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International Journal of Endocrinology
Volume 2013 (2013), Article ID 412103, 11 pages
Protein Glycation in Diabetes as Determined by Mass Spectrometry
1Department of Medicine, Padova University, Via Giustiniani 2, I35100 Padova, Italy
2National Council of Researches, Institute of Molecular Sciences and Technologies, Corso Stati Uniti 4, I35127 Padova, Italy
Received 9 January 2013; Accepted 12 February 2013
Academic Editor: Roberto Miccoli
Copyright © 2013 Annunziata Lapolla et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- J. E. Shaw, R. A. Sicree, and P. Z. Zimmet, “Global estimates of the prevalence of diabetes for 2010 and 2030,” Diabetes Research and Clinical Practice, vol. 87, no. 1, pp. 4–14, 2010.
- L. C. Maillard, “Action des acides aminés sur les sucres: formation des mélanoïdines par voie méthodique,” Compte-Rendu De L'Académie Des Sciences, pp. 66–68, 1912.
- R. Bucala, P. Model, and A. Cerami, “Modification of DNA by reducing sugars: a possible mechanism for nucleic acid aging and age-related dysfunction in gene expression,” Proceedings of the National Academy of Sciences of the United States of America, vol. 81, no. 1, pp. 105–109, 1984.
- S. Waris, M. Pischetsrieder, and M. Saleemuddin, “DNA damage by ribose: inhibition at high ribose concentrations,” Indian Journal of Biochemistry and Biophysics, vol. 47, no. 3, pp. 148–156, 2010.
- A. Lapolla, D. Fedele, R. Seraglia et al., “A new effective method for the evaluation of glycated intact plasma proteins in diabetic subjects,” Diabetologia, vol. 38, no. 9, pp. 1076–1081, 1995.
- A. Lapolla, D. Fedele, R. Aronica et al., “Evaluation of IgG Levels by matrix assisted laser desorption/ionization mass spectrometry,” Rapid Communications in Mass Spectrometry, vol. 11, no. 12, pp. 1342–1346, 1997.
- K. R. Clauser, P. Baker, and A. L. Burlingame, “Role of accurate mass measurement (±10 ppm) in protein identification strategies employing MS or MS/MS and database searching,” Analytical Chemistry, vol. 71, no. 14, pp. 2871–2882, 1999.
- M. Hamdan and P. G. Righetti, Proteomics Today, Jhon Wiley & Sons, Hoboken, NJ, USA, 2005.
- B. Thiede, W. Höhenwarter, A. Krah et al., “Peptide mass fingerprinting,” Methods, vol. 35, no. 3, pp. 237–247, 2005.
- C. Dass, Fundamentals of Contemporary Mass Spectrometry, Jhon Wiley and Sons, Hoboken, NJ, USA, 2007.
- A. Lapolla, C. Gerhardinger, L. Baldo et al., “A study on in vitro glycation processes by matrix-assisted laser desorption ionization mass spectrometry,” Biochimica et Biophysica Acta, vol. 1225, no. 1, pp. 33–38, 1993.
- A. Lapolla, D. Fedele, R. Seraglia, S. Catinella, and P. Traldi, “Matrix-assisted laser desorption/ionization capabilities in the study of non-enzymatic protein glycation,” Rapid Communications in Mass Spectrometry, vol. 8, no. 8, pp. 645–652, 1994.
- A. Lapolla, L. Baldo, R. Aronica et al., “Matrix-assisted laser desorption/ionization mass spectrometric studies on protein glycation. 2. The reaction of ribonuclease with hexoses,” Biological Mass Spectrometry, vol. 23, no. 5, pp. 241–248, 1994.
- A. Lapolla, D. Fedele, R. Aronica et al., “The in vitro glycation of lysozyme and the influence of buffer concentration investigated by mass spectrometry,” Rapid Communication in Mass Spectrometry, vol. 10, no. 12, pp. 1512–1518, 1996.
- P. Traldi, D. Favretto, R. Seraglia, and A. Lapolla, “Mass spectrometry in the study of non-enzymatic glyco-oxidation of proteins,” Rapid Communication in Mass Spectrometry, vol. 11, no. 6, pp. 673–678, 1997.
- A. Lapolla, D. Fedele, R. Aronica et al., “Evaluation of IgG glycation levels by matrix-assisted laser desorption/ionization mass spectrometry,” Rapid Communication in Mass Spectrometry, vol. 11, no. 12, pp. 1342–1346, 1997.
- V. M. Monnier, “The fructosamine 3-kinase knockout mouse: a tool for testing the glycation hypothesis of intracellular protein damage in diabetes and aging,” The Biochemical Journal, vol. 399, no. 2, pp. e11–e13, 2006.
- B. S. Szwergold and P. J. Beisswenger, “Enzymatic deglycation—a new paradigm or an epiphenomenon?” Biochemical Society Transactions, vol. 31, no. 6, pp. 1428–1432, 2003.
- J. R. Conner, P. J. Beisswenger, and B. S. Szwergold, “Some clues as to the regulation, expression, function, and distribution of fructosamine-3-kinase and fructosamine-3-kinase-related protein,” Annals of the New York Academy of Sciences, vol. 1043, pp. 824–836, 2005.
- G. Delpierre, M. Veiga-da-Cunha, D. Vertommen, M. Buysschaert, and E. Van Schaftingen, “Variability in erythrocyte fructosamine 3-kinase activity in humans correlates with polymorphisms in the FN3K gene and impacts on haemoglobin glycation at specific sites,” Diabetes and Metabolism, vol. 32, no. 1, pp. 31–39, 2006.
- M. Mohás, P. Kisfali, E. Baricza et al., “A polymorphism within the fructosamine-3-kinase gene is associated with HbA1c levels and the onset of type 2 diabetes mellitus,” Experimental and Clinical Endocrinology and Diabetes, vol. 118, no. 3, pp. 209–212, 2010.
- L. Mosca, S. Penco, M. C. Patrosso et al., “Genetic variability of the fructosamine 3-kinase gene in diabetic patients,” Clinical Chemistry and Laboratory Medicine, vol. 49, no. 5, pp. 803–808, 2011.
- E. Marotta, A. Lapolla, D. Fedele et al., “Accurate mass measurements by Fourier transform mass spectrometry in the study of advanced glycation end products/peptides,” Journal of Mass Spectrometry, vol. 38, no. 2, pp. 196–205, 2003.
- A. Lapolla, D. Fedele, R. Reitano et al., “Enzymatic digestion and mass spectrometry in the study of advanced glycation end products/peptides,” Journal of the American Society for Mass Spectrometry, vol. 15, no. 4, pp. 496–509, 2004.
- A. Lapolla, D. Fedele, R. Aronica et al., “The in vivo glyco-oxidation of α- and β-globins investigated by matrix assisted laser desorption/ionization mass spectrometry,” Rapid Communications in Mass Spectrometry, vol. 10, no. 9, pp. 1133–1135, 1996.
- A. Lapolla, D. Fedele, R. Aronica et al., “A highly specific method for the characterization of glycation and glycooxidation products of globins,” Rapid Communications in Mass Spectrometry, vol. 11, no. 6, pp. 613–617, 1997.
- A. Lapolla, D. Fedele, M. Plebani et al., “Direct evaluation of glycated and glyco-oxidized globins by matrix-assisted laser desorption/ionization mass spectrometry,” Rapid Communications in Mass Spectrometry, vol. 13, no. 1, pp. 8–14, 1999.
- A. Lapolla, D. Fedele, M. Plebani et al., “Evaluation of glycated globins by matrix-assisted laser desorption/ionization mass spectrometry,” Clinical Chemistry, vol. 45, no. 2, pp. 288–290, 1999.
- J. M. Hempe, R. Gomez, R. J. McCarter, and S. A. Chalew, “High and low hemoglobin glycation phenotypes in type 1 diabetes: a challenge for interpretation of glycemic control,” Journal of Diabetes and its Complications, vol. 16, no. 5, pp. 313–320, 2002.
- A. Lapolla, M. Brioschi, C. Banfi et al., “On the search for glycated lipoprotein ApoA-I in the plasma of diabetic and nephropathic patients,” Journal of Mass Spectrometry, vol. 43, no. 1, pp. 74–81, 2008.
- J. Janke, S. Engeli, M. Boschmann et al., “Retinol-binding protein 4 in human obesity,” Diabetes, vol. 55, no. 10, pp. 2805–2810, 2006.
- J. Shea, E. Randell, S. Vasdev, P. P. Wang, B. Roebothan, and G. Sun, “Serum retinol-binding protein 4 concentrations in response to shortterm overfeeding in normal-weight, overweight, and obese men,” American Journal of Clinical Nutrition, vol. 86, no. 5, pp. 1310–1315, 2007.
- P. Chaurand, F. Luetzenkirchen, and B. Spengler, “Peptide and protein identification by matrix-assisted laser desorption ionization (MALDI) and MALDI-post-source decay time-of-flight mass spectrometry,” Journal of the American Society for Mass Spectrometry, vol. 10, no. 2, pp. 91–103, 1999.
- U.S. Renal Data System, URDS 2001 Annual Data Report: Atlas of End-Stage Renal Disease in the United States, National Institute of Health, National Institutre of Diabetes, Bethesda, Md, USA, 2001.
- P. Gaede, P. Vedel, H. H. Parving, and O. Pedersen, “Intensified multifactorial intervention in patients with type 2 diabetes mellitus and microalbuminuria: the Steno type 2 randomised study,” The Lancet, vol. 353, no. 9153, pp. 617–622, 1999.
- D. Gorman, E. Sochett, and D. Daneman, “The natural history of microalbuminuria in adolescents with type 1 diabetes,” Journal of Pediatrics, vol. 134, no. 3, pp. 333–337, 1999.
- H. H. Parving, N. Chaturvedi, G. Viberti, and C. E. Mogensen, “Does microalbuminuria predict diabetic nephropathy?” Diabetes Care, vol. 24, no. 9, pp. 1560–1566, 2001.
- M. L. Caramori, P. Fioretto, and M. Mauer, “The need for early predictors of diabetic nephropathy risk: is albumin excretion rate sufficient?” Diabetes, vol. 49, no. 9, pp. 1399–1408, 2000.
- H. H. Parving, H. Lehnert, J. Brochner-Mortensen, R. Gomis, S. Andersen, and P. Arner, “The effect of irbesartan on the development of diabetic nephropathy in patients with type 2 diabetes,” New England Journal of Medicine, vol. 345, no. 12, pp. 870–878, 2001.
- P. V. Rao, X. Lu, M. Standley et al., “Proteomic identification of urinary biomarkers of diabetic nephropathy,” Diabetes Care, vol. 30, no. 3, pp. 629–637, 2007.
- D. M. Good, P. Zürbig, A. Argiles et al., “Naturally occurring human urinary peptides for use in diagnosis of chronic kidney disease,” Molecular and Cellular Proteomics, vol. 9, no. 11, pp. 2424–2437, 2010.
- A. Lapolla, R. Seraglia, L. Molin et al., “Low molecular weight proteins in urines from healthy subjects as well as diabetic, nephropathic and diabetic-nephropathic patients: a MALDI study,” Journal of Mass Spectrometry, vol. 44, no. 3, pp. 419–425, 2009.
- L. Molin, R. Seraglia, A. Lapolla et al., “A comparison between MALDI-MS and CE-MS data for biomarker assessment in chronic kidney diseases,” Journal of Proteomics, vol. 75, no. 18, pp. 5888–5897, 2012.