Fig. 4

HSP70 and GRP78 inhibit insulin-stimulated Akt phosphorylation and glucose uptake in HepG2. ^*P < 0.05, ^**P < 0.009, ^***P < 0.0009. Number of samples = 5. Data are mean ± s.e.m. or are expressed as median plus minimum and maximum values for whisker plots. Original blot images are reported in the Supplementary Figure 6. a, b Akt Ser473 relative phosphorylation in HepG2 cells during insulin stimulation (100 nM) is inhibited by HSP70 (a) and GRP78 (b) in the concentration range of 200–800 pg mL⁻¹. c Akt Ser473 relative phosphorylation in the insulin-stimulated (100 nM) HepG2 cells is inhibited by complete serum of obese IR, NAFLD subjects before metabolic surgery. Immunodepleted (immunoprecipitation (IP)) serum of HSP70 or GRP78 from the same obese IR, NAFLD subjects did not inhibit Ser473 Akt phosphorylation. d, e HSP70 (d) and GRP78 (e) inhibit insulin-mediated (100 nM) 2-DG6P uptake in HepG2 cells. f Insulin-mediated (100 nM) 2-DG6P uptake in HepG2 cells is inhibited by complete serum from obese IR, NAFLD subjects before metabolic surgery. Immunedepleted serum of HSP70 or GRP78 from the same obese IR, NAFLD subject did not affect insulin-mediated 2-DG6P uptake