Cloning and expression of a novelcatechol-O-methyltransferase in common marmosets
[摘要] Catechol-O-methyltransferase (COMT) catalyzes theO-methylation of endogenous catechol amines and estrogens and exogenouscatechol-type of drugs. A Parkinsonâs disease model of common marmoset (Callithrixjacchus) has been widely used in preclinical studies to evaluate inhibitorypotential of new drug candidates on marmoset COMT. Despite COMT inhibitors couldpotentiate the pharmacological action of levodopa on Parkinsonâs disease in animal models,marmoset COMT cDNA has not yet been identified and characterized. In this study, a cDNAhighly homologous to human COMT was cloned from marmoset livers. This cDNA encoded 268amino acids containing a transmembrane region and critical amino acid residues forcatalytic function. The amino acid sequences of marmoset COMT shared high sequenceidentity (90%) with human COMT. COMT mRNA was expressed in all five tissues tested,including brain, lung, liver, kidney and small intestine, and was more abundant inmarmoset liver and kidney. Membrane-bound COMT was immunochemically detected in livers andkidneys, whereas soluble COMT was detected in livers, similar to humans. These resultsindicated that the molecular characteristics of marmoset COMT were generally similar tothe human ortholog.
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[效力级别] [学科分类] 兽医学
[关键词] marmoset;membrane-bound COMT;soluble COMT [时效性]