OGG1 Does not Interact with NKX3.1 and AR to Repair 8-OHdG Base Damage in LNCaP Cells

Abstract

OGG1 (8-oxo-G DNA glycosylase 1) is a BER (base excision repair) enzyme responsible for the repair of 8-oxo-G base damage related to oxidative stress through glycosylation. Determination of the interaction of DNA repair enzymes with other proteins that contributes to repairing base damages in the cell, is highly relevant in cancer treatment strategies and therapeutic targeting studies. In a previous study, it is shown that OGG1 associated with the homeobox protein NKX3.1 and androgen receptor (AR) in the 8-OHdG-repair complex in prostate cell line LNCaP, when treated with etoposide. Additionally, it is still uncertain that whether S326C, a polymorphic variant of OGG1 formed by a single amino acid change, might harbor functional loss, which might cause a deficiency in repair activity augmenting the susceptibility to (PCa). Therefore, in our study, we investigated the interaction of OGG1 and its polymorphic variant S326C with prostate specific proteins in LNCaP cells under oxidative conditions. Thus, we confirmed the previously determined interactions, however oxidative induction via menadione treatment impairs these interactions.

Keywords

• OGG1
• S326C
• NKX3.1
• AR
• prostate cancer