Study of advanced glycation endproducts (AGEs) of human fibrinogen and nucleobases with methyl glyoxal: An in vitro investigation of ages formation
Advanced glycation endproducts (AGEs) are formed from the non-enzymatic interaction of reducing sugars and their metabolites with free amino acids in plasma or amino groups of proteins, lipids or nucleic acids. These are a heterogeneous group of molecules and can accumulate in plasma and tissues. AGEs are found to be responsible to the pathology of diabetes, Alzheimer’s disease, cataract formation and coronary heart disease. This current dissertation demonstrates the in-vitro formation of AGEs produced by the reaction of human Fibrinogen with MethylGlyoxal (MG). Results from HPLC and MALDI analysis supported the formation of three different types of Fib-MG AGEs or AGLEs species namely, Aggregated Insoluble AGE (AIsA), Partially De-Aggregated Soluble AGE (PDASA) and Non Aggregated Soluble AGEs (NASA).^ GTP and dGMP produced AGEs with methylglyoxal in vitro. Several analytical techniques including HPLC, UV, fluorescence, and mass spectrometry were applied to characterize the AGE’s of GTP and dGMP with methylglyoxal. UV and fluorescence spectrometry combined with HPLC demonstrated the in vitro AGEs formation of both GTP and dGMP with methylglyoxal. Mass spectrometry demonstrated that the condensation of GTP and dGMP with methyl glyoxal occurred via the classical Amadori pathway. ^
Chemistry, Analytical|Chemistry, Biochemistry|Health Sciences, Aging
Lasker S Lasker,
"Study of advanced glycation endproducts (AGEs) of human fibrinogen and nucleobases with methyl glyoxal: An in vitro investigation of ages formation"
Dissertations and Master's Theses (Campus Access).