2017
DOI: 10.1016/j.cbpb.2016.10.003
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Chicken albumin exhibits natural resistance to glycation

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Cited by 11 publications
(3 citation statements)
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“…However, the logarithmic nature of the relationship, together with a scaling factor lower than 1, suggests that species with higher plasma glucose levels exhibit relatively greater resistance to glycation. This finding aligns with previous research indicating that in vitro glycation levels of chicken albumin increase at a slower rate than those of human albumin when glucose concentration is elevated [71]. Moreover, these levels are consistently lower than those of bovine serum albumin regardless of glucose concentration and exposition time [34].…”
Section: Bird Glycemia Appears Affected By Body Mass and Maximum Life...supporting
confidence: 91%
“…However, the logarithmic nature of the relationship, together with a scaling factor lower than 1, suggests that species with higher plasma glucose levels exhibit relatively greater resistance to glycation. This finding aligns with previous research indicating that in vitro glycation levels of chicken albumin increase at a slower rate than those of human albumin when glucose concentration is elevated [71]. Moreover, these levels are consistently lower than those of bovine serum albumin regardless of glucose concentration and exposition time [34].…”
Section: Bird Glycemia Appears Affected By Body Mass and Maximum Life...supporting
confidence: 91%
“…This site specificity obviously depends on the amino acid composition of a given protein, but also and above all, on its multidimensional conformation, with theoretically glycatable amino acids being either exposed at the surface or, on the contrary, inaccessible because hidden. Thus, the lower number of lysines in chicken albumin and the fact that most of these residues are located in the inner part of the protein (only one lysine on the surface) seem to explain why it is glycated at a lower rate than bovine or human albumin (three lysines on the surface) when exposed to the same increasing concentrations of glucose [ 102 , 103 ]. Moreover, the presence of certain amino acids (such as aspartic acid or specific binding sites for phosphate or phosphorylated molecules) in the neighbourhood of the preferential glycation sites also seems to be of importance [ 104 ].…”
Section: Mechanisms Of Glycation Resistance That Need To Be Explored ...mentioning
confidence: 99%
“…Despite the high plasma glucose concentrations and documented insulin resistance (Braun & Sweazea, 2008;Sweazea & Braun, 2005), birds do not develop any 2 of 6 | MOORADIAN AND HAAS known complications of diabetes, and they outlive mammals of comparable body size (Braun & Sweazea, 2008;Holmes et al, 2001;Speakman, 2005). This natural resistance to hyperglycemia-related tissue damage has been attributed partly to reduced protein glycation (Zuck et al, 2017), higher levels of carbonyl-scavenging amino acids in plasma (Szwergold and Miller, 2014), and lack of the gene for the receptor for advanced glycation endproducts (RAGE) (Sessa et al, 2014). However, the absence of RAGE in birds has yet to be confirmed at the protein level and species-specific differences in defenses against oxidative stress may also be important for the ability of birds to live with chronic relative hyperglycemia (Klandorf et al, 2001).…”
Section: Introductionmentioning
confidence: 99%