Pharmacokinetic?pharmacodynamic interaction between BIA 3-202, a novel COMT inhibitor, and levodopa/benserazide
نویسندگان
چکیده
منابع مشابه
Human metabolism of nebicapone (BIA 3-202), a novel catechol-o-methyltransferase inhibitor: characterization of in vitro glucuronidation.
Nebicapone (BIA 3-202; 1-[3,4-dihydroxy-5-nitrophenyl]-2-phenylethanone), a novel catechol-O-methyltransferase inhibitor, is mainly metabolized by glucuronidation. The purpose of this study was to characterize the major plasma metabolites of nebicapone following p.o. administration of nebicapone to healthy volunteers, and to determine the human UDP-glucuronosyltransferase (UGT) enzymes involved...
متن کاملMolecular modeling and metabolic studies of the interaction of catechol-O-methyltransferase and a new nitrocatechol inhibitor.
Catechol-O-methyltransferase (COMT, EC 2.1.1.6) plays a central role in the metabolic inactivation of neurotransmitters and neuroactive xenobiotics possessing a catechol motif. 1-(3,4-Dihydroxy-5-nitrophenyl)-2-phenyl-ethanone (BIA 3-202) is a novel nitrocatechol-type inhibitor of COMT, the potential clinical benefit of which is currently being evaluated in the treatment of Parkinson's disease....
متن کاملAssociation of COMT and COMT-DRD2 interaction with creative potential
Several lines of evidence suggest that genes involved in dopamine (DA) transmission may contribute to creativity. Among these genes, the catechol-O-methyltransferase gene (COMT) and the dopamine D2 receptor gene (DRD2) are the most promising candidates. Our previous study has revealed evidence for the involvement of DRD2 in creative potential. The present study extended our previous study by sy...
متن کاملEN 202 : Problem Set 3
At this point, we require an explicit form of the characteristics. First, consider the solution to the ODE ȳξ(ξ, η) = 1. Integrating with respect to ξ, we find ȳ = ξ + φ(η). Applying the initial value on Γ, where y0(η) = 0 and ξ = 0, we find φ(η) = 0. Next, consider the solution to the ODE x̄ξ(ξ, η) = η . Integrating with respect to ξ, we find x̄ = ξη + ψ(η). Using the initial value on Γ, where x...
متن کاملKinetics and crystal structure of catechol-o-methyltransferase complex with co-substrate and a novel inhibitor with potential therapeutic application.
Catechol-O-methyltransferase (COMT; E.C. 2.1.1.6) is a ubiquitous enzyme in nature that plays an important role in the metabolism of catechol neurotransmitters and xenobiotics. In particular, inactivation of drugs such as L-3,4-dihydroxyphenylalanine (L-DOPA) via O-methylation is of relevant pharmacological importance, because L-DOPA is currently the most effective drug used in the treatment of...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: European Journal of Clinical Pharmacology
سال: 2003
ISSN: 0031-6970,1432-1041
DOI: 10.1007/s00228-003-0680-5