A putative glutathione peroxidase of Drosophila encodes a thioredoxin peroxidase that provides resistance against oxidative stress but fails to complement a lack of catalase activity - Research portal of Justus Liebig University Giessen:

Journal article

A putative glutathione peroxidase of Drosophila encodes a thioredoxin peroxidase that provides resistance against oxidative stress but fails to complement a lack of catalase activity

Authors list: Missirlis, F; Rahlfs, S; Dimopoulos, N; Bauer, H; Becker, K; Hilliker, A; Phillips, JP; Jäckle, H

Publication year: 2003

Pages: 463-472

Journal: Biological Chemistry

Volume number: 384

Issue number: 3

ISSN: 1431-6730

eISSN: 1437-4315

DOI Link: https://doi.org/10.1515/BC.2003.052

Publisher: De Gruyter Brill

Abstract:
Cellular defense systems against reactive oxygen species (ROS) include thioredoxin reductase (TrxR) and glutathione reductase (GR). They generate sulfhydrylreducing systems which are coupled to antioxidant enzymes, the thioredoxin and glutathione peroxidases (TPx and GPx). The fruit fly Drosophila lacks a functional GR, suggesting that the thioredoxin system is the major source for recycling glutathione. Whole genome in silico analysis identified two nonselenium containing putative GPx genes. We examined the biochemical characteristics of one of these gene products and found that it lacks GPx activity and functions as a TPx. Transgenedependent overexpression of the newly identified Glutathione peroxidase homolog with thioredoxin peroxidase activity (Gtpx-1) gene increases resistance to experimentally induced oxidative stress, but does not compensate for the loss of catalase, an enzyme which, like GTPx-1, functions to eliminate hydrogen peroxide. The results suggest that GTPx-1 is part of the Drosophila Trx antioxidant defense system but acts in a genetically distinct pathway or in a different cellular compartment than catalase.

Authors/Editors

- Dr. Stefan Wilfried Rahlfs

Citation Styles

Harvard Citation style: Missirlis, F., Rahlfs, S., Dimopoulos, N., Bauer, H., Becker, K., Hilliker, A., et al. (2003) A putative glutathione peroxidase of Drosophila encodes a thioredoxin peroxidase that provides resistance against oxidative stress but fails to complement a lack of catalase activity, Biological Chemistry, 384(3), pp. 463-472. https://doi.org/10.1515/BC.2003.052

APA Citation style: Missirlis, F., Rahlfs, S., Dimopoulos, N., Bauer, H., Becker, K., Hilliker, A., Phillips, J., & Jäckle, H. (2003). A putative glutathione peroxidase of Drosophila encodes a thioredoxin peroxidase that provides resistance against oxidative stress but fails to complement a lack of catalase activity. Biological Chemistry. 384(3), 463-472. https://doi.org/10.1515/BC.2003.052