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Mass spectrometric study on the protein chemical modification of uremic patients in advanced Maillard reaction
Affiliation:1. Departamento de Nutrición y Bromatología, Toxicología y Medicina Legal, Facultad de Farmacia, Universidad de Sevilla, C/ Profesor García González 2, 41012 Sevilla, Spain;2. Departamento de Biología Molecular e Ingeniería Bioquímica, Universidad Pablo de Olavide, Ctra. Utrera, Km 1, Sevilla 41013, Spain;3. Departament de Bioquimica i Biotecnologia, Facultat d’Enologia, Universitat Rovira i Virgili, C/ Marcel·lí Domingo 1, Campus, Sescelades 43007, Tarragona, Spain;1. Teagasc Food Research Centre, Ashtown, Dublin 15, Ireland;2. School of Agriculture and Food Science, University College Dublin, Dublin 4, Ireland
Abstract:The Maillard reaction, initiated by the nonenzymatic reaction of reducing sugar with protein, is proposed to play a significant role in protein aging and the complications of aging and diabetes. In this study, we detected and quantified some advanced glycation endproducts (AGEs) in human serum proteins of control and uremic patients by a highly selective and specific assay, electrospray ionization liquid chromatography–mass spectrometry–mass spectrometry (ESI-LC–MS–MS). From our results, levels of each AGEs in serum of uremic patients were significantly elevated, compared to age-matched controls. These results provide the evidence for increased modifications of proteins by Maillard reaction in uremia.
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