메뉴 건너뛰기




Volumn 92, Issue 4, 2007, Pages 308-314

Effects of tetrahydrobiopterin and phenylalanine on in vivo human phenylalanine hydroxylase by phenylalanine breath test

Author keywords

Biopterin; Breath test; Hyperphenylalaninemia; Phenylalanine hydroxylase; Phenylketonuria; Stable isotope

Indexed keywords

CARBON 13; CARBON DIOXIDE; ENZYME ACTIVATOR; PHENYLALANINE; PHENYLALANINE 4 MONOOXYGENASE; TETRAHYDROBIOPTERIN;

EID: 36148951051     PISSN: 10967192     EISSN: 10967206     Source Type: Journal    
DOI: 10.1016/j.ymgme.2007.07.013     Document Type: Article
Times cited : (4)

References (40)
  • 1
    • 0000134296 scopus 로고    scopus 로고
    • Hyperphenylalaninemia: phenylalanine hydroxylase deficiency
    • Scriver C.R., Baudet A.L., Valle D., and Sly W.S. (Eds), McGraw-Hill, New York
    • Scriver C.R., and Kaufman S. Hyperphenylalaninemia: phenylalanine hydroxylase deficiency. In: Scriver C.R., Baudet A.L., Valle D., and Sly W.S. (Eds). The Metabolic and Molecular Bases of Inherited Disease. eighth ed. vol. II (2001), McGraw-Hill, New York 1667-1724
    • (2001) The Metabolic and Molecular Bases of Inherited Disease. eighth ed. , vol.II , pp. 1667-1724
    • Scriver, C.R.1    Kaufman, S.2
  • 3
    • 0002595234 scopus 로고    scopus 로고
    • A patient with phenylketonuria successfully treated with tetrahydrobiopterin
    • Nuoffer J.M., Thöny B., Romstad A., and Blau N. A patient with phenylketonuria successfully treated with tetrahydrobiopterin. J. Inherit. Metab. Dis. 24 Suppl 1 (2001) 29
    • (2001) J. Inherit. Metab. Dis. , vol.24 , Issue.SUPPL. 1 , pp. 29
    • Nuoffer, J.M.1    Thöny, B.2    Romstad, A.3    Blau, N.4
  • 5
    • 0035048113 scopus 로고    scopus 로고
    • Successful treatment of phenylketonuria with tetrahydrobiopterin
    • Trefz F.K., Aulela-Scholz C., and Blau N. Successful treatment of phenylketonuria with tetrahydrobiopterin. Eur. J. Pediatr. 160 (2001) 315
    • (2001) Eur. J. Pediatr. , vol.160 , pp. 315
    • Trefz, F.K.1    Aulela-Scholz, C.2    Blau, N.3
  • 6
    • 0036351315 scopus 로고    scopus 로고
    • Tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency: possible regulation of gene expression in a patient with the homozygous L48S mutation
    • Blau N., and Trefz F.K. Tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency: possible regulation of gene expression in a patient with the homozygous L48S mutation. Mol. Genet. Metab. 75 (2002) 186-187
    • (2002) Mol. Genet. Metab. , vol.75 , pp. 186-187
    • Blau, N.1    Trefz, F.K.2
  • 9
    • 0034744074 scopus 로고    scopus 로고
    • 4 responsiveness in patients with mild forms of hyperphenylalaninaemia and phenylketonuria
    • 4 responsiveness in patients with mild forms of hyperphenylalaninaemia and phenylketonuria. J. Inherit. Metab. Dis. 24 (2001) 213-230
    • (2001) J. Inherit. Metab. Dis. , vol.24 , pp. 213-230
    • Erlandsen, H.1    Stevens, R.C.2
  • 10
    • 2542429299 scopus 로고    scopus 로고
    • The metabolic and molecular bases of tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency
    • Blau N., and Erlandsen H. The metabolic and molecular bases of tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency. Mol. Genet. Metab. 82 (2004) 101-111
    • (2004) Mol. Genet. Metab. , vol.82 , pp. 101-111
    • Blau, N.1    Erlandsen, H.2
  • 11
    • 4744342508 scopus 로고    scopus 로고
    • Wild-type phenylalanine hydroxylase activity is enhanced by tetrahydrobiopterin supplementation in vivo: an implication for therapeutic basis of tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency
    • Kure S., Sato K., Fujii K., Aoki Y., Suzuki Y., Kato S., and Matsubara Y. Wild-type phenylalanine hydroxylase activity is enhanced by tetrahydrobiopterin supplementation in vivo: an implication for therapeutic basis of tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency. Mol. Genet. Metab. 83 (2004) 150-156
    • (2004) Mol. Genet. Metab. , vol.83 , pp. 150-156
    • Kure, S.1    Sato, K.2    Fujii, K.3    Aoki, Y.4    Suzuki, Y.5    Kato, S.6    Matsubara, Y.7
  • 13
    • 28844451504 scopus 로고    scopus 로고
    • The activity of wild-type and mutant phenylalanine hydroxylase and its regulation by phenylalanine and tetrahydrobiopterin at physiological and pathological concentrations: an isothermal titration calorimetry study
    • Pey A.L., and Martinez A. The activity of wild-type and mutant phenylalanine hydroxylase and its regulation by phenylalanine and tetrahydrobiopterin at physiological and pathological concentrations: an isothermal titration calorimetry study. Mol. Genet. Metab. 86 Suppl 1 (2005) S43-S53
    • (2005) Mol. Genet. Metab. , vol.86 , Issue.SUPPL. 1
    • Pey, A.L.1    Martinez, A.2
  • 14
    • 8844256618 scopus 로고    scopus 로고
    • Tetrahydrobiopterin protects phenylalanine hydroxylase activity in vivo: implications for tetrahydrobiopterin-responsive hyperphenylalaninemia
    • Thöny B., Ding Z., and Martinez A. Tetrahydrobiopterin protects phenylalanine hydroxylase activity in vivo: implications for tetrahydrobiopterin-responsive hyperphenylalaninemia. FEBS Lett. 577 (2004) 507-511
    • (2004) FEBS Lett. , vol.577 , pp. 507-511
    • Thöny, B.1    Ding, Z.2    Martinez, A.3
  • 16
    • 6344293954 scopus 로고    scopus 로고
    • In vivo studies of phenylalanine hydroxylase by phenylalanine breath test: diagnosis of tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency
    • Okano Y., Hase Y., Kawajiri M., Nishi Y., Inui K., Sakai N., Tanaka Y., Takatori K., Kajiwara M., and Yamano T. In vivo studies of phenylalanine hydroxylase by phenylalanine breath test: diagnosis of tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency. Pediatr. Res. 56 (2004) 714-719
    • (2004) Pediatr. Res. , vol.56 , pp. 714-719
    • Okano, Y.1    Hase, Y.2    Kawajiri, M.3    Nishi, Y.4    Inui, K.5    Sakai, N.6    Tanaka, Y.7    Takatori, K.8    Kajiwara, M.9    Yamano, T.10
  • 17
    • 0028265336 scopus 로고
    • Molecular characterization of phenylketonuric mutations in Japanese by analysis of phenylalanine hydroxylase mRNA from lymphoblasts
    • Okano Y., Hase Y., Shintaku H., Araki K., Furuyama J.-I., Oura T., and Isshiki G. Molecular characterization of phenylketonuric mutations in Japanese by analysis of phenylalanine hydroxylase mRNA from lymphoblasts. Hum. Mol. Genet. 4 (1994) 659-660
    • (1994) Hum. Mol. Genet. , vol.4 , pp. 659-660
    • Okano, Y.1    Hase, Y.2    Shintaku, H.3    Araki, K.4    Furuyama, J.-I.5    Oura, T.6    Isshiki, G.7
  • 20
    • 0018718487 scopus 로고
    • A microprocessor controlled mass spectrometer for the fully automated purification and isotopic analysis of breath carbon dioxide
    • Schoeller D.A., and Klein P.D. A microprocessor controlled mass spectrometer for the fully automated purification and isotopic analysis of breath carbon dioxide. Biomed. Mass Spectrom. 6 (1979) 350-355
    • (1979) Biomed. Mass Spectrom. , vol.6 , pp. 350-355
    • Schoeller, D.A.1    Klein, P.D.2
  • 21
    • 0021776312 scopus 로고
    • Predicting basal metabolic rate, new standards and review of previous work
    • Schofield W.N. Predicting basal metabolic rate, new standards and review of previous work. Hum. Nutr. Clin. Nutr. 39C Suppl 1 (1985) 5-41
    • (1985) Hum. Nutr. Clin. Nutr. , vol.39 C , Issue.SUPPL. 1 , pp. 5-41
    • Schofield, W.N.1
  • 22
    • 13044309416 scopus 로고
    • Biochemical studies on phenylketonuria I. Experimental hyperphenylalanemia in the rat
    • Goldstein F.B. Biochemical studies on phenylketonuria I. Experimental hyperphenylalanemia in the rat. J. Biol. Chem. 236 (1961) 2656-2661
    • (1961) J. Biol. Chem. , vol.236 , pp. 2656-2661
    • Goldstein, F.B.1
  • 23
    • 0015582942 scopus 로고
    • Detection of hepatic phenylalanine 4-hydroxylase in classical phenylketonuria
    • Friedman P.A., Fisher D.B., Kang E.S., and Kaufman S. Detection of hepatic phenylalanine 4-hydroxylase in classical phenylketonuria. Proc. Natl. Acad. Sci. USA 70 (1973) 552-556
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 552-556
    • Friedman, P.A.1    Fisher, D.B.2    Kang, E.S.3    Kaufman, S.4
  • 24
    • 0015233932 scopus 로고
    • Activation of phenylalanine hydroxylase by phenylalanine
    • Tourian A. Activation of phenylalanine hydroxylase by phenylalanine. Biochim. Biophys. Acta 242 (1971) 345-354
    • (1971) Biochim. Biophys. Acta , vol.242 , pp. 345-354
    • Tourian, A.1
  • 25
    • 0021337538 scopus 로고
    • The interaction of aromatic amino acids with rat liver phenylalanine hydroxylase
    • Phillips R.S., Parniak M.A., and Kaufman S. The interaction of aromatic amino acids with rat liver phenylalanine hydroxylase. J. Biol. Chem. 259 (1984) 271-277
    • (1984) J. Biol. Chem. , vol.259 , pp. 271-277
    • Phillips, R.S.1    Parniak, M.A.2    Kaufman, S.3
  • 26
    • 0021322175 scopus 로고
    • Ligand effects on the phosphorylation state of hepatic phenylalanine hydroxylase
    • Phillips R.S., and Kaufman S. Ligand effects on the phosphorylation state of hepatic phenylalanine hydroxylase. J. Biol. Chem. 259 (1984) 2474-2479
    • (1984) J. Biol. Chem. , vol.259 , pp. 2474-2479
    • Phillips, R.S.1    Kaufman, S.2
  • 27
    • 0021127277 scopus 로고
    • The effect of ligands of phenylalanine 4-monooxygenase on the cAMP-dependent phosphorylation of the enzyme
    • Doskeland A.P., Doskeland S.O., Ogreid D., and Flatmark T. The effect of ligands of phenylalanine 4-monooxygenase on the cAMP-dependent phosphorylation of the enzyme. J. Biol. Chem. 259 (1984) 11242-11248
    • (1984) J. Biol. Chem. , vol.259 , pp. 11242-11248
    • Doskeland, A.P.1    Doskeland, S.O.2    Ogreid, D.3    Flatmark, T.4
  • 28
    • 0026580410 scopus 로고
    • Phenylalanine-induced phosphorylation and activation of rat hepatic phenylalanine hydroxylase in vivo
    • Tipper J., and Kaufman S. Phenylalanine-induced phosphorylation and activation of rat hepatic phenylalanine hydroxylase in vivo. J. Biol. Chem. 267 (1992) 889-896
    • (1992) J. Biol. Chem. , vol.267 , pp. 889-896
    • Tipper, J.1    Kaufman, S.2
  • 29
    • 0027355636 scopus 로고
    • The phenylalanine hydroxylating system
    • Kaufman S. The phenylalanine hydroxylating system. Adv. Enzymol. 67 (1993) 77-264
    • (1993) Adv. Enzymol. , vol.67 , pp. 77-264
    • Kaufman, S.1
  • 30
    • 0028033734 scopus 로고
    • Regulation of rat liver phenylalanine hydroxylase: III. Control of catalysis by (6R)-tetrahydrobiopterin and phenylalanine
    • Xia T., Gray D.W., and Shiman R. Regulation of rat liver phenylalanine hydroxylase: III. Control of catalysis by (6R)-tetrahydrobiopterin and phenylalanine. J. Biol. Chem. 269 (1994) 24657-24665
    • (1994) J. Biol. Chem. , vol.269 , pp. 24657-24665
    • Xia, T.1    Gray, D.W.2    Shiman, R.3
  • 31
    • 0028853230 scopus 로고
    • Coordinate regulation of tetrahydrobiopterin turnover and phenylalanine hydroxylase activity in rat liver cells
    • Mitnaul L.J., and Shiman R. Coordinate regulation of tetrahydrobiopterin turnover and phenylalanine hydroxylase activity in rat liver cells. Proc. Natl. Acad. Sci. USA 92 (1995) 885-889
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 885-889
    • Mitnaul, L.J.1    Shiman, R.2
  • 32
    • 0030057695 scopus 로고    scopus 로고
    • Structure-function relationships of phenylalanine hydroxylase revealed by radiation target analysis
    • Davis M.D., Parniak M.A., Kaufman S., and Kempner E. Structure-function relationships of phenylalanine hydroxylase revealed by radiation target analysis. Arch. Biochem. Biophys. 325 (1996) 235-244
    • (1996) Arch. Biochem. Biophys. , vol.325 , pp. 235-244
    • Davis, M.D.1    Parniak, M.A.2    Kaufman, S.3    Kempner, E.4
  • 33
    • 0031037146 scopus 로고    scopus 로고
    • The role of phenylalanine in structure-function relationships of phenylalanine hydroxylase revealed by radiation target analysis
    • Davis M.D., Parniak M.A., Kaufman S., and Kempner E. The role of phenylalanine in structure-function relationships of phenylalanine hydroxylase revealed by radiation target analysis. Proc. Natl. Acad. Sci. USA 94 (1997) 491-495
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 491-495
    • Davis, M.D.1    Parniak, M.A.2    Kaufman, S.3    Kempner, E.4
  • 34
    • 0017180252 scopus 로고
    • Biopterin derivatives in normal and phenylketonuric patients after oral loads of l-phenylalanine, l-tyrosine, and l-tryptophan
    • Leeming R.J., Blair J.A., Green A., and Raine D.N. Biopterin derivatives in normal and phenylketonuric patients after oral loads of l-phenylalanine, l-tyrosine, and l-tryptophan. Arch. Dis. Child. 51 (1976) 771-777
    • (1976) Arch. Dis. Child. , vol.51 , pp. 771-777
    • Leeming, R.J.1    Blair, J.A.2    Green, A.3    Raine, D.N.4
  • 35
    • 0025019368 scopus 로고
    • Missense mutations associated with RFLP haplotypes 1 and 4 of the human phenylalanine hydroxylase gene
    • Okano Y., Wang T., Eisensmith R.C., Steinmann B., Gitzelmann R., and Woo S.L.C. Missense mutations associated with RFLP haplotypes 1 and 4 of the human phenylalanine hydroxylase gene. Am. J. Hum. Genet. 46 (1990) 18-25
    • (1990) Am. J. Hum. Genet. , vol.46 , pp. 18-25
    • Okano, Y.1    Wang, T.2    Eisensmith, R.C.3    Steinmann, B.4    Gitzelmann, R.5    Woo, S.L.C.6
  • 37
    • 0031813245 scopus 로고    scopus 로고
    • PAH Mutation Analysis Consortium Database: 1997 prototype for relational locus-specific mutation databases
    • Nowacki P.M., Byck S., Prevost L., and Scriver C.R. PAH Mutation Analysis Consortium Database: 1997 prototype for relational locus-specific mutation databases. Nucleic Acids Res. 26 (1998) 220-225
    • (1998) Nucleic Acids Res. , vol.26 , pp. 220-225
    • Nowacki, P.M.1    Byck, S.2    Prevost, L.3    Scriver, C.R.4
  • 38
    • 0030249197 scopus 로고    scopus 로고
    • Recombinant human phenylalanine hydroxylase: novel regulatory and structural properties
    • Kowlessur D., Citron B.A., and Kaufman S. Recombinant human phenylalanine hydroxylase: novel regulatory and structural properties. Arch. Biochem. Biophys. 333 (1996) 85-95
    • (1996) Arch. Biochem. Biophys. , vol.333 , pp. 85-95
    • Kowlessur, D.1    Citron, B.A.2    Kaufman, S.3
  • 39
    • 0028901398 scopus 로고
    • Expression of recombinant human phenylalanine hydroxylase as fusion protein in Escherichia coli circumvents proteolytic degradation by host cell proteases. Isolation and characterization of the wild-type enzyme
    • Martinez A., Knappskog P.M., Olafsdottir S., Doskeland A.P., Eiken H.G., Svebak R.M., Bozzini M., Apold J., and Flatmark T. Expression of recombinant human phenylalanine hydroxylase as fusion protein in Escherichia coli circumvents proteolytic degradation by host cell proteases. Isolation and characterization of the wild-type enzyme. Biochem. J. 306 (1995) 589-597
    • (1995) Biochem. J. , vol.306 , pp. 589-597
    • Martinez, A.1    Knappskog, P.M.2    Olafsdottir, S.3    Doskeland, A.P.4    Eiken, H.G.5    Svebak, R.M.6    Bozzini, M.7    Apold, J.8    Flatmark, T.9
  • 40
    • 0016833290 scopus 로고
    • Studies on the phenylalanine hydroxylase system in liver slices
    • Milstien S., and Kaufman S. Studies on the phenylalanine hydroxylase system in liver slices. J. Biol. Chem. 250 (1975) 4777-4781
    • (1975) J. Biol. Chem. , vol.250 , pp. 4777-4781
    • Milstien, S.1    Kaufman, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.