Prolonged Incubation in PUGNAc Results in Increased Protein O-Linked Glycosylation and Insulin Resistance in Rat Skeletal Muscle

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FIG. 6.
FIG. 6.

Effect of insulin and PUGNAc on phosphorylation of the 160-kDa protein on the Akt phosphomotif. A: Dose response for insulin in muscles incubated without PUGNAc at basal (no insulin), 0.6, or 12 nmol/l insulin during the final 75 min of incubation (n = 4 per group). Paired muscles incubated with or without PUGNAc for 19 h and with 0.6 nmol/l insulin (B) during the final 75 min of incubation (n = 11 per group) or 12 nmol/l insulin (C) during the final 75 min of incubation (n = 12 per group). Protein blots were probed with anti-phospho-(Ser/Thr)Akt substrate. Bands corresponding to the phosphorylated 160-kDa protein were quantitated by densitometry and expressed as the mean ± SE. *Basal vs. 0.6 nmol/l insulin (P < 0.001); **basal vs. 12 nmol/l insulin (P < 0.001) and 0.6 vs. 12 nmol/l insulin (P < 0.05).

This Article

  1. Diabetes vol. 53 no. 4 921-930