Partial cloning of CYP2C23a genes and hepatic protein expression in eight representative avian species
Large interspecies differences in avian xenobiotic metabolism have been revealed by microsome‐based studies, but specific enzyme isoforms in different bird species have not yet been compared. We have previously shown that CYP2C23 genes are the most induced CYP isoforms in chicken liver. In this stud...
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Published in | Journal of veterinary pharmacology and therapeutics Vol. 38; no. 2; pp. 190 - 195 |
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Main Authors | , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
England
Blackwell Publishing Ltd
01.04.2015
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Subjects | |
Online Access | Get full text |
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Summary: | Large interspecies differences in avian xenobiotic metabolism have been revealed by microsome‐based studies, but specific enzyme isoforms in different bird species have not yet been compared. We have previously shown that CYP2C23 genes are the most induced CYP isoforms in chicken liver. In this study, we collected partial CYP2C23a gene sequences from eight avian species (ostrich, blue‐eared pheasant, snowy owl, great‐horned owl, Chilean flamingo, peregrin falcon, Humboldt penguin, and black‐crowned night heron) selected to cover the whole avian lineage: Paleognathae, Galloanserae, and Neoaves. Genetic analysis showed that CYP2C23 genes of Galloanserae species (chicken and blue‐eared pheasant) had unique characteristics. We found some duplicated genes (CYP2C23a and CYP2C23b) and two missing amino acid residues in Galloanserae compared to the other two lineages. The genes have lower homology than in other avian lineages, which suggests Galloanserae‐specific rapid evolutionary changes. These genetic features suggested that the Galloanserae are not the most representative avian species, considering that the Neoaves comprise more than 95% of birds. Moreover, we succeeded in synthesizing an antipeptide polyclonal antibody against the region of CYP2C23 protein conserved in avians. However, comparative quantitation of CYP2C23 proteins in livers from six species showed that expression levels of these proteins differed no more than fourfold. Further study is needed to clarify the function of avian CYP2C23 proteins. |
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Bibliography: | istex:3A95BE7FCCFD338F284C830C9A365DB1B565220D ark:/67375/WNG-KL3CX8GX-X Ministry of Education, Culture, Sports, Science, and Technology of Japan - No. 24248056; No. 24405004; No. 26304043 ArticleID:JVP12159 Japan Society for the Promotion of Science - No. 2300186400 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0140-7783 1365-2885 |
DOI: | 10.1111/jvp.12159 |