Thymidine catabolism as a metabolic strategy for cancer survival
Open accessAbstract
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.
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Nucleotide salvage pathways can support tumor cell proliferation in certain contexts.
“Though nucleotide salvage pathways can support tumor cell proliferation in certain contexts (Tabata et al., 2017), concentrations of circulating nucleotides are likely too low for many tumors to satisfy their nucleotides demand via salvage alone (Traut, 1994).”
From Targeting Metabolism for Cancer Therapy (2017) · cites this paper as Tabata et al., 2017
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References 38 · Cited by 68
Research works printed but not linked: 2
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- Shimaoka, S., Matsushita, S., Nitanda, T., Matsuda, A., Nioh, T., Suenaga, T., Nishimata, Y., Akiba, S., Akiyama, S., and Nishimata, H. (2000). The role of thymidine phosphorylase expression in the invasiveness of gastric carcinoma. Cancer 88 , 2220-2227. http://refhub.elsevier.com/S2211-1247(1730572-7/sref29)
- Authors
- Tabata, S., Yamamoto, M., Goto, H., Hirayama, A., Ohishi, M., Kuramoto, T., Mitsuhashi, A., Ikeda, R., Haraguchi, M., Kawahara, K., Shinsato, Y., Minami, K., Saijo, A., Hanibuchi, M., Nishioka, Y., Sone, S., Esumi, H., Tomita, M., Soga, T., Furukawa, T., & Akiyama, S.-I.
- Affiliations
- Institute for Advanced Biosciences, Keio University (JP)
- Kagoshima University (JP)
- Tokushima University (JP)
- Tokyo University of Science (JP)
- National Hospital Organization Kyushu Cancer Center (JP)
- Corresponding author
- Tabata, Sho
- Furukawa, Tatsuhiko
- Akiyama, Shin-ichi
- ORCID
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2017-05
- Volume
- 19
- Issue
- 7
- Pages
- 1313-1321
- ISSN
- 2211-1247 (ISSN-L)
- OpenAlex
- W2615157652
- Cited by
- 68
- References
- 38
- Citations by year
- 2026: 7 · 2025: 10 · 2024: 8 · 2023: 9 · 2022: 7 · 2021: 6 · 2020: 5 · 2019: 9 · 2018: 3 · 2017: 4
- FWCI
- 1.93
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Cell Reports (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Institutional Repositories DataBase (IRDB) (submittedVersion, cc-by-nc-nd)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Japan Society for the Promotion of Science KAKENHI (JP15K10338, JP26870456, JP16K07121, JP22501048, JP26870576, JP16K21361)
- Research Support Foundation of The University of Tokushima and TAIHO Pharmaceutical Co., Ltd.
- Yamagata Prefecture Government
- Tsuruoka City
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- thymidine phosphorylase, glycolysis, glucose-6-phosphate, lactate, serine, nutrient deprivation, low glucose, tumor cell survival, gastric cancer, cancer metabolism
- MeSH terms
- Animals, Carbon, Deoxyribose, Glycolysis, Humans, Nutritional Status, Phosphorylation, Stomach Neoplasms, Thymidine, Thymidine Phosphorylase, Survival Analysis, Cell Line, Tumor, Cell Proliferation, Mice, Human Umbilical Vein Endothelial Cells
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