Development and Characterization of 1C6-203, a New Monoclonal Antibody Specific to Human Thymidine PhosphorylaseToru Konoa, Miwa Nishidab, Naohito Inagakib, Yutaka Tanakab, Masashi Yonedaa, and Shinichi Kasaiaa Second Department of Surgery and Medicine, Kamakura, Kanagawa, Japan b Asahikawa Medical College, Asahikawa, Hokkaido, Japan, and Cytostatics Group, Nippon Roche Research Center, Kamakura, Kanagawa, Japan Correspondence to: Toru Kono, Second Dept. of Surgery, Asahikawa Medical College, 2-1 Midorigaoka-Higashi, Asahikawa, Hokkaido 078-8510, Japan. E-mail: kono@asahikawa-med.ac.jp Thymidine phosphorylase (dThdPase) is an essential enzyme for activation of the oral cytostatic drug capecitabine and its intermediate metabolite, doxifluridine, to 5-fluorouracil in tumors. Methods to estimate dThdPase expression in tumor tissue might be useful to predict the efficacy of capecitabine and doxifluridine in cancer patients. We established a new monoclonal antibody (MAb), 1C6-203, applicable for dThdPase immunohistochemistry and compared its staining characteristics with those of a previously established MAb, 654-1. In 4% paraformaldehyde-fixed colorectal carcinoma, 1C6-203 and 654-1 stained cancer cells in 19/30 and 9/30 patients, respectively. In 10% formalin-fixed colorectal carcinoma, 1C6-203 and 654-1 stained cancer cells in 18/30 and 6/30 patients, respectively. In negative 10% formalin-fixed tissues, microwave treatment improved the positivity of 654-1-stained cancer cells. These results suggest that an epitope recognized by 1C6-203 is resistant to epitope masking by formaldehyde fixation, whereas that for MAb 654-1 is sensitive. Therefore, MAb 1C6-203 might be more suitable than MAb 654-1 for evaluating dThdPase expression in colorectal carcinoma. (J Histochem Cytochem 49:131137, 2001) Key Words: thymidine phosphorylase, monoclonal antibody, Western blotting, immunohistochemistry, human, colorectal cancer, cancer cell, stromal cell
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