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ID 115054
著者
Tabata, Sho Keio University
Yamamoto, Masatatsu Kagoshima University
Hirayama, Akiyoshi Keio University
Ohishi, Maki Keio University
Kuramoto, Takuya Tokushima University
Ikeda, Ryuji Kagoshima University
Haraguchi, Misako Kagoshima University
Kawahara, Kohichi Kagoshima University
Shinsato, Yoshinari Kagoshima University
Minami, Kentaro Kagoshima University
Esumi, Hiroyasu Tokyo University of Science
Tomita, Masaru Keio University
Soga, Tomoyoshi Keio University
Furukawa, Tatsuhiko Kagoshima University
秋山, 伸一 National Kyushu Cancer Center
資料タイプ
学術雑誌論文
抄録
Thymidine phosphorylase (TP), a rate-limiting enzyme in thymidine catabolism, plays a pivotal role in tumor progression; however, the mechanisms underlying this role are not fully understood. Here, we found that TP-mediated thymidine catabolism could supply the carbon source in the glycolytic pathway and thus contribute to cell survival under conditions of nutrient deprivation. In TP-expressing cells, thymidine was converted to metabolites, including glucose 6-phosphate, lactate, 5-phospho-α-D-ribose 1-diphosphate, and serine, via the glycolytic pathway both in vitro and in vivo. These thymidine-derived metabolites were required for the survival of cells under low-glucose conditions. Furthermore, activation of thymidine catabolism was observed in human gastric cancer. These findings demonstrate that thymidine can serve as a glycolytic pathway substrate in human cancer cells.
掲載誌名
Cell Reports
ISSN
22111247
出版者
Elsevier
19
7
開始ページ
1313
終了ページ
1321
発行日
2017-05-16
権利情報
This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
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出版社版URL
フルテキストファイル
言語
eng
著者版フラグ
出版社版
部局
医学系