Cloning and expression of a novel catechol-O-methyltransferase in common marmosets.

作者: Shotaro UEHARA , Yasuhiro UNO , Takashi INOUE , Erika SASAKI , Hiroshi YAMAZAKI

DOI: 10.1292/JVMS.16-0459

关键词:

摘要: Catechol-O-methyltransferase (COMT) catalyzes the O-methylation of endogenous catechol amines and estrogens exogenous catechol-type drugs. A Parkinson's disease model common marmoset (Callithrix jacchus) has been widely used in preclinical studies to evaluate inhibitory potential new drug candidates on COMT. Despite COMT inhibitors could potentiate pharmacological action levodopa animal models, cDNA not yet identified characterized. In this study, a highly homologous human was cloned from livers. This encoded 268 amino acids containing transmembrane region critical acid residues for catalytic function. The sequences shared high sequence identity (90%) with mRNA expressed all five tissues tested, including brain, lung, liver, kidney small intestine, more abundant liver kidney. Membrane-bound immunochemically detected livers kidneys, whereas soluble livers, similar humans. These results indicated that molecular characteristics were generally ortholog.

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