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Isolation and characterization of arylacetamide deacetylase in cynomolgus macaques

Arylacetamide deacetylase (AADAC), a microsomal serine esterase, hydrolyzes drugs, such as flutamide, phenacetin and rifampicin. Because AADAC has not been fully investigated at molecular levels in cynomolgus macaques, the non-human primate species widely used in drug metabolism studies, cynomolgus...

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Autores principales: UNO, Yasuhiro, HOSOKAWA, Masakiyo, IMAI, Teruko
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Japanese Society of Veterinary Science 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4488411/
https://www.ncbi.nlm.nih.gov/pubmed/25715734
http://dx.doi.org/10.1292/jvms.14-0496
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author UNO, Yasuhiro
HOSOKAWA, Masakiyo
IMAI, Teruko
author_facet UNO, Yasuhiro
HOSOKAWA, Masakiyo
IMAI, Teruko
author_sort UNO, Yasuhiro
collection PubMed
description Arylacetamide deacetylase (AADAC), a microsomal serine esterase, hydrolyzes drugs, such as flutamide, phenacetin and rifampicin. Because AADAC has not been fully investigated at molecular levels in cynomolgus macaques, the non-human primate species widely used in drug metabolism studies, cynomolgus AADAC cDNA was isolated and characterized. The deduced amino acid sequence, highly homologous (92%) to human AADAC, was more closely clustered with human AADAC than the dog, rat or mouse ortholog in a phylogenetic tree. AADAC was flanked by AADACL2 and SUCNR1 in the cynomolgus and human genomes. Moreover, relatively abundant expression of AADAC mRNA was found in liver and jejunum, the drug-metabolizing organs, in cynomolgus macaques, similar to humans. The results suggest molecular similarities of AADAC between cynomolgus macaques and humans.
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spelling pubmed-44884112015-07-06 Isolation and characterization of arylacetamide deacetylase in cynomolgus macaques UNO, Yasuhiro HOSOKAWA, Masakiyo IMAI, Teruko J Vet Med Sci Pharmacology Arylacetamide deacetylase (AADAC), a microsomal serine esterase, hydrolyzes drugs, such as flutamide, phenacetin and rifampicin. Because AADAC has not been fully investigated at molecular levels in cynomolgus macaques, the non-human primate species widely used in drug metabolism studies, cynomolgus AADAC cDNA was isolated and characterized. The deduced amino acid sequence, highly homologous (92%) to human AADAC, was more closely clustered with human AADAC than the dog, rat or mouse ortholog in a phylogenetic tree. AADAC was flanked by AADACL2 and SUCNR1 in the cynomolgus and human genomes. Moreover, relatively abundant expression of AADAC mRNA was found in liver and jejunum, the drug-metabolizing organs, in cynomolgus macaques, similar to humans. The results suggest molecular similarities of AADAC between cynomolgus macaques and humans. The Japanese Society of Veterinary Science 2015-02-07 2015-06 /pmc/articles/PMC4488411/ /pubmed/25715734 http://dx.doi.org/10.1292/jvms.14-0496 Text en ©2015 The Japanese Society of Veterinary Science http://creativecommons.org/licenses/by-nc-nd/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution Non-Commercial No Derivatives (by-nc-nd) License.
spellingShingle Pharmacology
UNO, Yasuhiro
HOSOKAWA, Masakiyo
IMAI, Teruko
Isolation and characterization of arylacetamide deacetylase in cynomolgus macaques
title Isolation and characterization of arylacetamide deacetylase in cynomolgus macaques
title_full Isolation and characterization of arylacetamide deacetylase in cynomolgus macaques
title_fullStr Isolation and characterization of arylacetamide deacetylase in cynomolgus macaques
title_full_unstemmed Isolation and characterization of arylacetamide deacetylase in cynomolgus macaques
title_short Isolation and characterization of arylacetamide deacetylase in cynomolgus macaques
title_sort isolation and characterization of arylacetamide deacetylase in cynomolgus macaques
topic Pharmacology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4488411/
https://www.ncbi.nlm.nih.gov/pubmed/25715734
http://dx.doi.org/10.1292/jvms.14-0496
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