Glycation of proteins and subsequent production of advanced glycation end products (AGEs) is a major contributor to the pathophysiology of diabetes. The objective of the present study was to compare the glycation of avian and human serum albumin to elucidate the mechanisms by which protein glycation in birds is prevented in the presence of naturally high plasma glucose concentrations. Solutions of purified chicken and human serum albumin (CSA and HSA) were prepared with four different glucose concentrations (0, 5.56, 11.1, and 22.2 mM) and incubated at three temperatures (37.0, 39.8, and 41.4 °C) for seven days. The solutions were sampled on Days 0, 3, and 7 and analyzed by liquid chromatography-electrospray ionization-mass spectrometry for the presence of glycated albumin. Four-way repeated measures ANOVA (p = 0.032) indicate that all independent variables (albumin type, glucose concentration, temperature and time) interacted to affect the degree of glycation. With increasing glucose concentration, the glycation of both HSA and CSA increased with time at all temperatures. In addition, HSA was glycated to a greater extent than CSA at the two higher glucose concentrations for all temperature conditions. Glycation was elevated with increasing temperatures for HSA but not CSA. The results suggest an inherent difference between human and chicken albumin that contributes to the observed differences in glycation. Further research is needed to characterize this inherent difference in an effort to elucidate mechanisms by which avian plasma protein is glycated to a lesser degree than that of mammals (humans).
|Original language||English (US)|
|Number of pages||7|
|Journal||Comparative Biochemistry and Physiology Part - B: Biochemistry and Molecular Biology|
|State||Published - Jan 1 2017|
ASJC Scopus subject areas
- Molecular Biology