number of access : ?
number of downloads : ?
ID 115054
Author
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
Akiyama, Shin-ichi National Kyushu Cancer Center
Content Type
Journal Article
Description
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.
Journal Title
Cell Reports
ISSN
22111247
Publisher
Elsevier
Volume
19
Issue
7
Start Page
1313
End Page
1321
Published Date
2017-05-16
Rights
This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
EDB ID
DOI (Published Version)
URL ( Publisher's Version )
FullText File
language
eng
TextVersion
Publisher
departments
Medical Sciences