Rat strain differences in stereospecific 2-oxidation of RS-8359, a reversible and selective MAO-A inhibitor, by aldehyde oxidase.
作者： Takamitsu Sasaki , Akiko Masubuchi , Mayumi Yamamura , Nobuaki Watanabe , Masahiro Hiratsuka
DOI: 10.1002/BDD.504
关键词:
摘要: Aldehyde oxidase catalysed 2-oxidation activity of the (S)-enantiomer RS-8359, a selective and reversible monoamine A (MAO-A) inhibitor, was investigated in liver cytosolic fractions from ten rat strains. Remarkably large strain differences were observed with approximately 230 variation between highest Wistar-Imamichi lowest Slc:Wistar strain. The activities Crj:SD Slc:SD rats considerably low, that F344/DuCrj very low. Among six Wistar strains, Crj:Wistar, Slc:Wistar, WKY/Izm, WKAH/Hkm, Jcl:Wistar Wistar-Imamichi, showed exceptionally low comparable to catalytic aldehyde could correlate part expressed levels protein based on mRNA oxidase. However, no small discrepancy existed almost negligible fairly high expression rats. Some genetic factors might possibly be one reasons for discrepancy.
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