Original Article
Copyright ©2012 Baishideng Publishing Group Co., Limited. All rights reserved.
World J Gastroenterol. Dec 21, 2012; 18(47): 6935-6942
Published online Dec 21, 2012. doi: 10.3748/wjg.v18.i47.6935
Impaired suppressive activities of human MUTYH variant proteins against oxidative mutagenesis
Kazuya Shinmura, Masanori Goto, Hong Tao, Shun Matsuura, Tomonari Matsuda, Haruhiko Sugimura
Kazuya Shinmura, Masanori Goto, Hong Tao, Shun Matsuura, Haruhiko Sugimura, Department of Tumor Pathology, Hamamatsu University School of Medicine, Shizuoka 431-3192, Japan
Tomonari Matsuda, Research Center for Environmental Quality Management, Kyoto University, Shiga 520-0811, Japan
Author contributions: Shinmura K conceived the study, performed the experiments, and wrote the manuscript; Goto M, Tao H and Matsuura S performed part of the experiments; Matsuda T and Sugimura H analyzed the data; all the authors were involved in the writing of the paper and approved the final version of the manuscript.
Supported by Grants from the Ministry of Health, Labour and Welfare (21-1); the Japan Society for the Promotion of Science (22590356 and 22790378); the Hamamatsu Foundation for Science and Technology Promotion, the Ministry of Education, Culture, Sports, Science and Technology (221S0001); the Takeda Science Foundation; the Aichi Cancer Research Foundation; and the Smoking Research Foundation
Correspondence to: Kazuya Shinmura, MD, PhD, Department of Tumor Pathology, Hamamatsu University School of Medicine, 1-20-1 Handayama, Higashi Ward, Hamamatsu, Shizuoka 431-3192, Japan. kzshinmu@hama-med.ac.jp
Telephone: +81-53-4352220 Fax: +81-53-4352225
Received: June 20, 2012
Revised: September 19, 2012
Accepted: September 22, 2012
Published online: December 21, 2012
Abstract

AIM: To investigate the suppressive activity of MUTYH variant proteins against mutations caused by oxidative lesion, 8-hydroxyguanine (8OHG), in human cells.

METHODS: p.R154H, p.M255V, p.L360P, and p.P377L MUTYH variants, which were previously found in patients with colorectal polyposis and cancer, were selected for use in this study. Human H1299 cancer cell lines inducibly expressing wild-type (WT) MUTYH (type 2) or one of the 4 above-mentioned MUTYH variants were established using the piggyBac transposon vector system, enabling the genomic integration of the transposon sequence for MUTYH expression. MUTYH expression was examined after cumate induction using Western blotting analysis and immunofluorescence analysis. The intracellular localization of MUTYH variants tagged with FLAG was also immunofluorescently examined. Next, the mutation frequency in the supF of the shuttle plasmid pMY189 containing a single 8OHG residue at position 159 of the supF was compared between empty vector cells and cells expressing WT MUTYH or one of the 4 MUTYH variants using a supF forward mutation assay.

RESULTS: The successful establishment of human cell lines inducibly expressing WT MUTYH or one of the 4 MUTYH variants was concluded based on the detection of MUTYH expression in these cell lines after treatment with cumate. All of the MUTYH variants and WT MUTYH were localized in the nucleus, and nuclear localization was also observed for FLAG-tagged MUTYH. The mutation frequency of supF was 2.2 × 10-2 in the 8OHG-containing pMY189 plasmid and 2.5 × 10-4 in WT pMY189 in empty vector cells, which was an 86-fold increase with the introduction of 8OHG. The mutation frequency (4.7 × 10-3) of supF in the 8OHG-containing pMY189 plasmid in cells overexpressing WT MUTYH was significantly lower than in the empty vector cells (P < 0.01). However, the mutation frequencies of the supF in the 8OHG-containing pMY189 plasmid in cells overexpressing the p.R154H, p.M255V, p.L360P, or p.P377L MUTYH variant were 1.84 × 10-2, 1.55 × 10-2, 1.91 × 10-2, and 1.96 × 10-2, respectively, meaning that no significant difference was observed in the mutation frequency between the empty vector cells and cells overexpressing MUTYH mutants.

CONCLUSION: The suppressive activities of p.R154H, p.M255V, p.L360P, and p.P377L MUTYH variants against mutations caused by 8OHG are thought to be severely impaired in human cells.

Keywords: 8-hydroxyguanine; Mutation; MUTYH; MUTYH-associated polyposis; Oxidative mutagenesis; supF forward mutation assay; piggyBac transposon; Colorectal polyposis