Reduced formation of advanced glycation endproducts via interactions between glutathione peroxidase 3 and dihydroxyacetone kinase 1

• Published in: Biochemical and biophysical research communications Vol. 389; no. 1; pp. 177 - 180
• Main Authors: Lee, Hana, Chi, Seung Wook, Lee, Phil Young, Kang, Sunghyun, Cho, Sayeon, Lee, Chong-Kil, Bae, Kwang-Hee, Park, Byoung Chul, Park, Sung Goo
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 06.11.2009
• Subjects: Advanced glycation endproduct; Dihydroxyacetone; Dihydroxyacetone - metabolism; Dihydroxyacetone kinase 1; Gene Deletion; Glutathione Peroxidase - genetics; Glutathione Peroxidase - metabolism; Glutathione peroxidase 3; Glycation End Products, Advanced - biosynthesis; Glycation End Products, Advanced - genetics; Oxidative Stress; Phosphotransferases (Alcohol Group Acceptor) - metabolism; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae - growth & development; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae Proteins - genetics; Saccharomyces cerevisiae Proteins - metabolism; Glutathione peroxidase 3; Oxidative stress; Dihydroxyacetone kinase 1; Dihydroxyacetone; Advanced glycation endproduct
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2009.08.116

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.