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The expression of GST isoenzymes in acinar adenocarcinoma, intraepithelial neoplasia, and benign prostate tissue: correlation of clinical parameters with GST isoenzymes

This study investigated the immunohistochemical staining characteristics of glutathione-S-transferase (GST) alpha, pi, mu, and theta in prostatic acinar adenocarcinoma (PCA), prostatic intraepithelial neoplasia (PIN), and benign prostatic tissues from 19 patients. | Turk J Biol 36 (2012) 687-693 © TÜBİTAK doi:10.3906/biy-1203-31 The expression of GST isoenzymes in acinar adenocarcinoma, intraepithelial neoplasia, and benign prostate tissue: correlation of clinical parameters with GST isoenzymes 1 Gülçin ŞİMŞEK1, Serpil OĞUZTÜZÜN2, Servet GÜREŞCİ1, Murat KILIÇ3, Ömer Faruk BOZKURT4, Ali ÜNSAL4 Department of Pathology, Keçiören Research and Training Hospital, Ankara − TURKEY 2 Department of Biology, Kırıkkale University, 71451 Yahşihan, Kırıkkale − TURKEY 3 4 The Vocational School of Acıpayam, Pamukkale University, Denizli − TURKEY Department of Urology, Keçiören Research and Training Hospital, Ankara − TURKEY Received: 15.03.2012 ● Accepted: 02.07.2012 Abstract: This study investigated the immunohistochemical staining characteristics of glutathione-S-transferase (GST) alpha, pi, mu, and theta in prostatic acinar adenocarcinoma (PCA), prostatic intraepithelial neoplasia (PIN), and benign prostatic tissues from 19 patients. Relationships between GST isoenzyme expression in benign, PIN, and PCA tissue were examined by the Wilcoxon signed-rank test and clinicopathological data were examined by the Spearman correlation rank test. When the benign, PIN, and PCA tissues from these cases were compared according to their staining intensity, GST alpha, pi, mu, and theta expressions in tumor cells were significantly lower than in benign epithelial cells (P 0.05). Key words: Prostate acinar adenocarcinoma, prostatic intraepithelial neoplasia, glutathione-S-transferase, immunohistochemistry Introduction Glutathione-S-transferases (GSTs) are a family of enzymes that detoxify intracellular xenobiotics, primarily by catalysis of the nucleophilic attack of reduced glutathione on electrophilic compounds (1,2). Since conjugation to glutathione renders these potential carcinogens chemically inactive and hence incapable of forming DNA adducts, it has been hypothesized that GSTs protect against neoplastic transformation (3). In humans, .