PubMed · 14959688
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Laurinda Poirier-Solomon. 2002. Slowing down.. https://pubmed.ncbi.nlm.nih.gov/14959688/
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BACKGROUND: Recent evidence has shown that hyperglycemia is able to cause increased production of superoxide on the mitochondrial transport chain, and that this is the key event which activates some events such as increased AGE formation, increased hexosamine and polyol flux, and activation of PKC, all believed to be important for the development of the chronic complications of diabetes, aging and uremia. In this context, non-enzymatic protein glyco-oxidation leads to the formation of a series of products whose intra- and extra-cellular accumulation is of key importance in the pathogenesis of these chronic diseases. METHODS: Various spectrometric approaches, such as matrix-assisted laser desorption ionisation (MALDI), and liquid chromatography-electrospray ionisation (ESI) were used. RESULTS AND CONCLUSIONS: The latest mass spectrometric approaches have shown their power in proteomics, and we report here some applications of this technique in the study of in vitro and in vivo non-enzymatic protein glyco-oxidation.
Capillary electrophoretic (CE) method was developed for the determination of urinary 3-methylhistidine (3MH) and 1-methylhistidine (1MH) indicating the extent of degradation of skeletal muscle proteins and thereby the state of human health. 3MH, 1MH and histidine can be separated in both acidic and alkaline media, where these amino acids form cation and anion, respectively. The effective mobility of all ionic forms was measured over a broad range of pH (1.67-11.80), which made it possible to evaluate the corresponding dissociation constants. 3MH and 1MH were determined together with creatinine in untreated urine samples with the limit of detection of 2.4 microM (0.4 mgL(-1)) and 3.0 microM (0.5 mgL(-1)), respectively. Determination was fast and took ca. 12 min including the column washing. Method was employed for an analysis of urine collected from healthy individuals, and from the patients hospitalized with obesity and diabetes mellitus II. This analysis has revealed differences between the healthy individuals and the patients pointing to a more extensive degradation of muscle proteins in the latter group.
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