Thymidine phosphorylase in cancer; Enemy or friend?

Elamin, Yasir Y., Rafee, Shereen, Osman, Nemer, O'Byrne, Kenneth J., & Gately, Kathy (2016) Thymidine phosphorylase in cancer; Enemy or friend? Cancer Microenvironment, 9(1), pp. 33-43.

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Abstract

Thymidine phosphorylase (TP) is a nucleoside metabolism enzyme that plays an important role in the pyrimidine pathway.TP catalyzes the conversion of thymidine to thymine and 2-deoxy-α-D-ribose-1-phosphate (dRib-1-P). Although this reaction is reversible, the main metabolic function of TP is catabolic. TP is identical to the angiogenic factor platelet-derived endothelial-cell growth factor (PD-ECGF). TP is overexpressed in several human cancers in response to cellular stressful conditions like hypoxia, acidosis, chemotherapy and radiotherapy. TP has been shown to promote tumor angiogenesis, invasion, metastasis, evasion of the immune-response and resistance to apoptosis. Some of the biological effects of TP are dependent on its enzymatic activity, while others are mediated through cytokines like interleukin 10 (IL-10), basic fibroblast growth factor (bFGF) and tumour necrosis factor α (TNFα). Interestingly, TP also plays a role in cancer treatment through its role in the conversion of the oral fluoropyrimidine capecitabine into its active form 5-FU. TP is a predictive marker for fluoropyrimidine response. Given its various biological functions in cancer progression, TP is a promising target in cancer treatment. Further translational research is required in this area.

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ID Code: 95329
Item Type: Journal Article
Refereed: Yes
Keywords: Thymidine phosphorylase, Hallmarks of cancer, Angiogenesis, Predictive biomarkers
DOI: 10.1007/s12307-015-0173-y
ISSN: 1875-2284
Divisions: Current > Schools > School of Biomedical Sciences
Current > QUT Faculties and Divisions > Faculty of Health
Current > Institutes > Institute of Health and Biomedical Innovation
Copyright Owner: Copyright 2015 Springer Science+Business Media Dordrecht
Copyright Statement: The final publication is available at Springer via http://dx.doi.org/10.1007/s12307-015-0173-y
Deposited On: 02 May 2016 23:03
Last Modified: 08 May 2016 05:26

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