Definition
TP is a nucleoside metabolism enzyme involved in the maintenance of healthy mitochondria and balanced nucleoside triphosphate pool for DNA replication and repair. TP provides multiple cellular biological functions such as stimulation of angiogenesis and antiapoptosis.
Characteristics
TP was purified in the mid-1970s from both Escherichia coli and Salmonella as a nucleoside metabolism enzyme; it is a homodimer of 45 kDa subunits. In the middle of the 1980s, a molecule exhibited angiogenic activity was extracted from human platelets and named PD-ECGF. Subsequently, it was discovered that 2-deoxy-d-ribose (2-DDR), a thymidine metabolite, stimulates chemotaxis of the endothelium and angiogenesis, and then it was clarified that PD-ECGF had TP activity and these two molecules were the same. Somatic mitochondrial DNA point mutations with TP deficiencies result in mitochondrial neurogastrointestinal...
References
Hotchkiss KA, Ashton AW, Schwartz EL (2003) Thymidine phosphorylase and 2-deoxyribose stimulate human endothelial cell migration by specific activation of the integrins αβ and αβ. J Biol Chem 278:19272–19279
Ikeda R, Che XF, Ushiyama M et al (2006) 2-Deoxy-d-ribose inhibits hypoxia-induced apoptosis by suppressing the phosphorylation of p38 MAPK. Biochem Biophys Res Commun 342:280–285
Leek RD, Talks KL, Pezzella F et al (2000) Thymidine phosphorylase induces carcinoma cell oxidative stress and promotes secretion of angiogenic factors. Cancer Res 60:6298–6302
Seeliger H, Guba M, Koehl GE et al (2004) Blockage of 2-deoxy-d-ribose-induced angiogenesis with rapamycin counteracts a thymidine phosphorylase-based escape mechanism available for colon cancer under 5-fluorouracil therapy. Clin Cancer Res 10:1843–1852
Toi M, Rahman MA, Bando H et al (2005) Role of thymidine phosphorylase/PD-ECGF in cancer biology and treatment. Lancet Oncol 6:158–166
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Toi, M. (2014). Thymidine Phosphorylase. In: Schwab, M. (eds) Encyclopedia of Cancer. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-27841-9_5800-2
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DOI: https://doi.org/10.1007/978-3-642-27841-9_5800-2
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Publisher Name: Springer, Berlin, Heidelberg
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