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β‐Hydroxypyruvate induced side chain modification of human serum albumin and the formation of advanced glycation end‐products (AGEs)
Author(s) -
Liu Weixi,
Dain Joel A
Publication year - 2016
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.30.1_supplement.864.21
Subject(s) - glycation , chemistry , incubation , human serum albumin , pentosidine , lysine , arginine , albumin , circular dichroism , diabetes mellitus , endocrinology , medicine , serum albumin , methylglyoxal , biochemistry , amino acid , biology , enzyme , receptor
Glycation of human serum albumin (HSA) results in the formation of advanced glycation end‐productis (AGEs), a major contributor to the pathology of diabetes and aging. Recently, β‐hydroxypyruvate (β‐HP) was proposed to be a new diabetogenic factor as increased plasma levels of β‐HP were reported in diabetic mellitus. However, the exact role of β‐HP in the progression of diabetic pathology is not known. Herein, we report for the first time the in vitro HSA glycation and AGE formation by β‐HP. At physiological temperature and pH, β‐HP readily glycated HSA at concentrations ranging from 1 to 1000 μM. Modified lysine and arginine residues of HSA formed within 24 hr incubation. AGE formation was observed with prolonged incubation by florescence (FL). Intrinsic fluorescence and HPLC‐FL both detected pentosidine formation after 72 hr incubation in a concentration dependent manner. AGE formation also caused structural alteration of HSA, as measured by circular dichroism and zeta‐sizer. The content of α‐helical structure of HSA decreased 38% after 72 hr incubation with β‐HP, accompanied by an increase of β‐strands and random coil. A glycation and AGE formation of HSA by β‐HP suggest that this may contribute to the pathology of diabetes. Further studies focusing on mass spectrometry are in progress to elucidate the AGE structures formed by HSA from β‐HP.