The mechanism of the form a of aldose redustase formation in diabetes mellitus. the probable regulation of the enzyme activities in the result of the impairments of the thiol/disulfide exchange in diabetes mellitus

Rabinovich S.E., Shono N.I., Platonova L.V., Diuzheva T.G., Galperin E.I.
Year: 1997  Volume: 43  Issue: 2  Pages: 104-111
Incubation of form b (Km 3,0-4,0 mM; Vmax 4,38+0,6 mE/D) of aldose reductase (AR; E.C. from the human red cells in the oxygen radical generating systems or treatment by the abundance of the concentrations of GSSG (10 mM) caused the increase of specific activity (Vmax 10,0 mE/D), decrease of the affinity for D-glucose (Km 25,4 mM) and alterations of the chromatographic properties of the enzyme. The modified form b of AR has very similar properties with form a of this enzyme (Km 6,5-19,0 mM; Vmax 16,7+3,2 mE/D), that had been found in red cell of the diabeties mellitus. The treatment of the modified form b or form a by GSH (10 mM) caused the appearence of the AR that has very similar properties with form b. On the bases of thise results the main role of SH-groups of AR in the interconversion of the form b and a is concluded. It is suggested that the increase of the lipid peroxidation may be one of the reasons of the formation of the form a AR, because the product of the lipid peroxidation can oxidize the SH-groups of the protein and enzymes or cause the increase of GSSG in the cell. Alteration of the properties of the carbohydrate metabolism's enzymes in the result of the impairment of the thiol/disulfide ezchange in diabetes mellitus is discussed.
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Rabinovich S.E., Shono N.I., Platonova L.V., Diuzheva T.G., Galperin E.I. (1997) Voprosy meditsinskoi khimii, 43(2), 104-111.
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