Thymidylate synthase and dihydropyrimidine dehydrogenase
are related to histological effects of 5-fluorouracil and cisplatin neoadjuvant chemotherapy for primary gastric cancer patients.
Importance of dihydropyrimidine dehydrogenase
(DPD) deficiency in patients exhibiting toxicity following treatment with 5-fluorouracil.
Population study of dihydropyrimidine dehydrogenase
in cancer patients.
Patients with a dihydropyrimidine dehydrogenase
deficiency had concentrations of the pyrimidine de novo metabolites that were within reference values.
pharmacogenetics in Caucasian subjects.
Eniluracil, an oral dihydropyrimidine dehydrogenase
(DPD) inhibitor, is being developed to improve the tolerability and effectiveness of 5-fluorouracil (5-FU), one of the most widely used oncology drugs in the world.
(DPYD) is the initial and rate-limiting enzyme in the metabolism of the chemotherapeutic drug 5-fluorouracil (5-FU), thus affecting its pharmacokinetics, efficacy, and toxicity (1).
Catabolism of the pyrimidine bases thymine and uracil consists of three consecutive steps: (a) thymine and uracil are catabolized by dihydropyrimidine dehydrogenase
(DPD; EC 1.
Quantitation of dihydropyrimidine dehydrogenase
expression by real-time reverse transcription polymerase chain reaction.
The human dihydropyrimidine dehydrogenase
gene (DPYD) encodes dihydropyrimidine dehydrogenase
(DPD; EC 1.
Correlation between dihydropyrimidine dehydrogenase
activity in peripheral mononuclear cells and systemic clearance of fluorouracil in cancer patients.
Therefore, eniluracil not only irreversibly inhibits the enzyme dihydropyrimidine dehydrogenase
(DPD) which breaks down 5-fluorouracil (5-FU), it can also reversibly inhibit the activation of 5-FU, thereby limiting the effectiveness of 5-FU as an anti-cancer agent when not dosed properly.