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Volumn 460, Issue 2-3, 2003, Pages 163-170

Kinetic inhibitory profile of BIA 3-202, a novel fast tight-binding, reversible and competitive catechol-O-methyltransferase inhibitor

Author keywords

BIA 3 202; Catechol O methyltransferase inhibitor; Kinetic; Liver catechol O methyltransferase; Parkinson's disease

Indexed keywords

1 (3,4 DIHYDROXY 5 NITROPHENYL) 2 PHENYLETHANONE; ADRENALIN; ADRENALIN HYDROGEN TARTRATE; BENZENE DERIVATIVE; CATECHOL METHYLTRANSFERASE INHIBITOR; ENTACAPONE; METADRENALIN; NITECAPONE; S ADENOSYLMETHIONINE; TOLCAPONE; UNCLASSIFIED DRUG;

EID: 0037462481     PISSN: 00142999     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-2999(02)02879-0     Document Type: Article
Times cited : (28)

References (28)
  • 1
    • 70449228544 scopus 로고
    • Enzymatic O-methylation of epinephrine and other catechols
    • Axelrod J., Tomchick R. Enzymatic O-methylation of epinephrine and other catechols. J. Biol. Chem. 233:1958;702-705.
    • (1958) J. Biol. Chem. , vol.233 , pp. 702-705
    • Axelrod, J.1    Tomchick, R.2
  • 2
    • 0032949477 scopus 로고    scopus 로고
    • New, selective catechol-O-methyltransferase inhibitors as therapeutic agents in Parkinson's disease
    • Bonifati V., Meco G. New, selective catechol-O-methyltransferase inhibitors as therapeutic agents in Parkinson's disease. Pharmacol. Ther. 81:1999;1-36.
    • (1999) Pharmacol. Ther. , vol.81 , pp. 1-36
    • Bonifati, V.1    Meco, G.2
  • 3
    • 0017184389 scopus 로고
    • A rapid method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0016700753 scopus 로고
    • Tight binding inhibitors: I. Kinetic behavior
    • Cha S. Tight binding inhibitors: I. Kinetic behavior. Biochem. Pharmacol. 24:1975;2177-2185.
    • (1975) Biochem. Pharmacol. , vol.24 , pp. 2177-2185
    • Cha, S.1
  • 5
    • 0016829492 scopus 로고
    • Catechol-O-methyltransferase: Pharmacological aspects and physiological role
    • Guldberg H.C., Marsden C.A. Catechol-O-methyltransferase: pharmacological aspects and physiological role. Pharmacol. Rev. 27:1975;135-206.
    • (1975) Pharmacol. Rev. , vol.27 , pp. 135-206
    • Guldberg, H.C.1    Marsden, C.A.2
  • 6
    • 0015327378 scopus 로고
    • A linear equation that describes the steady-state kinetics of enzymes and subcellular particles interacting with tightly bound inhibitors
    • Henderson P.J.F. A linear equation that describes the steady-state kinetics of enzymes and subcellular particles interacting with tightly bound inhibitors. Biochem. J. 127:1972;321-333.
    • (1972) Biochem. J. , vol.127 , pp. 321-333
    • Henderson, P.J.F.1
  • 7
    • 0033816348 scopus 로고    scopus 로고
    • Costs in the treatment of parkinsonism
    • Jost W.H. Costs in the treatment of parkinsonism. J. Neurol. 247:2000;31-33.
    • (2000) J. Neurol. , vol.247 , pp. 31-33
    • Jost, W.H.1
  • 8
    • 0034095886 scopus 로고    scopus 로고
    • Clinical pharmacology, therapeutic use and potential of COMT inhibitors in Parkinson's disease
    • Kaakkola S. Clinical pharmacology, therapeutic use and potential of COMT inhibitors in Parkinson's disease. Drugs. 59:2000;1233-1250.
    • (2000) Drugs , vol.59 , pp. 1233-1250
    • Kaakkola, S.1
  • 10
    • 0031923914 scopus 로고    scopus 로고
    • COMT inhibition: A new treatment strategy for Parkinson's disease
    • Kurth M.C., Adler C.H. COMT inhibition: a new treatment strategy for Parkinson's disease. Neurology. 50:1998;S3-S14.
    • (1998) Neurology , vol.50
    • Kurth, M.C.1    Adler, C.H.2
  • 11
    • 0035133553 scopus 로고    scopus 로고
    • Molecular mechanisms controlling the rate and specificity of catechol O-methylation by human soluble catechol O-methyltransferase
    • Lautala P., Ulmanen I., Taskinen J. Molecular mechanisms controlling the rate and specificity of catechol O-methylation by human soluble catechol O-methyltransferase. Mol. Pharmacol. 59:2001;393-402.
    • (2001) Mol. Pharmacol. , vol.59 , pp. 393-402
    • Lautala, P.1    Ulmanen, I.2    Taskinen, J.3
  • 12
    • 0037204048 scopus 로고    scopus 로고
    • Synthesis of 1-(3,4-dihydroxy-5-nitrophenyl)-2-phenyl-ethanone and derivatives as potent and long-acting peripheral inhibitors of catechol-O-methyltransferase
    • Learmonth D.A., Vieira-Coelho M.A., Benes J., Alves P.C., Borges N., Freitas A.P., Soares-da-Silva P. Synthesis of 1-(3,4-dihydroxy-5-nitrophenyl)-2-phenyl-ethanone and derivatives as potent and long-acting peripheral inhibitors of catechol-O-methyltransferase. J. Med. Chem. 45:2002;685-695.
    • (2002) J. Med. Chem. , vol.45 , pp. 685-695
    • Learmonth, D.A.1    Vieira-Coelho, M.A.2    Benes, J.3    Alves, P.C.4    Borges, N.5    Freitas, A.P.6    Soares-da-Silva, P.7
  • 13
    • 0028918413 scopus 로고
    • Kinetics of human soluble and membrane-bound catechol O-methyltransferase: A revised mechanism and description of the thermolabile variant of the enzyme
    • Lotta T., Vidgren J., Tilgmann C., Ulmanen I., Melen K., Julkunen I., Taskinen J. Kinetics of human soluble and membrane-bound catechol O-methyltransferase: a revised mechanism and description of the thermolabile variant of the enzyme. Biochemistry. 34:1995;4202-4210.
    • (1995) Biochemistry , vol.34 , pp. 4202-4210
    • Lotta, T.1    Vidgren, J.2    Tilgmann, C.3    Ulmanen, I.4    Melen, K.5    Julkunen, I.6    Taskinen, J.7
  • 14
    • 0025801604 scopus 로고
    • Cloning and characterization of human placental catechol-O-methyltransferase cDNA
    • Lundström K., Salminen M., Jalanko A., Savolainen R., Ulmanen I. Cloning and characterization of human placental catechol-O-methyltransferase cDNA. DNA Cell Biol. 10:1991;181-189.
    • (1991) DNA Cell Biol. , vol.10 , pp. 181-189
    • Lundström, K.1    Salminen, M.2    Jalanko, A.3    Savolainen, R.4    Ulmanen, I.5
  • 15
    • 0038287034 scopus 로고    scopus 로고
    • Catechol-O-methyltransferase (COMT): Biochemistry, molecular biology, pharmacology, and clinical efficacy of the new selective COMT inhibitors
    • Männistö P.T., Kaakkola S. Catechol-O-methyltransferase (COMT): biochemistry, molecular biology, pharmacology, and clinical efficacy of the new selective COMT inhibitors. Pharmacol. Rev. 51:1999;593-628.
    • (1999) Pharmacol. Rev. , vol.51 , pp. 593-628
    • Männistö, P.T.1    Kaakkola, S.2
  • 17
    • 0026671534 scopus 로고
    • Biochemical and pharmacological properties of a peripherally acting catechol-O-methyltransferase inhibitor entacapone
    • Nissinen E., Linden I.B., Schultz E., Pohto P. Biochemical and pharmacological properties of a peripherally acting catechol-O-methyltransferase inhibitor entacapone. Naunyn-Schmiedeberg's Arch. Pharmacol. 346:1992;262-266.
    • (1992) Naunyn-Schmiedeberg's Arch. Pharmacol. , vol.346 , pp. 262-266
    • Nissinen, E.1    Linden, I.B.2    Schultz, E.3    Pohto, P.4
  • 19
    • 0034973443 scopus 로고    scopus 로고
    • An algorithm (decision tree) for the management of Parkinson's disease (2001): Treatment guidelines
    • Olanow C.W., Watts R.L., Koller W.C. An algorithm (decision tree) for the management of Parkinson's disease (2001): treatment guidelines. Neurology. 56:2001;S1-S88.
    • (2001) Neurology , vol.56
    • Olanow, C.W.1    Watts, R.L.2    Koller, W.C.3
  • 20
    • 0035907998 scopus 로고    scopus 로고
    • BIA 3-202, a novel catechol-O-methyltransferase inhibitor, enhances the availability of L-DOPA to the brain and reduces its O-methylation
    • Parada A., Loureiro A.I., Vieira-Coelho M.A., Hainzl D., Soares-da-Silva P. BIA 3-202, a novel catechol-O-methyltransferase inhibitor, enhances the availability of L-DOPA to the brain and reduces its O-methylation. Eur. J. Pharmacol. 420:2001;27-32.
    • (2001) Eur. J. Pharmacol. , vol.420 , pp. 27-32
    • Parada, A.1    Loureiro, A.I.2    Vieira-Coelho, M.A.3    Hainzl, D.4    Soares-da-Silva, P.5
  • 22
    • 0024388924 scopus 로고
    • Inhibition of rat liver and duodenum soluble catechol-O-methyltransferase by a tight-binding inhibitor OR-462
    • Schultz E., Nissinen E. Inhibition of rat liver and duodenum soluble catechol-O-methyltransferase by a tight-binding inhibitor OR-462. Biochem. Pharmacol. 38:1989;3953-3956.
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 3953-3956
    • Schultz, E.1    Nissinen, E.2
  • 23
    • 0041769319 scopus 로고    scopus 로고
    • Entacapone as an adjunctive treatment to levodopa in Parkinson's disease
    • Southampton: The Wessex Institute for Health Research and Development
    • Shepherd J., Clegg A. Entacapone as an adjunctive treatment to levodopa in Parkinson's disease. Development and Evaluation Committee Report. vol. 104:1999;1-50 The Wessex Institute for Health Research and Development, Southampton.
    • (1999) Development and Evaluation Committee Report , vol.104 , pp. 1-50
    • Shepherd, J.1    Clegg, A.2
  • 24
    • 0028210328 scopus 로고
    • Crystal structure of catechol-O-methyltransferase
    • Vidgren J., Svensson L.A., Liljas A. Crystal structure of catechol-O-methyltransferase. Nature. 368:1994;354-358.
    • (1994) Nature , vol.368 , pp. 354-358
    • Vidgren, J.1    Svensson, L.A.2    Liljas, A.3
  • 25
    • 0030040182 scopus 로고    scopus 로고
    • Ontogenic aspects of liver and kidney catechol-O-methyltransferase sensitivity to tolcapone
    • Vieira-Coelho M.A., Soares-da-Silva P. Ontogenic aspects of liver and kidney catechol-O-methyltransferase sensitivity to tolcapone. Br. J. Pharmacol. 117:1996;516-520.
    • (1996) Br. J. Pharmacol. , vol.117 , pp. 516-520
    • Vieira-Coelho, M.A.1    Soares-da-Silva, P.2
  • 26
    • 0033528426 scopus 로고    scopus 로고
    • Effects of tolcapone upon soluble and membrane-bound brain and liver catechol-O-methyltransferase
    • Vieira-Coelho M.A., Soares-da-Silva P. Effects of tolcapone upon soluble and membrane-bound brain and liver catechol-O-methyltransferase. Brain Res. 821:1999;69-78.
    • (1999) Brain Res. , vol.821 , pp. 69-78
    • Vieira-Coelho, M.A.1    Soares-da-Silva, P.2
  • 27
    • 12244273058 scopus 로고
    • Evaluation of methods for estimating the dissociation constant of tight binding enzyme inhibitors
    • William R., Hakala M.T. Evaluation of methods for estimating the dissociation constant of tight binding enzyme inhibitors. J. Biol. Chem. 264:1979;1204-1209.
    • (1979) J. Biol. Chem. , vol.264 , pp. 1204-1209
    • William, R.1    Hakala, M.T.2
  • 28
    • 0018699952 scopus 로고
    • The kinetics of reversible tight-binding inhibition
    • Purich D.L. New York: Academic Press
    • Williams J.W., Morrison J.F. The kinetics of reversible tight-binding inhibition. Purich D.L. Methods in Enzymology. vol. 63:1979;437-467 Academic Press, New York.
    • (1979) Methods in Enzymology , vol.63 , pp. 437-467
    • Williams, J.W.1    Morrison, J.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.