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Fewer Exposed Lysine Residues May Explain Relative Resistance of Chicken Serum Albumin to In Vitro Protein Glycation in Comparison to Bovine Serum Albumin.
Journal of Molecular Evolution ( IF 2.1 ) Pub Date : 2020-09-15 , DOI: 10.1007/s00239-020-09964-y
Claire M Anthony-Regnitz 1 , Amanda E Wilson 2 , Karen L Sweazea 3, 4 , Eldon J Braun 1
Affiliation  

Protein glycation and formation of advanced glycation end products is associated with several diseases resulting from high blood glucose concentrations. Plasma albumin is directly exposed to circulating glucose concentrations and is therefore at greater risk of glycation than hemoglobin. As plasma glucose concentrations in birds are 1.5–2 times higher than mammals of similar mass, avian albumin may be particularly at risk of glycation. Thus, the goal of the present study was to compare the in vitro formation of glycated albumin in chicken serum albumin (CSA) and bovine serum albumin (BSA) exposed to a range of glucose concentrations over a 16-week period. The level of glycation for CSA and BSA was quantified using boronate affinity columns to separate glycated albumin from non-glycated albumin and calculating the difference in protein concentration of each sample. The results indicate that CSA is glycated to a lesser degree than BSA when the albumins are exposed to increasing concentrations of glucose (38.8–500 mM). This was most apparent at week sixteen (500 mM glucose) where BSA expressed a higher degree of glycation (37.8 ± 0.76%) compared to CSA (19.7 ± 1.06%, P < 0.05). Additionally, percent glycation at week sixteen was significantly higher than the glucose-free solutions for both BSA and CSA, indicating that glycation is glucose-dependent. Analyses of the protein structures suggest that the relative resistance of CSA to glycation may be due to fewer lysine residues and variations in protein folding that shield more lysine residues from the plasma. Moreover, comparisons of reconstructed ancestral albumin sequences show that the ancestor of birds had 6–8 fewer lysine residues compared to that of mammals.



中文翻译:

与牛血清白蛋白相比,较少暴露的赖氨酸残留可以解释鸡血清白蛋白对体外蛋白糖化的相对抗性。

蛋白质糖基化和晚期糖基化终产物的形成与由高血糖浓度引起的多种疾病有关。血浆白蛋白直接暴露于循环葡萄糖浓度,因此比血红蛋白有更大的糖化风险。由于鸟类的血浆葡萄糖浓度比同等质量的哺乳动物高 1.5-2 倍,因此鸟类白蛋白可能特别容易发生糖基化。因此,本研究的目的是比较在 16 周内暴露于一系列葡萄糖浓度的鸡血清白蛋白 (CSA) 和牛血清白蛋白 (BSA) 中糖化白蛋白的体外形成。使用硼酸盐亲和柱将糖化白蛋白与非糖化白蛋白分开并计算每个样品的蛋白质浓度差异,对 CSA 和 BSA 的糖化水平进行量化。结果表明,当白蛋白暴露于浓度增加的葡萄糖 (38.8-500 mM) 时,CSA 的糖化程度低于 BSA。这在第 16 周(500 mM 葡萄糖)最为明显,与 CSA(19.7 ± 1.06%,P  < 0.05)。此外,对于 BSA 和 CSA,第 16 周的糖基化百分比显着高于无葡萄糖溶液,表明糖基化是葡萄糖依赖性的。对蛋白质结构的分析表明,CSA 对糖化的相对抗性可能是由于较少的赖氨酸残基和蛋白质折叠的变化,从而使更多的赖氨酸残基远离血浆。此外,重建祖先白蛋白序列的比较表明,与哺乳动物相比,鸟类祖先的赖氨酸残基少 6-8 个。

更新日期:2020-09-15
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