Abstract
Non-enzymatic glycation of reactive amino groups in model proteins increased the rate of free radical production at physiologic pH by nearly fifty-fold over non-glycated protein. Superoxide generation was confirmed by electron paramagnetic resonance measurements with the spin-trap phenyl-t-butyl-nitrone. Both Schiff base and Amadori glycation products were found to generate free radicals in a ratio of 1:1.5. Free radicals generated by glycated protein increased peroxidation of membranes of linoleic/arachidonic acid vesicles nearly 2-fold over control, suggesting that the increased glycation of proteins in diabetes may accelerate vascular wall lipid oxidative modification.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Arteriosclerosis / etiology
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Arteriosclerosis / metabolism*
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Catalase / pharmacology
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Cell Membrane / drug effects
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Cell Membrane / metabolism
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Cyclic N-Oxides
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Cytochrome c Group / metabolism
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Diabetes Complications
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Diabetes Mellitus / metabolism*
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Electron Spin Resonance Spectroscopy
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Free Radicals
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Glucose / metabolism*
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Humans
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Hyperglycemia / complications
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Hyperglycemia / metabolism*
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Linoleic Acid
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Linoleic Acids / metabolism
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Lipid Peroxidation
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Nitroblue Tetrazolium / metabolism
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Nitrogen Oxides
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Schiff Bases / metabolism
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Spin Labels
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Superoxide Dismutase / pharmacology
Substances
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Cyclic N-Oxides
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Cytochrome c Group
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Free Radicals
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Linoleic Acids
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Nitrogen Oxides
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Schiff Bases
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Spin Labels
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Nitroblue Tetrazolium
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phenyl-N-tert-butylnitrone
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Linoleic Acid
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Catalase
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Superoxide Dismutase
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Glucose