Effects of dimethylsulfoxide on friend erythroleukemic cell proliferation and on the activity of enzymes involved in this process

Abstract

Variations in catalase, glutathione peroxidase (GP) and adenylate cyclase (AC) activity in murine erythroleukemic (MEL) cells were studied during multiplication and dimethylsulfoxide (DMSO)-induced differentiation. The results demonstrated that, although DMSO favors the incorporation of 3H-thymidine into DNA of treated cells, it slows down cell multiplication. Increased incorporation was also observed in superoxide dismutase (SOD)-treated cells. DMSO also determined an early and significant drop in AC activity and a late fall in catalase activity, whereas there was no significant variation in GP activity in parallel with the decreased cell multiplication that accompanied cell differentiation. We hypothesize that DMSO and SOD favor 3H-thymidine incorporation by neutralizing the reactive forms of oxygen and that the reduction in catalase and AC activity is closely related to the mitotic activity of MEL cells.

Ferricytochrome c Directly Oxidizes Aminoacetone to Methylglyoxal, a Catabolite Accumulated in Carbonyl Stress

“…Expectedly, CuZnSOD addition was highly efficient in decreasing the signal of the DMSO-derived methyl radical (Figure 3B, trace e), whereas 15 µM catalase had little effect on the EPR signal amplitude obtained with 150 µM ferricyt c and 15 mM AA (data not shown). Because DMSO is known to lessen the catalase activity [40], ESR spin-trapping experiments were performed using DMPO/ethanol to demonstrate that H 2 O 2 is the main source of HO • radical in the AA/ferricyt c system (Figure 3C). Ethanol is known to be harmless to catalase and can be oxidized by HO • radical to an α-hydroxyethyl radical yielding the stable adduct DMPO- • CHOH-CH 3 (a H  = 2.28 mT; a N  = 1.58 mT) [41].…”