In vitro inhibition of topoisomerase IIα by reduced glutathione. | Zendy

Zahid M. Delwar | Zendy; Marina Vita | Zendy; Åke Sidén | Zendy; Mabel Cruz | Zendy; Juan Sebastián Yakisich | Zendy

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In vitro inhibition of topoisomerase IIα by reduced glutathione.

Author(s) -

Zahid M. Delwar,

Marina Vita,

Åke Sidén,

Mabel Cruz,

Juan Sebastián Yakisich

Publication year - 2011

Publication title -

acta biochimica polonica

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.452

H-Index - 78

eISSN - 1734-154X

pISSN - 0001-527X

DOI - 10.18388/abp.2011_2276

Subject(s) - glutathione , thiol , glutathione disulfide , topoisomerase , chemistry , intracellular , in vitro , biochemistry , in vivo , redox , reactive oxygen species , enzyme , biology , microbiology and biotechnology , organic chemistry

In most cells, the major intracellular redox buffer is glutathione (GSH) and its disulfide-oxidized (GSSG) form. The GSH/GSSG system maintains the intracellular redox balance and the essential thiol status of proteins by thiol disulfide exchange. Topoisomerases are thiol proteins and are a target of thiol-reactive substances. In this study, the inhibitory effect of physiological concentration of GSH and GSSG on topoisomerase IIα activity in vitro was investigated. GSH (0-10 mM) inhibited topoisomerase IIα in a concentration-dependent manner while GSSG (1-100 µM) had no significant effect. These findings suggest that the GSH/GSSG system could have a potential in vivo role in regulating topoisomerase IIα activity.

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