Identification of differences in the formation of plasma glycated proteins between dogs and humans under diabetes-like glucose concentration conditions.

Dogs have been proposed as a translational model and used for studying aging, diabetes, and diabetes-related complications in humans. However, no studies have ever compared the glycation of plasma proteins between dogs and humans under similar experimental conditions. Thus, the aim of this study was to fill this gap by comparing the plasma protein glycation patterns of dogs and humans in an ex-vivo system. Canine and human plasma samples were incubated with glucose at concentrations comparable to those observed in diabetic patients. The final glucose plasma concentration resulted in similar glucose:albumin ratios in both species. Glycated proteins were evaluated by measuring the content of fructosamine, protein carbonyls, and the formation of advanced glycation end-products (AGEs). The concentrations of fructosamine and protein carbonyls in canine and human plasma increased in a glucose concentration-dependent manner (P < 0.0001). Of note, the relative increment of fructosamine and protein carbonyl content and AGE formation was always higher in human than in dog plasma. Our results reveal that the plasma glycation processes in dogs and humans are not similar. These novel findings could contribute to improve our understating about canine and human diabetes as well as other condition associated in the glycation of proteins.