Comparison of dihydropyrimidine dehydrogenase from human, rat, pig and cow liver: Biochemical and immunological properties
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Phenotypic and clinical implications of variants in the dihydropyrimidine dehydrogenase gene
2016, Biochimica et Biophysica Acta - Molecular Basis of DiseaseCitation Excerpt :A conceivable explanation for the latter observation is the fact that the uracil plasma concentration was on average 4.5 times higher than that of thymine. The fact that the plasma concentrations of uracil and thymine are 27 and 120-fold, respectively, lower than the Km values of DPD for uracil and thymine [56], indicates that under normal physiological conditions, the DPD enzyme is non-saturated and follows first-order kinetics. This phenomenon has been suggested to underlie the large variation in the U/UH2 ratio and indicates that the rate of uracil metabolism is largely depended on the uracil concentration and not primarily on the amount of active DPD enzyme [32].
Lack of carcinogenicity and increased survival in F344 rats treated with 5-fluorouracil for two years
2000, Food and Chemical ToxicologyCitation Excerpt :In the present study, many of the animals with such neoplasms in the control and 62 ppm-treated groups were dead or had been killed in extremis before the end of the experiment at wk 111 when the haematological examination was carried out, but sufficient numbers remained in the 125 ppm-treated group to have contributed to the increase in the mean number of peripheral WBC observed for this group. Dihydropyrimidine dehydrogenase (DPD), the initial, rate-limiting enzyme in 5-FU catabolism, catalysing the reduction of 5-FU to 5,6-dihydro-5-fluorouracil, exists in many species including man and the rat (Lu et al., 1993). DPD plays an important role in regulating the availability of 5-FU for anabolism, thereby affecting its pharmacokinetics, toxicity and efficacy.
Dose-dependency in local disposition of 5-fluorouracil under non-steady- state condition in rat liver
2000, Journal of Pharmaceutical Sciences