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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

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A Correction to this article was published on 21 December 2020

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Abstract

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.

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Acknowledgement

The authors thank Mr. Joshua Choi for determining the folded protein structures of BSA and CSA.

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Authors and Affiliations

  1. Department of Physiology, University of Arizona, Tucson, AZ, 85721, USA

    Claire M. Anthony-Regnitz & Eldon J. Braun

  2. Department of Biology and Center for Computational Genetics and Genomics, Temple University, Philadelphia, PA, 19122, USA

    Amanda E. Wilson

  3. College of Health Solutions, Arizona State University, Phoenix, AZ, 85004, USA

    Karen L. Sweazea

  4. School of Life Sciences, Arizona State University, 427 E Tyler Mall, Mail Code 4501, Tempe, AZ, 85287, USA

    Karen L. Sweazea

Authors
  1. Claire M. Anthony-Regnitz
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  2. Amanda E. Wilson
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  3. Karen L. Sweazea
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  4. Eldon J. Braun
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Corresponding author

Correspondence to Karen L. Sweazea.

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Handling editor: Konstantinos Voskarides.

The original online version of this article was revised: Supplementary information ‘239_2020_9964_MOESM1_ESM’ and ‘239_2020_9964_MOESM2_ESM’ are replaced.

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Anthony-Regnitz, C.M., Wilson, A.E., Sweazea, K.L. et al. Fewer Exposed Lysine Residues May Explain Relative Resistance of Chicken Serum Albumin to In Vitro Protein Glycation in Comparison to Bovine Serum Albumin. J Mol Evol 88, 653–661 (2020). https://doi.org/10.1007/s00239-020-09964-y

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  • DOI: https://doi.org/10.1007/s00239-020-09964-y

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