These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Butin decreases oxidative stress-induced 8-hydroxy-2'-deoxyguanosine levels via activation of oxoguanine glycosylase 1.
    Author: Kang KA, Lee JH, Chae S, Zhang R, Piao MJ, Kim HS, You HJ, Hyun JW.
    Journal: Chem Biol Interact; 2009 Oct 30; 181(3):338-42. PubMed ID: 19631197.
    Abstract:
    In response to oxidative DNA base damage, oxoguanine glycosylase 1 (OGG1), in a base-excision repair (BER) pathway in mammals, plays a vital role in the repair of 8-hydroxy-2'-deoxyguanosine (8-OHdG), which is a reliable marker of reactive oxygen species (ROS)-induced DNA base modification and contributes to the pathologic process of cancer. Recently, we have shown that butin (7,3',4'-trihydroxydihydroflavone) protects cells against hydrogen peroxide (H2O2)-induced damage of cellular components including DNA. In the present study, we examined the possible protective effect of butin on oxidative stress-induced DNA base modification, especially 8-OHdG. Hydrogen peroxide significantly increased the level of 8-OHdG, which was detected by 8-OHdG ELISA and confocal microscopy, but butin decreased this level. Suppression of 8-OHdG formation by butin was related to the enhanced mRNA and protein expression of OGG1, which was detected by RT-PCR and Western blot analysis. Butin also increased the transcriptional activity of OGG1, which was suppressed by H2O2 treatment; this transcriptional activity was detected by OGG1 promoter luciferase assay. Butin enhanced the expression of phosphorylated Akt (active form of Akt), a regulator of OGG1, which was decreased by H2O2 treatment. A PI3K-specific inhibitor, LY294002, abolished the phosphorylated Akt and OGG1 expressions induced by butin, suggesting that OGG1 induction by butin involves the PI3K/Akt pathway.
    [Abstract] [Full Text] [Related] [New Search]