Study of SOD1-mediated mechanism of glucose uptake into erythrocytes
Keywords:
human erythrocytes; superoxide dismutase; oxidative stress; casein kinasesAbstract
Superoxide dismutase is an enzyme that catalyzes the disproportionation of superoxide radicals to hydrogen peroxide and molecular oxygen. Using spectrophotometric and kinetic methods, we studied the change in SOD1 activity in human erythrocytes, which were incubated for five hours at 20 ° C in an oxidizing medium of the composition AscH – 1×10-4 М, Cu2+ – 5×10-6 М with different glucose content (from 0 up to 50 mM). Based on the experimental data obtained, it was assumed that, in the presence of glucose, SOD1 participates in the stabilization of two homologues of 1-gamma (CK1γ) casein kinase, Yck1p and Yck2p, which are required to suppress oxygen binding and enhance glycolysis. It was shown that the change in SOD1 activity occurs due to binding to the erythrocyte membrane and to the cytoplasmic degron Yck1p / Yck2p.
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