NDLI: Mechanism of Lysine Oxidation in Human Lens Crystallins during Aging and in Diabetes

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Mechanism of Lysine Oxidation in Human Lens Crystallins during Aging and in Diabetes

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Mechanism of Lysine Oxidation in Human Lens Crystallins during Aging and in Diabetes

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Nemet, Ina Monnier, Vincent M. Fan, Xingjun Strauch, Christopher Qian, Juan Zhang, Jianye Theves, Mathilde Giblin, Frank J. Liu, Xiaoqin
Description	Author Affiliation: Fan X ( Department of Pathology, Case Western Reserve University, Cleveland, Ohio 44106 , USA.)
Abstract	Oxidative mechanisms during nuclear sclerosis of the lens are poorly understood, in particular metal-catalyzed oxidation. The lysyl oxidation product adipic semialdehyde (allysine, ALL) and its oxidized end-product 2-aminoadipic acid (2-AAA) were determined as a function of age and presence of diabetes. Surprisingly, whereas both ALL and 2-AAA increased with age and strongly correlated with cataract grade and protein absorbance at 350 nm, only ALL formation but not 2-AAA was increased by diabetes. To clarify the mechanism of oxidation, rabbit lenses were treated with hyperbaric oxygen (HBO) for 48 h, and proteins were analyzed by gas and liquid chromatography mass spectrometry for ALL, 2-AAA, and multiple glycation products. Upon exposure to HBO, rabbit lenses were swollen, and nuclei were yellow. Protein-bound ALL increased 8-fold in the nuclear protein fractions versus controls. A dramatic increase in methyl-glyoxal hydroimidazolone and carboxyethyl-lysine but no increase of 2-AAA occurred, suggesting more drastic conditions are needed to oxidize ALL into 2-AAA. Indeed the latter formed only upon depletion of glutathione and was catalyzed by H(2)O(2). Neither carboxymethyl-lysine nor glyoxal hydroimidazolone, two markers of glyco-/lipoxidation, nor markers of lenticular glycemia (fructose-lysine, glucospane) were elevated by HBO, excluding significant lipid peroxidation and glucose involvement. The findings strongly implicate dicarbonyl/metal catalyzed oxidation of lysine to allysine, whereby low GSH combined with ascorbate-derived H(2)O(2) likely contributes toward 2-AAA formation, since virtually no 2-AAA formed in the presence of methylglyoxal instead of ascorbate. An important translational conclusion is that chelating agents might help delay nuclear sclerosis.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	50
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-12-11
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Aging Physiology Crystallins Metabolism Diabetes Mellitus Lens, Crystalline Lysine 2-Aminoadipic Acid Analogs & Derivatives Adolescent Animals Chemistry Genetics Pathology Hydrogen Peroxide Hyperbaric Oxygenation Leucine Mice Mice, Inbred C57BL Molecular Structure Oxidants Oxidation-Reduction Rabbits Regression Analysis Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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