Prolonged Incubation in PUGNAc Results in Increased Protein O-Linked Glycosylation and Insulin Resistance in Rat Skeletal
(Downloading may take up to 30 seconds. If the slide opens in your browser, select File -> Save As to save it.)
Click on image to view larger version.
O-linked glycosylation of muscle proteins following 19 h of incubation of paired skeletal muscles with or without 100 μmol/l
PUGNAc. A: Muscle homogenates were subjected to 8% SDS-PAGE. Subsequent protein blots were probed with anti-O-GlcNAc and visualized
following enhanced chemiluminescence. Relative molecular weight standards are denoted. B: Protein bands were quantitated by densitometry, and values for PUGNAc-treated samples are expressed relative to the mean
value for the corresponding protein band in muscles incubated without PUGNAc (mean ± SE; n = 6 per group). *Significant difference for paired muscles with PUGNAc versus without PUGNAc (P < 0.005).