메뉴 건너뛰기




Volumn 80, Issue 10, 2010, Pages 1563-1571

New insights into tetrahydrobiopterin pharmacodynamics from Pahenu1/2, a mouse model for compound heterozygous tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency

Author keywords

Compound heterozygous; Mouse model; Pharmacodynamics; Phenylketonuria; Tetrahydrobiopterin

Indexed keywords

CARBON 13; PHENYLALANINE; PHENYLALANINE 4 MONOOXYGENASE; TETRAHYDROBIOPTERIN; BIOPTERIN; SAPROPTERIN; TYROSINE;

EID: 77957018961     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2010.07.042     Document Type: Article
Times cited : (13)

References (39)
  • 1
    • 0028124992 scopus 로고
    • Regulation of rat liver phenylalanine hydroxylase. I. Kinetic properties of the enzymes iron and enzyme reduction site
    • Shiman R., Gray D.W., Hill M.A. Regulation of rat liver phenylalanine hydroxylase. I. Kinetic properties of the enzymes iron and enzyme reduction site. J Biol Chem 1994, 269:24637-24646.
    • (1994) J Biol Chem , vol.269 , pp. 24637-24646
    • Shiman, R.1    Gray, D.W.2    Hill, M.A.3
  • 2
    • 0027937757 scopus 로고
    • Regulation of rat liver phenylalanine hydroxylase. II. Substrate binding and the role of activation in the control of enzymatic activity
    • Shiman R., Xia T., Hill M.A., Gray D.W. Regulation of rat liver phenylalanine hydroxylase. II. Substrate binding and the role of activation in the control of enzymatic activity. J Biol Chem 1994, 269:24647-24656.
    • (1994) J Biol Chem , vol.269 , pp. 24647-24656
    • Shiman, R.1    Xia, T.2    Hill, M.A.3    Gray, D.W.4
  • 3
    • 0028033734 scopus 로고
    • Regulation of rat liver phenylalanine hydroxylase. III. Control of catalysis by (6R)-tetrahydrobiopterin and phenylalanine
    • Xia T., Gray D.W., Shiman R. Regulation of rat liver phenylalanine hydroxylase. III. Control of catalysis by (6R)-tetrahydrobiopterin and phenylalanine. J Biol Chem 1994, 269:24657-24665.
    • (1994) J Biol Chem , vol.269 , pp. 24657-24665
    • Xia, T.1    Gray, D.W.2    Shiman, R.3
  • 4
    • 46149093432 scopus 로고    scopus 로고
    • Loss of function in phenylketonuria is caused by impaired molecular motions and conformational instability
    • Gersting S.W., Kemter K.F., Staudigl M., Messing D.D., Danecka M.K., Lagler F.B., et al. Loss of function in phenylketonuria is caused by impaired molecular motions and conformational instability. Am J Hum Genet 2008, 83:5-17.
    • (2008) Am J Hum Genet , vol.83 , pp. 5-17
    • Gersting, S.W.1    Kemter, K.F.2    Staudigl, M.3    Messing, D.D.4    Danecka, M.K.5    Lagler, F.B.6
  • 6
  • 7
    • 0033504353 scopus 로고    scopus 로고
    • Tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency
    • Kure S., Hou D.C., Ohura T., Iwamoto H., Suzuki S., Sugiyama N., et al. Tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency. J Pediatr 1999, 135:375-378.
    • (1999) J Pediatr , vol.135 , pp. 375-378
    • Kure, S.1    Hou, D.C.2    Ohura, T.3    Iwamoto, H.4    Suzuki, S.5    Sugiyama, N.6
  • 10
    • 63449107693 scopus 로고    scopus 로고
    • Efficacy of sapropterin dihydrochloride in increasing phenylalanine tolerance in children with phenylketonuria: a phase III, randomized, double-blind, placebo-controlled study
    • Trefz F.K., Burton B.K., Longo N., Casanova M.M., Gruskin D.J., Dorenbaum A., et al. Efficacy of sapropterin dihydrochloride in increasing phenylalanine tolerance in children with phenylketonuria: a phase III, randomized, double-blind, placebo-controlled study. J Pediatr 2009, 154:700-707.
    • (2009) J Pediatr , vol.154 , pp. 700-707
    • Trefz, F.K.1    Burton, B.K.2    Longo, N.3    Casanova, M.M.4    Gruskin, D.J.5    Dorenbaum, A.6
  • 11
    • 35248882919 scopus 로고    scopus 로고
    • The response of patients with phenylketonuria and elevated serum phenylalanine to treatment with oral sapropterin dihydrochloride (6R-tetrahydrobiopterin): a phase II, multicentre, open-label, screening study
    • Burton B.K., Grange D.K., Milanowski A., Vockley G., Feillet F., Crombez E.A., et al. The response of patients with phenylketonuria and elevated serum phenylalanine to treatment with oral sapropterin dihydrochloride (6R-tetrahydrobiopterin): a phase II, multicentre, open-label, screening study. J Inherit Metab Dis 2007, 30:700-707.
    • (2007) J Inherit Metab Dis , vol.30 , pp. 700-707
    • Burton, B.K.1    Grange, D.K.2    Milanowski, A.3    Vockley, G.4    Feillet, F.5    Crombez, E.A.6
  • 12
    • 34547697475 scopus 로고    scopus 로고
    • Efficacy of sapropterin dihydrochloride (tetrahydrobiopterin, 6R-BH4) for reduction of phenylalanine concentration in patients with phenylketonuria: a phase III randomised placebo-controlled study
    • Levy H.L., Milanowski A., Chakrapani A., Cleary M., Lee P., Trefz F.K., et al. Efficacy of sapropterin dihydrochloride (tetrahydrobiopterin, 6R-BH4) for reduction of phenylalanine concentration in patients with phenylketonuria: a phase III randomised placebo-controlled study. Lancet 2007, 370:504-510.
    • (2007) Lancet , vol.370 , pp. 504-510
    • Levy, H.L.1    Milanowski, A.2    Chakrapani, A.3    Cleary, M.4    Lee, P.5    Trefz, F.K.6
  • 13
    • 56049113280 scopus 로고    scopus 로고
    • Safety and efficacy of 22 weeks of treatment with sapropterin dihydrochloride in patients with phenylketonuria
    • Lee P., Treacy E.P., Crombez E., Wasserstein M., Waber L., Wolff J., et al. Safety and efficacy of 22 weeks of treatment with sapropterin dihydrochloride in patients with phenylketonuria. Am J Med Genet A 2008, 146A:2851-2859.
    • (2008) Am J Med Genet A , vol.146 A , pp. 2851-2859
    • Lee, P.1    Treacy, E.P.2    Crombez, E.3    Wasserstein, M.4    Waber, L.5    Wolff, J.6
  • 14
    • 10044279157 scopus 로고    scopus 로고
    • Correction of kinetic and stability defects by tetrahydrobiopterin in phenylketonuria patients with certain phenylalanine hydroxylase mutations
    • Erlandsen H., Pey A.L., Gámez A., Pérez B., Desviat L.R., Aguado C., et al. Correction of kinetic and stability defects by tetrahydrobiopterin in phenylketonuria patients with certain phenylalanine hydroxylase mutations. Proc Natl Acad Sci USA 2004, 101:16903-16908.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 16903-16908
    • Erlandsen, H.1    Pey, A.L.2    Gámez, A.3    Pérez, B.4    Desviat, L.R.5    Aguado, C.6
  • 15
    • 8144220031 scopus 로고    scopus 로고
    • Mechanisms underlying responsiveness to tetrahydrobiopterin in mild phenylketonuria mutations
    • Pey A.L., Pérez B., Desviat L.R., Martínez M.A., Aguado C., Erlandsen H., et al. Mechanisms underlying responsiveness to tetrahydrobiopterin in mild phenylketonuria mutations. Hum Mutat 2004, 24:388-399.
    • (2004) Hum Mutat , vol.24 , pp. 388-399
    • Pey, A.L.1    Pérez, B.2    Desviat, L.R.3    Martínez, M.A.4    Aguado, C.5    Erlandsen, H.6
  • 16
    • 77952483396 scopus 로고    scopus 로고
    • Pahenu1 is a mouse model for tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency and promotes analysis of the pharmacological chaperone mechanism in vivo
    • Gersting S.W., Lagler F.B., Eichinger A., Kemter K.F., Danecka M.K., Messing D.D., et al. Pahenu1 is a mouse model for tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency and promotes analysis of the pharmacological chaperone mechanism in vivo. Hum Mol Genet 2010, 19:2039-2049.
    • (2010) Hum Mol Genet , vol.19 , pp. 2039-2049
    • Gersting, S.W.1    Lagler, F.B.2    Eichinger, A.3    Kemter, K.F.4    Danecka, M.K.5    Messing, D.D.6
  • 17
    • 0025156603 scopus 로고
    • The use of N-ethyl-N-nitrosourea to produce mouse models for human phenylketonuria and hyperphenylalaninemia
    • McDonald J.D., Bode V.C., Dove W.F., Shedlovsky A. The use of N-ethyl-N-nitrosourea to produce mouse models for human phenylketonuria and hyperphenylalaninemia. Prog Clin Biol Res 1990, 340C:407-413.
    • (1990) Prog Clin Biol Res , vol.340 C , pp. 407-413
    • McDonald, J.D.1    Bode, V.C.2    Dove, W.F.3    Shedlovsky, A.4
  • 19
    • 0031081364 scopus 로고    scopus 로고
    • Characterization of mutations at the mouse phenylalanine hydroxylase locus
    • McDonald J.D., Charlton C.K. Characterization of mutations at the mouse phenylalanine hydroxylase locus. Genomics 1997, 39:402-405.
    • (1997) Genomics , vol.39 , pp. 402-405
    • McDonald, J.D.1    Charlton, C.K.2
  • 20
    • 0034012174 scopus 로고    scopus 로고
    • A heteroallelic mutant mouse model: a new orthologue for human hyperphenylalaninemia
    • Sarkissian C.N., Boulais D.M., McDonald J.D., Scriver C.R. A heteroallelic mutant mouse model: a new orthologue for human hyperphenylalaninemia. Mol Genet Metab 2000, 69:188-194.
    • (2000) Mol Genet Metab , vol.69 , pp. 188-194
    • Sarkissian, C.N.1    Boulais, D.M.2    McDonald, J.D.3    Scriver, C.R.4
  • 21
    • 28844441226 scopus 로고    scopus 로고
    • Clinical and nutritional evaluation of phenylketonuric patients on tetrahydrobiopterin monotherapy
    • Lambruschini N., Pérez-Dueñas B., Vilaseca M.A., Mas A., Artuch R., Gassió R., et al. Clinical and nutritional evaluation of phenylketonuric patients on tetrahydrobiopterin monotherapy. Mol Genet Metab 2005, 86(Suppl. 1):S54-60.
    • (2005) Mol Genet Metab , vol.86 , Issue.SUPPL. 1
    • Lambruschini, N.1    Pérez-Dueñas, B.2    Vilaseca, M.A.3    Mas, A.4    Artuch, R.5    Gassió, R.6
  • 22
    • 28844448239 scopus 로고    scopus 로고
    • Spanish BH4-responsive phenylalanine hydroxylase-deficient patients: evolution of seven patients on long-term treatment with tetrahydrobiopterin
    • Bélanger-Quintana A., García M.J., Castro M., Desviat L.R., Pérez B., Mejía B., et al. Spanish BH4-responsive phenylalanine hydroxylase-deficient patients: evolution of seven patients on long-term treatment with tetrahydrobiopterin. Mol Genet Metab 2005, 86(Suppl. 1):S61-S66.
    • (2005) Mol Genet Metab , vol.86 , Issue.SUPPL. 1
    • Bélanger-Quintana, A.1    García, M.J.2    Castro, M.3    Desviat, L.R.4    Pérez, B.5    Mejía, B.6
  • 23
    • 38149014672 scopus 로고    scopus 로고
    • Molecular genetics of tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency
    • Zurflüh M.R., Zschocke J., Lindner M., Feillet F., Chery C., Burlina A., et al. Molecular genetics of tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency. Hum Mutat 2008, 29:167-175.
    • (2008) Hum Mutat , vol.29 , pp. 167-175
    • Zurflüh, M.R.1    Zschocke, J.2    Lindner, M.3    Feillet, F.4    Chery, C.5    Burlina, A.6
  • 24
    • 77649233104 scopus 로고    scopus 로고
    • Tetrahydrobiopterin responsiveness after extended loading test of 12 Danish PKU patients with the Y414C mutation
    • Nielsen J.B., Nielsen K.E., Güttler F. Tetrahydrobiopterin responsiveness after extended loading test of 12 Danish PKU patients with the Y414C mutation. J Inherit Metab Dis 2010, 33:9-16.
    • (2010) J Inherit Metab Dis , vol.33 , pp. 9-16
    • Nielsen, J.B.1    Nielsen, K.E.2    Güttler, F.3
  • 25
    • 28844468010 scopus 로고    scopus 로고
    • Extended tetrahydrobiopterin loading test in the diagnosis of cofactor-responsive phenylketonuria: a pilot study
    • Fiege B., Bonafé L., Ballhausen D., Baumgartner M., Thöny B., Meili D., et al. Extended tetrahydrobiopterin loading test in the diagnosis of cofactor-responsive phenylketonuria: a pilot study. Mol Genet Metab 2005, 86(Suppl. 1):S91-S95.
    • (2005) Mol Genet Metab , vol.86 , Issue.SUPPL. 1
    • Fiege, B.1    Bonafé, L.2    Ballhausen, D.3    Baumgartner, M.4    Thöny, B.5    Meili, D.6
  • 26
    • 67349161346 scopus 로고    scopus 로고
    • Genotype-predicted tetrahydrobiopterin (BH4)-responsiveness and molecular genetics in Croatian patients with phenylalanine hydroxylase (PAH) deficiency
    • Karacić I., Meili D., Sarnavka V., Heintz C., Thöny B., Ramadza D.P., et al. Genotype-predicted tetrahydrobiopterin (BH4)-responsiveness and molecular genetics in Croatian patients with phenylalanine hydroxylase (PAH) deficiency. Mol Genet Metab 2009, 97:165-171.
    • (2009) Mol Genet Metab , vol.97 , pp. 165-171
    • Karacić, I.1    Meili, D.2    Sarnavka, V.3    Heintz, C.4    Thöny, B.5    Ramadza, D.P.6
  • 27
    • 0030849458 scopus 로고    scopus 로고
    • Analysis of phenylalanine hydroxylase genotypes and hyperphenylalaninemia phenotypes using l-[1-13C]phenylalanine oxidation rates in vivo: a pilot study
    • Treacy E.P., Delente J.J., Elkas G., Carter K., Lambert M., Waters P.J., et al. Analysis of phenylalanine hydroxylase genotypes and hyperphenylalaninemia phenotypes using l-[1-13C]phenylalanine oxidation rates in vivo: a pilot study. Pediatr Res 1997, 42:430-435.
    • (1997) Pediatr Res , vol.42 , pp. 430-435
    • Treacy, E.P.1    Delente, J.J.2    Elkas, G.3    Carter, K.4    Lambert, M.5    Waters, P.J.6
  • 28
    • 0029804894 scopus 로고    scopus 로고
    • 2 in human bicarbonate studies: a critical review with original data
    • 2 in human bicarbonate studies: a critical review with original data. Clin Sci (Lond) 1996, 91:665-677.
    • (1996) Clin Sci (Lond) , vol.91 , pp. 665-677
    • Leijssen, D.P.1    Elia, M.2
  • 29
    • 28844443876 scopus 로고    scopus 로고
    • Screening for tetrahydrobiopterin deficiencies using dried blood spots on filter paper
    • Zurflüh M.R., Giovannini M., Fiori L., Fiege B., Gokdemir Y., Baykal T., et al. Screening for tetrahydrobiopterin deficiencies using dried blood spots on filter paper. Mol Genet Metab 2005, 86(Suppl. 1):S96-103.
    • (2005) Mol Genet Metab , vol.86 , Issue.SUPPL. 1
    • Zurflüh, M.R.1    Giovannini, M.2    Fiori, L.3    Fiege, B.4    Gokdemir, Y.5    Baykal, T.6
  • 31
    • 77957018675 scopus 로고    scopus 로고
    • The bi-exponential pharmacokinetic equation is suited to characterize lactate and ammonia concentration versus time data of the ischemic forearm exercise test
    • Koch H.J., Uyanik G., Raschka C., Schweizer J. The bi-exponential pharmacokinetic equation is suited to characterize lactate and ammonia concentration versus time data of the ischemic forearm exercise test. Neurol Rehabil 2002, 8:235-238.
    • (2002) Neurol Rehabil , vol.8 , pp. 235-238
    • Koch, H.J.1    Uyanik, G.2    Raschka, C.3    Schweizer, J.4
  • 32
    • 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
    • Martínez A., Knappskog P.M., Olafsdottir S., Døskeland A.P., Eiken H.G., Svebak R.M., et al. 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 1995, 306(Pt 2):589-597.
    • (1995) Biochem J , vol.306 , Issue.PART 2 , pp. 589-597
    • Martínez, A.1    Knappskog, P.M.2    Olafsdottir, S.3    Døskeland, A.P.4    Eiken, H.G.5    Svebak, R.M.6
  • 33
    • 19444380153 scopus 로고    scopus 로고
    • The active site residue tyrosine 325 influences iron binding and coupling efficiency in human phenylalanine hydroxylase
    • Miranda F.F., Kolberg M., Andersson K.K., Geraldes C.F., Martínez A. The active site residue tyrosine 325 influences iron binding and coupling efficiency in human phenylalanine hydroxylase. J Inorg Biochem 2005, 99:1320-1328.
    • (2005) J Inorg Biochem , vol.99 , pp. 1320-1328
    • Miranda, F.F.1    Kolberg, M.2    Andersson, K.K.3    Geraldes, C.F.4    Martínez, A.5
  • 34
    • 0021322175 scopus 로고
    • Ligand effects on the phosphorylation state of hepatic phenylalanine hydroxylase
    • Phillips R.S., Kaufman S. Ligand effects on the phosphorylation state of hepatic phenylalanine hydroxylase. J Biol Chem 1984, 259:2474-2479.
    • (1984) J Biol Chem , vol.259 , pp. 2474-2479
    • Phillips, R.S.1    Kaufman, S.2
  • 35
    • 0030437749 scopus 로고    scopus 로고
    • Structure/function relationships in human phenylalanine hydroxylase. Effect of terminal deletions on the oligomerization, activation and cooperativity of substrate binding to the enzyme
    • Knappskog P.M., Flatmark T., Aarden J.M., Haavik J., Martínez A. Structure/function relationships in human phenylalanine hydroxylase. Effect of terminal deletions on the oligomerization, activation and cooperativity of substrate binding to the enzyme. Eur J Biochem 1996, 242:813-821.
    • (1996) Eur J Biochem , vol.242 , pp. 813-821
    • Knappskog, P.M.1    Flatmark, T.2    Aarden, J.M.3    Haavik, J.4    Martínez, A.5
  • 36
    • 0034053789 scopus 로고    scopus 로고
    • The V388M mutation results in a kinetic variant form of phenylalanine hydroxylase
    • Leandro P., Rivera I., Lechner M.C., de Almeida I.T., Konecki D. The V388M mutation results in a kinetic variant form of phenylalanine hydroxylase. Mol Genet Metab 2000, 69:204-212.
    • (2000) Mol Genet Metab , vol.69 , pp. 204-212
    • Leandro, P.1    Rivera, I.2    Lechner, M.C.3    de Almeida, I.T.4    Konecki, D.5
  • 37
    • 64649100230 scopus 로고    scopus 로고
    • Sapropterin: a review of its use in the treatment of primary hyperphenylalaninaemia
    • Sanford M., Keating G.M. Sapropterin: a review of its use in the treatment of primary hyperphenylalaninaemia. Drugs 2009, 69:461-476.
    • (2009) Drugs , vol.69 , pp. 461-476
    • Sanford, M.1    Keating, G.M.2
  • 38
    • 37349013379 scopus 로고    scopus 로고
    • A counterintuitive approach to treat enzyme deficiencies: use of enzyme inhibitors for restoring mutant enzyme activity
    • Fan J.Q. A counterintuitive approach to treat enzyme deficiencies: use of enzyme inhibitors for restoring mutant enzyme activity. Biol Chem 2008, 389:1-11.
    • (2008) Biol Chem , vol.389 , pp. 1-11
    • Fan, J.Q.1
  • 39
    • 33751064142 scopus 로고    scopus 로고
    • Pharmacokinetics of orally administered tetrahydrobiopterin in patients with phenylalanine hydroxylase deficiency
    • Zurflüh M.R., Fiori L., Fiege B., Ozen I., Demirkol M., Gärtner K.H., et al. Pharmacokinetics of orally administered tetrahydrobiopterin in patients with phenylalanine hydroxylase deficiency. J Inherit Metab Dis 2006, 29:725-731.
    • (2006) J Inherit Metab Dis , vol.29 , pp. 725-731
    • Zurflüh, M.R.1    Fiori, L.2    Fiege, B.3    Ozen, I.4    Demirkol, M.5    Gärtner, K.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.