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Production of advanced glycation end products from the glycosylation of avian serum albumin
Author(s) -
Braun Eldon,
Casotti Giovanni,
Di Bussolo Joe M.
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.6.a1197
Subject(s) - glycation , glycosylation , albumin , chemistry , biochemistry , serum albumin , blood proteins , incubation , in vitro , bovine serum albumin , diabetes mellitus , medicine , endocrinology , biology , receptor
Sustained, elevated plasma glucose concentrations in mammals (humans) leads to the glycosylation of serum albumin in a non‐enzymatic reaction. Through a series of chemical re‐arrangements of the glycated albumin, advanced glycation end products (AGEs) form that lead to the pathologies characteristic of Type 2 diabetes. Birds, as a normal aspect of their physiology, have plasma glucose concentrations that by mammalian standards are diabetic, yet they do not suffer the pathologies associated with diabetes. The physiological mechanisms that have evolved allowing birds to escape these pathologies are not understood. In vitro experiments were conducted to assess the degree of glycosylation of avian serum albumin over time. Non‐glycosylation and glycated albumin were separated using HPLC. The AGEs formed were quantified using a tandem HPLC‐mass spectrometer (LC‐MS/MS) system following turbulent‐flow on‐line extraction. Data will be presented describing the degree of glycosylation of avian albumin and the AGEs formed during in vitro incubation.