Application
Western blot analysis of Akt expression in mouse small intestine tissue lysate.
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(C–E) The phosphorylation of insulin receptor substrate (IRS)-1 (phospho Y632), AKT (phospho Ser473) and AKT (phospho Thr308) was markedly reduced by HG inducement.
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(D, E) DOP treatment markedly relived HG-induced suppressive effects on the phosphorylation of insulin receptor substrate (IRS)-1 (phospho Y632), AKT (phospho Ser473), AKT (phospho Thr308) and Nephrin.
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(C, D) IRS-1/2 inhibitor NT157 treatment notably reversed HG-induced increased phosphorylation of IRS-1 (phospho Y632), AKT (phospho Ser473), AKT (phospho Thr308) and Nephrin.
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(a–c) ECA109 and KYSE150 cells were treated each day with 5 μM GO-203 or CP-2 for 3 days, and GO-203 inhibits the phosphorylation of AKT and S6K1 protein and then increases PDCD4 leave in ESCC cells.
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Following LGR6 overexpression, protein expression levels were (A) determined by western blotting.
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A–E, Western blotting evaluations of Hsp70 (A), cleaved caspase-3 (B), p-Akt and Akt (C), p-JNK and JNK (D), and p-ERK and ERK (E) levels in the myocardium.