Identification of glutathione sulfotransferase-pi (GSTP1) as a new resveratrol targeting protein (RTP) and studies of resveratrol-responsive protein changes by resveratrol affinity chromatography.

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). 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. Glutathione sulfotransferase-pi (GSTP1) and estrogen receptor-beta (ER-beta) 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. Resveratrol affects cellular functions at multiple levels, ranging from interaction with detoxification enzymes, such as GSTP1 and transcription by targeting factors such as ER-beta.