Disparities of conjugating protective enzyme activities in the colon of patients with adenomas and carcinomas

To investigate the metabolic enzymatic capacity of the colon mucosa to detoxify noxious carcinogenic compounds. We investigated the activity of 2 conjugating enzymes-the microsomal uridine glucuronosyltransferase (UGT) and the cytosomal glutathione S-transferase (GST) in the uninvolved mucosa of the...

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Published in:World journal of gastroenterology : WJG Vol. 19; no. 36; pp. 6020 - 6025
Main Authors: Hoensch, Harald P, Roelofs, Hennie M J, Edler, Lutz, Kirch, Wilhelm, Peters, Wilbert H M
Format: Journal Article
Language:English
Published: United States Baishideng Publishing Group Co., Limited 28-09-2013
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Summary:To investigate the metabolic enzymatic capacity of the colon mucosa to detoxify noxious carcinogenic compounds. We investigated the activity of 2 conjugating enzymes-the microsomal uridine glucuronosyltransferase (UGT) and the cytosomal glutathione S-transferase (GST) in the uninvolved mucosa of the colon transversum and sigmoideum in patients with adenomatous polyps and colorectal cancer. Biopsies were taken from the mucosa during colonoscopies which were done for clinical (diagnostic) reasons. After storage, the biopsy material was homogenized and after differential centrifugation the enzyme assays were performed with 4-nitrophenol (UGT) and 1-chloro 2,4-dinitrobenzene (GST) as substrates. About 48 patients were included of which 28 had adenomas and 20 had colorectal carcinomas confirmed by histopathology. Enzyme activities were expressed as nmol/mg per minute protein for the GST and as pmol/mg per minute protein for the UGT. Analysis of variance (F-test) indicated that both enzymes were more widely distributed in adenoma than in cancer patients. The means ± SD were smaller for cancer patients: GST for adenomas 268 ± 152 vs 241 ± 69 for carcinomas and UGT for adenomas 197 ± 200 vs 150 ± 86 for carcinomas. Compared to patients with adenomatous colon polyps those with colorectal carcinoma exhibited a lower capacity of detoxifying enzyme metabolism and their activities clustered over a smaller range.
Bibliography:Author contributions: Hoensch HP is responsible for the study design, analysis and writing of the manuscript; Peters WHM and Roelofs HMJ performed the enzyme assays; Edler L analysed the data; Kirch W acts as guarantor for this article.
Correspondence to: Harald P Hoensch, Professor, Internal Medicine, Marien Hospital, Martinspfad 72, Darmstadt D-64285, Germany. h.p.hoensch@t-online.de
Telephone: +49-6152-56768 Fax: +49-6152-56742
ISSN:1007-9327
2219-2840
DOI:10.3748/wjg.v19.i36.6020