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Thymidine phosphorylase, 2-deoxy-D-ribose and angiogenesis
1Molecular Angiogenesis Laboratory, Imperial Cancer Research Fund, Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Oxford OX3 9DS, U.K.
The Biochemical Journal
|August 7, 1998
Summary
Thymidine phosphorylase (TP) produces 2-deoxy-D-ribose, an angiogenesis-inducing factor that attracts new blood vessels. This discovery expands TP
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Angiogenesis, the formation of new blood vessels, is crucial for tissue development and repair.
- Endothelial-cell chemoattractants guide the formation of new vasculature.
- Thymidine phosphorylase (TP) is an enzyme traditionally linked to nucleotide salvage pathways.
Purpose of the Study:
- To investigate the novel role of thymidine phosphorylase (TP) as an angiogenic factor.
- To identify 2-deoxy-D-ribose, a product of TP, as an endothelial-cell chemoattractant.
- To explore the mechanism of action for 2-deoxy-D-ribose in stimulating angiogenesis.
Main Methods:
- Enzyme assays to measure TP activity.
- In vivo studies to assess the angiogenic potential of 2-deoxy-D-ribose.
- Cell migration assays using endothelial cells.
- Comparison of 2-deoxy-D-ribose with other chemoattractants like glucose.
Main Results:
- TP catalyzes the production of 2-deoxy-D-ribose from thymidine.
- 2-Deoxy-D-ribose functions as an endothelial-cell chemoattractant and induces angiogenesis.
- TP expression is elevated in tumors and inflamed tissues, correlating with active angiogenesis.
- Unlike typical chemoattractants, 2-deoxy-D-ribose may not require a cell-surface receptor.
Conclusions:
- Thymidine phosphorylase (TP) is a novel angiogenic factor.
- 2-Deoxy-D-ribose is a key mediator of TP-induced angiogenesis.
- The findings suggest potential therapeutic targets for diseases involving abnormal angiogenesis.