Advanced glycation end products (AGEs) and their receptor (RAGE) have also been suggested to contribute to the pathogenesis of NASH in HFD-fed rats [18,19]. Also, oxidative stress has been reported to increase glycated protein levels [20]. As shown in Fig. 2F, the levels of AGE (top) and RAGE (middle) were evidently higher in the WT-HFD group compared to those of the other three groups, while p38 (bottom) and Coomassie staining (not shown) verified similar protein loading for all samples. In addition, staining for glycoproteins (Fig. 2G) and silver staining (Fig. 2H) confirmed that HFD increased the levels of glycoproteins only in WT-HFD. In fact, very few glycoproteins were detected in the Cyp2e1-null mouse groups, suggesting an important role of CYP2E1 in protein glycosylation/glycation.
