Identification of Glutathione Sulfotransferase-π (GSTP1) as a New Resveratrol Targeting Protein (RTP) and Studies of Resveratrol-responsive Protein Changes by Resveratrol Affinity Chromatography

Abstract

Background: Resveratrol shows chemopreventive and other biological affects in in vitro and some animal studies. The bioactivities of resveratrol may be attributed to qualitative and quantitative differences in its cell-type-specific interaction and binding with its cellular targets, denoted as resveratrol targeting proteins (RTPs). Materials and Methods: To isolate RTPs, resveratrol was linked to epoxy-activated agarose generating an affinity platform to allow the isolation, purification, and characterization of distinct RTPs from cultured prostate cancer cell extracts. Results: Glutathione sulfotransferase-π (GSTP1) and estrogen receptor-β, (ER-β) were found to be new RTPs. Resveratrol affinity chromatography was shown to be an easy method for analyzing resveratrol-responsive protein changes in the androgen-dependent LNCaP cells. Conclusion: Resveratrol affects cellular functions at multiple levels, ranging from interaction with detoxification enzymes, such as GSTP1 and transcription by targeting factors such as ER-β.