Related Experiment Video
Updated: Aug 9, 2026
09:46
Megakaryocyte Differentiation and Platelet Formation from Human Cord Blood-derived CD34+ Cells
Published on: December 27, 2017
Thymidine phosphorylase activity associated with platelet-derived endothelial cell growth factor
T Sumizawa1, T Furukawa, M Haraguchi
1Department of Cancer Chemotherapy, Institute of Cancer Research, Faculty of Medicine, Kagoshima University.
Journal of Biochemistry
|July 1, 1993
Summary
Human thymidine phosphorylase (dThdPase) is identical to platelet-derived endothelial cell growth factor (PD-ECGF). This finding was confirmed through molecular cloning, sequence identity, and enzymatic activity assays.
Area of Science:
- Biochemistry
- Molecular Biology
- Enzymology
Background:
- Thymidine phosphorylase (dThdPase) is an enzyme involved in nucleotide metabolism.
- Platelet-derived endothelial cell growth factor (PD-ECGF) is a growth factor with roles in angiogenesis.
Purpose of the Study:
- To investigate the molecular identity between human thymidine phosphorylase (dThdPase) and platelet-derived endothelial cell growth factor (PD-ECGF).
Main Methods:
- Polymerase chain reaction (PCR) for cDNA cloning.
- Amino acid sequencing and peptide fragment analysis.
- Western blotting using specific antibodies.
- Enzymatic activity assays.
- Expression studies in transfected COS cells.
Main Results:
- Complete sequence identity was found between the deduced amino acid sequence of dThdPase cDNA and PD-ECGF.
- All four peptide fragments of human dThdPase aligned with PD-ECGF residues 125-244.
- Antibodies against PD-ECGF recognized dThdPase, and vice versa.
- Recombinant PD-ECGF exhibited dThdPase activity.
- dThdPase activity and molecules were detected in cells transfected with PD-ECGF cDNA.
Conclusions:
- Human thymidine phosphorylase (dThdPase) is identical to platelet-derived endothelial cell growth factor (PD-ECGF).
- PD-ECGF possesses dThdPase enzymatic activity.
