K
Kunio Itoh
Researcher at Tohoku Pharmaceutical University
Publications - 24
Citations - 341
Kunio Itoh is an academic researcher from Tohoku Pharmaceutical University. The author has contributed to research in topics: Aldehyde oxidase & Enzyme. The author has an hindex of 14, co-authored 24 publications receiving 326 citations.
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Journal ArticleDOI
Stereoselective pharmacokinetics of RS‐8359, a selective and reversible MAO‐A inhibitor, by species‐dependent drug‐metabolizing enzymes
Wataru Takasaki,Mayumi Yamamura,Akiko Nozaki,Takashi Nitanai,Kunihiro Sasahara,Kunio Itoh,Yorihisa Tanaka +6 more
TL;DR: The rapid disappearance of the (S)-enantiomer from the plasma was thought to be due to the rapid metabolism of the (+/-)-4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta[d]pyrimidine by different drug-metabolizing enzymes, depending on species.
Journal ArticleDOI
Species differences in enantioselective 2-oxidations of RS-8359, a selective and reversible MAO-A inhibitor, and cinchona alkaloids by aldehyde oxidase.
TL;DR: In vitro results were in good accordance with previously reported in vivo excretion data of the 2‐keto metabolite and the non‐detectable plasma concentrations of the (S)‐enantiomer in monkeys and humans after administration of racemic RS‐8359.
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Lack of dimer formation ability in rat strains with low aldehyde oxidase activity
TL;DR: It is suggested that rat strains with low AO activity lack the ability to produce a dimer necessary for catalytic activity, and AO differences in rat strains should be discussed in terms of the expression levels of the dimer itself.
Journal ArticleDOI
Cloning, expression, and characterization of male cynomolgus monkey liver aldehyde oxidase
Kouichi Hoshino,Kunio Itoh,Akiko Masubuchi,Mayuko Adachi,Tasuku Asakawa,Nobuaki Watanabe,Toshiyuki Kosaka,Yorihisa Tanaka +7 more
TL;DR: The results suggested that two forms of aldehyde oxidase in monkey were the expression products by a single gene, and the biphasic pattern was observed for Eadie-Hofstee plots of the (S)-enantiospecific 2-oxidation activity of RS-8359 with the expressed and cytosolic monkey liver alde Hyde oxidase.
Journal ArticleDOI
Stereospecific oxidation of the (S)-enantiomer of RS-8359, a selective and reversible monoamine oxidase A (MAO-A) inhibitor, by aldehyde oxidase.
Kunio Itoh,M Yamamura,S Muramatsu,Kouichi Hoshino,Akiko Masubuchi,Takamitsu Sasaki,Yorihisa Tanaka +6 more
TL;DR: The results suggest that the enzyme responsible for the biotransformation of RS-8359 to give the 2-keto derivative is aldehyde oxidase (EC 1.2.3.1).