Protein glycation in diabetes mellitus.

Diabetes mellitus is the ninth leading cause of mortality worldwide. It is a complex disease that manifests as chronic hyperglycemia. Glucose exposure causes biochemical changes at the proteome level as reflected in accumulation of glycated proteins.

Comprehensive profiling and kinetic studies of glycated lysine residues in human serum albumin.

Lysine residues of proteins slowly react with glucose forming Amadori products. In hyperglycemic conditions, such as diabetes mellitus, this non-enzymatic glycation becomes more pervasive causing severe medical complications. The structure and conformation of a protein predisposes lysine sites to differing reactivity influenced by their steric availability and amino acid microenvironment.

Quantitation of glycated albumin by isotope dilution mass spectrometry.

Background: Glycated albumin is considered an alternative glycemic indicator in certain situations where HbA1c does not accurately reflect glycemic status. These patient cases are usually associated with decreased erythrocyte lifespan, gestational diabetes, or end-stage renal disease. The aim of our study was to develop an assay for absolute quantitation of glycated albumin based on isotope dilution liquid chromatography-mass spectrometry.