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Journal of Ophthalmology
Volume 2010 (2010), Article ID 274317, 7 pages
Inhibition of Methylglyoxal-Mediated Protein Modification in Glyoxalase I Overexpressing Mouse Lenses
1Department of Ophthalmology & Visual Sciences, Case Western Reserve University, Cleveland, OH 44106, USA
2Mason Eye Institute, University of Missouri, Columbia, MO 65212, USA
Received 1 March 2010; Accepted 1 June 2010
Academic Editor: Mark Petrash
Copyright © 2010 Mahesha H. Gangadhariah 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.
- A. J. Bron, G. F. J. M. Vrensen, J. Koretz, G. Maraini, and J. J. Harding, “The ageing lens,” Ophthalmologica, vol. 214, no. 1, pp. 86–104, 2000.
- V. Monnier and D. Sell, “Aging of long-lived proteins: extracellular matrix (collagens, elastins, proteoglycans) and lens crystallins,” in Handbook of Physiology, E. J. Masoro, Ed., pp. 235–305, Oxford University Press, New York, NY, USA, 1995.
- K. M. Bieme, D. A. Fried, and M. O. Lederer, “Identification and quantification of major Maillard cross-links in human serum albumin and lens protein: evidence for glucosepane as the dominant compound,” Journal of Biological Chemistry, vol. 277, no. 28, pp. 24907–24915, 2002.
- R. H. Nagaraj, D. R. Sell, M. Prabhakaram, B. J. Ortwerth, and V. M. Monnier, “High correlation between pentosidine protein crosslinks and pigmentation implicates ascorbate oxidation in human lens senescence and cataractogenesis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 88, no. 22, pp. 10257–10261, 1991.
- M. U. Ahmed, E. Brinkmann Frye, T. P. Degenhardt, S. R. Thorpe, and J. W. Baynes, “Nε-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins,” Biochemical Journal, vol. 324, no. 2, part 2, pp. 565–570, 1997.
- R. H. Nagaraj and C. Sady, “The presence of a glucose-derived Maillard reaction product in the human lens,” FEBS Letters, vol. 382, no. 3, pp. 234–238, 1996.
- R. Cheng, Q. Feng, O. K. Argirov, and B. J. Ortwerth, “Structure elucidation of a novel yellow chromophore from human lens protein,” Journal of Biological Chemistry, vol. 279, no. 44, pp. 45441–45449, 2004.
- F. Tessier, M. Obrenovich, and V. M. Monnier, “Structure and mechanism of formation of human lens fluorophore LM-1. Relationship to vesperlysine A and the advanced Maillard reaction in aging, diabetes, and cataractogenesis,” Journal of Biological Chemistry, vol. 274, no. 30, pp. 20796–20804, 1999.
- P. J. Thornalley, “Pharmacology of methylglyoxal: formation, modification of proteins and nucleic acids, and enzymatic detoxification—a role in pathogenesis and antiproliferative chemotherapy,” General Pharmacology, vol. 27, no. 4, pp. 565–573, 1996.
- T. W. C. Lo, M. E. Westwood, A. C. McLellan, T. Selwood, and P. J. Thornalley, “Binding and modification of proteins by methylglyoxal under physiological conditions: a kinetic and mechanistic study with Nα-acetylarginine, Nα-acetylcysteine, and Nα-acetyllysine, and bovine serum albumin,” Journal of Biological Chemistry, vol. 269, no. 51, pp. 32299–32305, 1994.
- P. Chellan and R. H. Nagaraj, “Protein crosslinking by the Maillard reaction: dicarbonyl-derived imidazolium crosslinks in aging and diabetes,” Archives of Biochemistry and Biophysics, vol. 368, no. 1, pp. 98–104, 1999.
- P. S. Padayatti, A. S. Ng, K. Ucbida, M. A. Glomb, and R. H. Nagaraj, “Argpyrimidine, a blue fluorophore in human lens proteins: high levels in brunescent cataractous lenses,” Investigative Ophthalmology and Visual Science, vol. 42, no. 6, pp. 1299–1304, 2001.
- N. Ahmed, P. J. Thornalley, J. Dawczynski et al., “Methylglyoxal-derived HI advanced glycation end-products of human lens proteins,” Investigative Ophthalmology and Visual Science, vol. 44, no. 12, pp. 5287–5292, 2003.
- D. L. Vander Jagt, R. K. Hassebrook, L. A. Hunsaker, W. M. Brown, and R. E. Royer, “Metabolism of the 2-oxoaldehyde methylglyoxal by aldose reductase and by glyoxalase-I: roles for glutathione in both enzymes and implications for diabetic complications,” Chemico-Biological Interactions, vol. 130-132, pp. 549–562, 2001.
- P. J. Thornalley, “The glyoxalase system in health and disease,” Molecular Aspects of Medicine, vol. 14, no. 4, pp. 287–371, 1993.
- M. Shinohara, P. J. Thornalley, I. Giardino et al., “Overexpression of glyoxalase-I in bovine endothelial cells inhibits intracellular advanced glycation endproduct formation and prevents hyperglycemia-induced increases in macromolecular endocytosis,” Journal of Clinical Investigation, vol. 101, no. 5, pp. 1142–1147, 1998.
- P. S. Padayatti, C. Jiang, M. A. Glomb, K. Uchida, and R. H. Nagaraj, “High concentrations of glucose induce synthesis of argpyrimidine in retinal endothelial cells,” Current Eye Research, vol. 23, no. 2, pp. 106–115, 2001.
- A. G. Miller, D. G. Smith, M. Bhat, and R. H. Nagaraj, “Glyoxalase I is critical for human retinal capillary pericyte survival under hyperglycemic conditions,” Journal of Biological Chemistry, vol. 281, no. 17, pp. 11864–11871, 2006.
- M. M. Staniszewska and R. H. Nagaraj, “Upregulation of glyoxalase I fails to normalize methylglyoxal levels: a possible mechanism for biochemical changes in diabetic mouse lenses,” Molecular and Cellular Biochemistry, vol. 288, no. 1-2, pp. 29–36, 2006.
- F. A. Shamsi, E. Sharkey, D. Creighton, and R. H. Nagaraj, “Maillard reactions in lens proteins: methylglyoxal-mediated modifications in the rat lens,” Experimental Eye Research, vol. 70, no. 3, pp. 369–380, 2000.
- L. W. Reneker, Q. Chen, A. Bloch, L. Xie, G. Schuster, and P. A. Overbeek, “Chick δ1-crystallin enhancer influences mouse αA-crystallin promoter activity in transgenic mice,” Investigative Ophthalmology and Visual Science, vol. 45, no. 11, pp. 4083–4090, 2004.
- M. Mailankot, S. Padmanabha, N. Pasupuleti, D. Major, S. Howell, and R. H. Nagaraj, “Glyoxalase I activity and immunoreactivity in the aging human lens,” Biogerontology, vol. 10, no. 6, pp. 711–720, 2009.
- A. Espinosa-Mansilla, I. Durán-Merás, and F. Salinas, “High-performance liquid chromatographic-fluorometric determination of glyoxal, methylglyoxal, and diacetyl in urine by prederivatization to pteridinic rings,” Analytical Biochemistry, vol. 255, no. 2, pp. 263–273, 1998.
- X.-L. Cui and M. F. Lou, “The effect and recovery of long-term exposure on lenss morphology and biochemistry,” Experimental Eye Research, vol. 57, no. 2, pp. 157–167, 1993.
- S. C. Wilker, P. Chellan, B. M. Arnold, and R. H. Nagaraj, “Chromatographic quantification of argpyrimidine, a methylglyoxal-derived product in tissue proteins: comparison with pentosidine,” Analytical Biochemistry, vol. 290, no. 2, pp. 353–358, 2001.
- S. Puttaiah, A. Biswas, M. Staniszewska, and R. H. Nagaraj, “Methylglyoxal inhibits glycation-mediated loss in chaperone function and synthesis of pentosidine in α-crystallin,” Experimental Eye Research, vol. 84, no. 5, pp. 914–921, 2007.
- T. Kumagai, M. Nangaku, I. Kojima et al., “Glyoxalase I overexpression ameliorates renal ischemia-reperfusion injury in rats,” American Journal of Physiology, vol. 296, no. 4, pp. F912–F921, 2009.
- M. Morcos, X. Du, F. Pfisterer et al., “Glyoxalase-1 prevents mitochondrial protein modification and enhances lifespan in Caenorhabditis elegans,” Aging Cell, vol. 7, no. 2, pp. 260–269, 2008.
- D. R. Sell and V. M. Monnir, “Structure elucidation of a senescence cross-link from human extracellular matrix. Implication of pentoses in the aging process,” Journal of Biological Chemistry, vol. 264, no. 36, pp. 21597–21602, 1989.
- I. N. Shipanova, M. A. Glomb, and R. H. Nagaraj, “Protein modification by methylglyoxal: chemical nature and synthetic mechanism of a major fluorescent adduct,” Archives of Biochemistry and Biophysics, vol. 344, no. 1, pp. 29–36, 1997.
- R. H. Nagaraj, T. Oya-Ito, P. S. Padayatti et al., “Enhancement of chaperone function of α-crystallin by methylglyoxal modification,” Biochemistry, vol. 42, no. 36, pp. 10746–10755, 2003.
- A. Biswas, S. Lewis, B. Wang et al., “Chemical modulation of the chaperone function of human αA-crystallin,” Journal of Biochemistry, vol. 144, no. 1, pp. 21–32, 2008.