Reduced formation of advanced glycation endproducts via interactions between glutathione peroxidase 3 and dihydroxyacetone kinase 1
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- Title
- Reduced formation of advanced glycation endproducts via interactions between glutathione peroxidase 3 and dihydroxyacetone kinase 1
- Author(s)
- Hana Lee; Seung-Wook Chi; P Y Lee; Sunghyun Kang; S Cho; C K Lee; Kwang-Hee Bae; Byoung Chul Park; Sung Goo Park
- Bibliographic Citation
- Biochemical and Biophysical Research Communications, vol. 389, no. 1, pp. 177-180
- Publication Year
- 2009
- Abstract
- Dihydroxyacetone (DHA) induces the formation of advanced glycation endproducts (AGEs), which are involved in several diseases. Earlier, we identified dihydroxyacetone kinase 1 (Dak1) as a candidate glutathione peroxidase 3 (Gpx3)-interacting protein in Saccharomyces cerevisiae. This finding is noteworthy, as no clear evidence on the involvement of oxidative stress systems in DHA-induced AGE formation has been found to date. Here, we demonstrate that Gpx3 interacts with Dak1, alleviates DHA-mediated stress by upregulating Dak activity, and consequently suppresses AGE formation. Based on these results, we propose that defense systems against oxidative stress and DHA-induced AGE formation are related via interactions between Gpx3 and Dak1.
- Keyword
- Advanced glycation endproductDihydroxyacetoneDihydroxyacetone kinase 1Glutathione peroxidase 3Oxidative stress
- ISSN
- 0006-291X
- Publisher
- Elsevier
- DOI
- http://dx.doi.org/10.1016/j.bbrc.2009.08.116
- Type
- Article
- Appears in Collections:
- Division of Biomedical Research > 1. Journal Articles
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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