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

✍ Scribed by F. S. Liotti; A. R. Menghini; P. Guerrieri; R. Bianchi

Publisher
John Wiley and Sons
Year
1989
Tongue
French
Weight
455 KB
Volume
43
Category
Article
ISSN
0020-7136

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✦ Synopsis

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 lH-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 'H-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.

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