Rat strain differences in stereospecific 2-oxidation of RS-8359, a reversible and selective MAO-A inhibitor, by aldehyde oxidase

Aldehyde oxidase catalysed 2‐oxidation activity of the (S)‐enantiomer of RS‐8359, a selective and reversible monoamine oxidase A (MAO‐A) inhibitor, was investigated in liver cytosolic fractions from ten rat strains. Remarkably large strain differences were observed with approximately a 230 variation...

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Published in	Biopharmaceutics & drug disposition Vol. 27; no. 5; pp. 247 - 255
Main Authors	Sasaki, Takamitsu, Masubuchi, Akiko, Yamamura, Mayumi, Watanabe, Nobuaki, Hiratsuka, Masahiro, Mizugaki, Michinao, Itoh, Kunio, Tanaka, Yorihisa
Format	Journal Article
Language	English
Published	Chichester, UK John Wiley & Sons, Ltd 01.07.2006 Wiley
Subjects	aldehyde oxidase Aldehyde Oxidase - analysis Aldehyde Oxidase - genetics Aldehyde Oxidase - metabolism Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Blotting, Northern Catalysis Cytosol - enzymology Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Liver - enzymology Male MAO-A inhibitor Mice Monoamine Oxidase Inhibitors - metabolism Nitriles - metabolism Oxidation-Reduction Oxidoreductases Pyrimidines - metabolism rat Rats Rats, Inbred Strains RNA, Messenger - analysis RNA, Messenger - metabolism RS-8359 Stereoisomerism stereoselectivity strain differences Rat Enzyme Rodentia Strain specificity Metabolism MAO-A inhibitor Isomer Monoamine oxidase A inhibitor strain differences Stereoselectivity Vertebrata Mammalia Animal Aldehyde oxidase Oxidation Oxidoreductases Pharmacokinetics RS-8359
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ISSN	0142-2782 1099-081X
DOI	10.1002/bdd.504

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Abstract	Aldehyde oxidase catalysed 2‐oxidation activity of the (S)‐enantiomer of RS‐8359, a selective and reversible monoamine oxidase A (MAO‐A) inhibitor, was investigated in liver cytosolic fractions from ten rat strains. Remarkably large strain differences were observed with approximately a 230 variation between the highest activity in the Wistar‐Imamichi strain and the lowest activity in the Slc:Wistar strain. The activities of Crj:SD and Slc:SD strain rats were considerably low, and that of the F344/DuCrj strain was very low. Among six Wistar strains, Crj:Wistar, Slc:Wistar, WKY/Izm, WKAH/Hkm, Jcl:Wistar and Wistar‐Imamichi, the Slc:Wistar strain rats showed exceptionally low 2‐oxidation activity that was comparable to that of the F344/DuCrj strain. The rat strain differences in the catalytic activity of aldehyde oxidase could correlate in part with the expressed levels of protein based on the mRNA of aldehyde oxidase. However, no small discrepancy existed in the almost negligible catalytic activity and the fairly high expression levels of protein and mRNA in the F344/DuCrj and Slc:Wistar strain rats. Some genetic factors might possibly be one of reasons for the discrepancy. Copyright © 2006 John Wiley & Sons, Ltd.
AbstractList	Aldehyde oxidase catalysed 2‐oxidation activity of the (S)‐enantiomer of RS‐8359, a selective and reversible monoamine oxidase A (MAO‐A) inhibitor, was investigated in liver cytosolic fractions from ten rat strains. Remarkably large strain differences were observed with approximately a 230 variation between the highest activity in the Wistar‐Imamichi strain and the lowest activity in the Slc:Wistar strain. The activities of Crj:SD and Slc:SD strain rats were considerably low, and that of the F344/DuCrj strain was very low. Among six Wistar strains, Crj:Wistar, Slc:Wistar, WKY/Izm, WKAH/Hkm, Jcl:Wistar and Wistar‐Imamichi, the Slc:Wistar strain rats showed exceptionally low 2‐oxidation activity that was comparable to that of the F344/DuCrj strain. The rat strain differences in the catalytic activity of aldehyde oxidase could correlate in part with the expressed levels of protein based on the mRNA of aldehyde oxidase. However, no small discrepancy existed in the almost negligible catalytic activity and the fairly high expression levels of protein and mRNA in the F344/DuCrj and Slc:Wistar strain rats. Some genetic factors might possibly be one of reasons for the discrepancy. Copyright © 2006 John Wiley & Sons, Ltd. Aldehyde oxidase catalysed 2-oxidation activity of the (S)-enantiomer of RS-8359, a selective and reversible monoamine oxidase A (MAO-A) inhibitor, was investigated in liver cytosolic fractions from ten rat strains. Remarkably large strain differences were observed with approximately a 230 variation between the highest activity in the Wistar-Imamichi strain and the lowest activity in the Slc:Wistar strain. The activities of Crj:SD and Slc:SD strain rats were considerably low, and that of the F344/DuCrj strain was very low. Among six Wistar strains, Crj:Wistar, Slc:Wistar, WKY/Izm, WKAH/Hkm, Jcl:Wistar and Wistar-Imamichi, the Slc:Wistar strain rats showed exceptionally low 2-oxidation activity that was comparable to that of the F344/DuCrj strain. The rat strain differences in the catalytic activity of aldehyde oxidase could correlate in part with the expressed levels of protein based on the mRNA of aldehyde oxidase. However, no small discrepancy existed in the almost negligible catalytic activity and the fairly high expression levels of protein and mRNA in the F344/DuCrj and Slc:Wistar strain rats. Some genetic factors might possibly be one of reasons for the discrepancy. Aldehyde oxidase catalysed 2-oxidation activity of the (S)-enantiomer of RS-8359, a selective and reversible monoamine oxidase A (MAO-A) inhibitor, was investigated in liver cytosolic fractions from ten rat strains. Remarkably large strain differences were observed with approximately a 230 variation between the highest activity in the Wistar-Imamichi strain and the lowest activity in the Slc:Wistar strain. The activities of Crj:SD and Slc:SD strain rats were considerably low, and that of the F344/DuCrj strain was very low. Among six Wistar strains, Crj:Wistar, Slc:Wistar, WKY/Izm, WKAH/Hkm, Jcl:Wistar and Wistar-Imamichi, the Slc:Wistar strain rats showed exceptionally low 2-oxidation activity that was comparable to that of the F344/DuCrj strain. The rat strain differences in the catalytic activity of aldehyde oxidase could correlate in part with the expressed levels of protein based on the mRNA of aldehyde oxidase. However, no small discrepancy existed in the almost negligible catalytic activity and the fairly high expression levels of protein and mRNA in the F344/DuCrj and Slc:Wistar strain rats. Some genetic factors might possibly be one of reasons for the discrepancy.Aldehyde oxidase catalysed 2-oxidation activity of the (S)-enantiomer of RS-8359, a selective and reversible monoamine oxidase A (MAO-A) inhibitor, was investigated in liver cytosolic fractions from ten rat strains. Remarkably large strain differences were observed with approximately a 230 variation between the highest activity in the Wistar-Imamichi strain and the lowest activity in the Slc:Wistar strain. The activities of Crj:SD and Slc:SD strain rats were considerably low, and that of the F344/DuCrj strain was very low. Among six Wistar strains, Crj:Wistar, Slc:Wistar, WKY/Izm, WKAH/Hkm, Jcl:Wistar and Wistar-Imamichi, the Slc:Wistar strain rats showed exceptionally low 2-oxidation activity that was comparable to that of the F344/DuCrj strain. The rat strain differences in the catalytic activity of aldehyde oxidase could correlate in part with the expressed levels of protein based on the mRNA of aldehyde oxidase. However, no small discrepancy existed in the almost negligible catalytic activity and the fairly high expression levels of protein and mRNA in the F344/DuCrj and Slc:Wistar strain rats. Some genetic factors might possibly be one of reasons for the discrepancy. Aldehyde oxidase catalysed 2‐oxidation activity of the ( S )‐enantiomer of RS‐8359, a selective and reversible monoamine oxidase A (MAO‐A) inhibitor, was investigated in liver cytosolic fractions from ten rat strains. Remarkably large strain differences were observed with approximately a 230 variation between the highest activity in the Wistar‐Imamichi strain and the lowest activity in the Slc:Wistar strain. The activities of Crj:SD and Slc:SD strain rats were considerably low, and that of the F344/DuCrj strain was very low. Among six Wistar strains, Crj:Wistar, Slc:Wistar, WKY/Izm, WKAH/Hkm, Jcl:Wistar and Wistar‐Imamichi, the Slc:Wistar strain rats showed exceptionally low 2‐oxidation activity that was comparable to that of the F344/DuCrj strain. The rat strain differences in the catalytic activity of aldehyde oxidase could correlate in part with the expressed levels of protein based on the mRNA of aldehyde oxidase. However, no small discrepancy existed in the almost negligible catalytic activity and the fairly high expression levels of protein and mRNA in the F344/DuCrj and Slc:Wistar strain rats. Some genetic factors might possibly be one of reasons for the discrepancy. Copyright © 2006 John Wiley & Sons, Ltd.
Author	Sasaki, Takamitsu Watanabe, Nobuaki Tanaka, Yorihisa Masubuchi, Akiko Yamamura, Mayumi Itoh, Kunio Hiratsuka, Masahiro Mizugaki, Michinao
Author_xml	– sequence: 1 givenname: Takamitsu surname: Sasaki fullname: Sasaki, Takamitsu organization: Department of Biopharmaceutics, Tohoku Pharmaceutical University, Sendai, Japan – sequence: 2 givenname: Akiko surname: Masubuchi fullname: Masubuchi, Akiko organization: Department of Biopharmaceutics, Tohoku Pharmaceutical University, Sendai, Japan – sequence: 3 givenname: Mayumi surname: Yamamura fullname: Yamamura, Mayumi organization: Drug Metabolism and Pharmacokinetics Research Laboratories, Sankyo Co. Ltd., Tokyo, Japan – sequence: 4 givenname: Nobuaki surname: Watanabe fullname: Watanabe, Nobuaki organization: Drug Metabolism and Pharmacokinetics Research Laboratories, Sankyo Co. Ltd., Tokyo, Japan – sequence: 5 givenname: Masahiro surname: Hiratsuka fullname: Hiratsuka, Masahiro organization: Department of Clinical Pharmaceutics, Tohoku Pharmaceutical University, Sendai, Japan – sequence: 6 givenname: Michinao surname: Mizugaki fullname: Mizugaki, Michinao organization: Department of Clinical Pharmaceutics, Tohoku Pharmaceutical University, Sendai, Japan – sequence: 7 givenname: Kunio surname: Itoh fullname: Itoh, Kunio organization: Department of Biopharmaceutics, Tohoku Pharmaceutical University, Sendai, Japan – sequence: 8 givenname: Yorihisa surname: Tanaka fullname: Tanaka, Yorihisa email: ytanaka@tohoku-pharm.ac.jp organization: Department of Biopharmaceutics, Tohoku Pharmaceutical University, Sendai, Japan
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Cites_doi	10.1111/j.2042-7158.1995.tb03277.x 10.1016/0003-9861(71)90005-1 10.1016/S1532-0456(02)00057-1 10.1248/bpb.22.498 10.3109/00498259609062804 10.1538/expanim.48.43 10.1080/00498250500202106 10.1177/095632029200300101 10.1002/chir.20124 10.1016/S0006-2952(99)00323-8 10.1080/00498250110056531 10.3109/03602538508991432 10.1016/S0742-8413(00)00095-5 10.1016/S0090-9556(24)14921-5 10.1016/B978-0-12-380001-5.50020-7 10.1211/0022357991772619 10.1097/00004850-199709005-00004 10.1080/713803569 10.1097/00004850-199709005-00005 10.1111/j.2042-7158.1989.tb06324.x 10.1023/A:1008668913093 10.1254/jjp.55.121 10.1002/0470846305.ch5 10.1016/S0742-8413(98)10134-2 10.1007/BF01277023 10.1006/abbi.1995.1320 10.1002/bdd.494 10.1016/S0079-6468(08)70420-X 10.1007/BF03189919
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Keywords	Rat Enzyme Rodentia Strain specificity Metabolism MAO-A inhibitor Isomer Monoamine oxidase A inhibitor strain differences Stereoselectivity Vertebrata Mammalia Animal Aldehyde oxidase Oxidation Oxidoreductases Pharmacokinetics RS-8359
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Snippet	Aldehyde oxidase catalysed 2‐oxidation activity of the (S)‐enantiomer of RS‐8359, a selective and reversible monoamine oxidase A (MAO‐A) inhibitor, was... Aldehyde oxidase catalysed 2‐oxidation activity of the ( S )‐enantiomer of RS‐8359, a selective and reversible monoamine oxidase A (MAO‐A) inhibitor, was... Aldehyde oxidase catalysed 2-oxidation activity of the (S)-enantiomer of RS-8359, a selective and reversible monoamine oxidase A (MAO-A) inhibitor, was...
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SubjectTerms	aldehyde oxidase Aldehyde Oxidase - analysis Aldehyde Oxidase - genetics Aldehyde Oxidase - metabolism Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Blotting, Northern Catalysis Cytosol - enzymology Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Liver - enzymology Male MAO-A inhibitor Mice Monoamine Oxidase Inhibitors - metabolism Nitriles - metabolism Oxidation-Reduction Oxidoreductases Pyrimidines - metabolism rat Rats Rats, Inbred Strains RNA, Messenger - analysis RNA, Messenger - metabolism RS-8359 Stereoisomerism stereoselectivity strain differences
Title	Rat strain differences in stereospecific 2-oxidation of RS-8359, a reversible and selective MAO-A inhibitor, by aldehyde oxidase
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