Abstract
Quinonoid dihydropteridine reductase (QDPR) catalyzes the regeneration of tetrahydrobiopterin (BH4), a cofactor for monoamine synthesis, phenylalanine hydroxylation and nitric oxide production. Here, we produced and analyzed a transgenic Qdpr-/- mouse model. Unexpectedly, the BH4 contents in the Qdpr-/- mice were not decreased and even increased in some tissues, whereas those of the oxidized form dihydrobiopterin (BH2) were significantly increased. We demonstrated that unlike the wild-type mice, dihydrofolate reductase regenerated BH4 from BH2 in the mutants. Furthermore, we revealed wide alterations in folate-associated metabolism in the Qdpr-/- mice, which suggests an interconnection between folate and biopterin metabolism in the transgenic mouse model.
Original language | English |
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Pages (from-to) | 3924-3931 |
Number of pages | 8 |
Journal | FEBS Letters |
Volume | 588 |
Issue number | 21 |
DOIs | |
Publication status | Published - 03-11-2014 |
All Science Journal Classification (ASJC) codes
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology