic differentiation. Overexpression of Hsp70 in the later stages of myogenic differentiation significantly upregulated the expression of Gsk3β, Pkm, Prkag3, and Pfkm genes (P<0.05), with no significant impact on Hk-2 gene expression (P>0.05). During C2C12 cell adipogenic induction, the expression trend of the Hsp70 gene was similar to that of Gsk3β, Pkm, Prkag3, Pfkm, and Hk-2 genes, indicating a relationship between Hsp70 and the glycolytic pathway during adipogenic induction. Following Hsp70 overexpression, in the later stages of adipogenic induction, the number of lipid droplets was significantly higher compared to the control group, with a significant upregulation of Gsk3β, Pkm, Prkag3, and Pfkm gene expression (P<0.05), while Hk-2 gene expression was not significantly affected (P>0.05). In conclusion, Hsp70 in C2C12 cells in myogenic and adipogenic states promoted the breakdown of glycogen into 6-phospho-glucose, thereby enhancing the glycolytic pathway, providing insights into the functional role of the Hsp70 gene in glycolysis in C2C12 cells.
