Journal article

Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster


Authors listKanzok, SM; Fechner, A; Bauer, H; Ulschmid, JK; Müller, HM; Botella-Munoz, J; Schneuwly, S; Schirmer, RH; Becker, K

Publication year2001

Pages643-646

JournalScience

Volume number291

Issue number5504

ISSN0036-8075

eISSN1095-9203

DOI Linkhttps://doi.org/10.1126/science.291.5504.643

PublisherAmerican Association for the Advancement of Science


Abstract
The disulfide reducing enzymes glutathione reductase and thioredoxin reductase are highly conserved among bacteria, fungi, worms, and mammals. These proteins maintain intracellular redox homeostasis to protect the organism from oxidative damage. Here we demonstrate the absence of glutathione reductase in Drosophila melanogaster, identify a new type of thioredoxin reductase, and provide evidence that a thioredoxin system supports GSSG reduction. Our data suggest that antioxidant defense in Drosophila, and probably in related insects, differs fundamentally from that in other organisms.



Citation Styles

Harvard Citation styleKanzok, S., Fechner, A., Bauer, H., Ulschmid, J., Müller, H., Botella-Munoz, J., et al. (2001) Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster, Science, 291(5504), pp. 643-646. https://doi.org/10.1126/science.291.5504.643

APA Citation styleKanzok, S., Fechner, A., Bauer, H., Ulschmid, J., Müller, H., Botella-Munoz, J., Schneuwly, S., Schirmer, R., & Becker, K. (2001). Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster. Science. 291(5504), 643-646. https://doi.org/10.1126/science.291.5504.643


Last updated on 2025-21-05 at 16:01