Molecular characterization and tissue distribution of cysteamine dioxygenase (ADO) in common carp Cyprinus carpio

The low production of hypotaurine from cysteine but a significantly high taurine deposition in common carp led to the hypothesis that this species utilizes an alternative pathway other than the cysteine sulfinic acid pathway. Cysteamine pathway is common in mammals but not in other animals such as birds, invertebrates, and fishes. The cloned cysteamine dioxygenase (ADO) cDNA in common carp consists of 790 nucleotide bases with 260 deduced amino acid sequence. The conserved domain is the DUF1637 which has a conserved tyrosine and cysteine residues and the presence of three predicted N-glycosylation sites. Phylogenetic analysis using neighbor joint method indicated that ADO in common carp branched after Sinocyclocheilus rhinocerous. ADO was expressed in hepatopancreas, brain, gill, intestine, and muscle of common carp. The hepatopacreas had a significantly higher gene expression level than the other organs examined. The present results suggest that ADO is present in common carp.

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Main Authors: Gonzales-Plasus, Maria Mojena G, Haga, Yutaka, Kondo, Hidehiro, Hirono, Ikuo, Satoh, Shuichi
Format: Journal Contribution biblioteca
Language:English
Published: 2019-07-01
Subjects:ASFA_2015::M::Molecular structure, ASFA_2015::E::Enzyme activity,
Online Access:http://hdl.handle.net/1834/17938
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spelling dig-aquadocs-1834-179382021-05-19T07:02:01Z Molecular characterization and tissue distribution of cysteamine dioxygenase (ADO) in common carp Cyprinus carpio Gonzales-Plasus, Maria Mojena G Haga, Yutaka Kondo, Hidehiro Hirono, Ikuo Satoh, Shuichi ASFA_2015::M::Molecular structure ASFA_2015::E::Enzyme activity The low production of hypotaurine from cysteine but a significantly high taurine deposition in common carp led to the hypothesis that this species utilizes an alternative pathway other than the cysteine sulfinic acid pathway. Cysteamine pathway is common in mammals but not in other animals such as birds, invertebrates, and fishes. The cloned cysteamine dioxygenase (ADO) cDNA in common carp consists of 790 nucleotide bases with 260 deduced amino acid sequence. The conserved domain is the DUF1637 which has a conserved tyrosine and cysteine residues and the presence of three predicted N-glycosylation sites. Phylogenetic analysis using neighbor joint method indicated that ADO in common carp branched after Sinocyclocheilus rhinocerous. ADO was expressed in hepatopancreas, brain, gill, intestine, and muscle of common carp. The hepatopacreas had a significantly higher gene expression level than the other organs examined. The present results suggest that ADO is present in common carp. Published Refereed 2021-04-21T10:01:50Z 2021-04-21T10:01:50Z 2019-07-01 Journal Contribution http://hdl.handle.net/1834/17938 en http://www.palawanscientist.org/research_journals/thepalawanscientist_vol11_2019/2a%20Plasus.pdf 17-28 Japan
institution UNESCO
collection DSpace
country Francia
countrycode FR
component Bibliográfico
access En linea
databasecode dig-aquadocs
tag biblioteca
region Europa del Oeste
libraryname Repositorio AQUADOCS
language English
topic ASFA_2015::M::Molecular structure
ASFA_2015::E::Enzyme activity
ASFA_2015::M::Molecular structure
ASFA_2015::E::Enzyme activity
spellingShingle ASFA_2015::M::Molecular structure
ASFA_2015::E::Enzyme activity
ASFA_2015::M::Molecular structure
ASFA_2015::E::Enzyme activity
Gonzales-Plasus, Maria Mojena G
Haga, Yutaka
Kondo, Hidehiro
Hirono, Ikuo
Satoh, Shuichi
Molecular characterization and tissue distribution of cysteamine dioxygenase (ADO) in common carp Cyprinus carpio
description The low production of hypotaurine from cysteine but a significantly high taurine deposition in common carp led to the hypothesis that this species utilizes an alternative pathway other than the cysteine sulfinic acid pathway. Cysteamine pathway is common in mammals but not in other animals such as birds, invertebrates, and fishes. The cloned cysteamine dioxygenase (ADO) cDNA in common carp consists of 790 nucleotide bases with 260 deduced amino acid sequence. The conserved domain is the DUF1637 which has a conserved tyrosine and cysteine residues and the presence of three predicted N-glycosylation sites. Phylogenetic analysis using neighbor joint method indicated that ADO in common carp branched after Sinocyclocheilus rhinocerous. ADO was expressed in hepatopancreas, brain, gill, intestine, and muscle of common carp. The hepatopacreas had a significantly higher gene expression level than the other organs examined. The present results suggest that ADO is present in common carp.
format Journal Contribution
topic_facet ASFA_2015::M::Molecular structure
ASFA_2015::E::Enzyme activity
author Gonzales-Plasus, Maria Mojena G
Haga, Yutaka
Kondo, Hidehiro
Hirono, Ikuo
Satoh, Shuichi
author_facet Gonzales-Plasus, Maria Mojena G
Haga, Yutaka
Kondo, Hidehiro
Hirono, Ikuo
Satoh, Shuichi
author_sort Gonzales-Plasus, Maria Mojena G
title Molecular characterization and tissue distribution of cysteamine dioxygenase (ADO) in common carp Cyprinus carpio
title_short Molecular characterization and tissue distribution of cysteamine dioxygenase (ADO) in common carp Cyprinus carpio
title_full Molecular characterization and tissue distribution of cysteamine dioxygenase (ADO) in common carp Cyprinus carpio
title_fullStr Molecular characterization and tissue distribution of cysteamine dioxygenase (ADO) in common carp Cyprinus carpio
title_full_unstemmed Molecular characterization and tissue distribution of cysteamine dioxygenase (ADO) in common carp Cyprinus carpio
title_sort molecular characterization and tissue distribution of cysteamine dioxygenase (ado) in common carp cyprinus carpio
publishDate 2019-07-01
url http://hdl.handle.net/1834/17938
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