Abstract
NADPH-dependent oxidoreductases of the aldo-keto reductase family are widely distributed in man and animals (Wirth and Wermuth, 1985; Wermuth, 1985; Grimshaw and Mathur, 1989; Carper et al., 1987). The broad overlapping substrate specificities of these enzymes in the reduction of aldehydes and ketones suggests a role in detoxification of reactive carbonyls. Aldose reductase (EC 1.1.1.21; alditol: NAD(P) oxidoreductase) has received special attention because of its possible role in the development of diabetic complications (Gabbay, 1973; Kador and Kinoshita, 1985). Aldose reductase catalyzes the reduction of glucose to sorbitol in the polyol pathway which is normally a minor pathway for metabolism of glucose but may become important during hyperglycemia (Hers, 1956; Kador, 1988). Sorbitol accumulates in certain tissues that are prone to diabetic complications and may damage those tissues through a hyperosmotic mechanism (Kinoshita; 1974). Sorbitol may also interfere with the uptake and processing of myo-inositol, leading to impairment of cellular processes that are regulated by phosphatidylinositol metabolism (Greene et al., 1987; Finegold et al., 1983).
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Vander Jagt, D.L., Hunsaker, L.A. (1993). Substrate Specificity of Reduced and Oxidized Forms of Human Aldose Reductase. In: Weiner, H., Crabb, D.W., Flynn, T.G. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 4. Advances in Experimental Medicine and Biology, vol 328. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2904-0_30
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DOI: https://doi.org/10.1007/978-1-4615-2904-0_30
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