Identification of proteins that bind to the neuroprotective agent neoechinulin A.
Identifieur interne : 000250 ( Main/Exploration ); précédent : 000249; suivant : 000251Identification of proteins that bind to the neuroprotective agent neoechinulin A.
Auteurs : Shinji Kamisuki [Japon] ; Natsumi Himeno [Japon] ; Yukine Tsurukawa [Japon] ; Tomoe Kusayanagi [Japon] ; Masahiro Takeno [Japon] ; Takashi Kamakura [Japon] ; Kouji Kuramochi [Japon] ; Fumio Sugawara [Japon]Source :
- Bioscience, biotechnology, and biochemistry [ 1347-6947 ] ; 2018.
Descripteurs français
- KwdFr :
- Alcaloïdes indoliques (métabolisme), Alcaloïdes indoliques (pharmacologie), Animaux (MeSH), Banque de peptides (MeSH), Cellules PC12 (MeSH), Chromogranine B (déficit), Chromogranine B (génétique), Chromogranine B (métabolisme), Extinction de l'expression des gènes (MeSH), Glutarédoxines (déficit), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Liaison aux protéines (MeSH), Neuroprotecteurs (métabolisme), Neuroprotecteurs (pharmacologie), Pipérazines (métabolisme), Pipérazines (pharmacologie), Rats (MeSH).
- MESH :
- déficit : Chromogranine B, Glutarédoxines.
- génétique : Chromogranine B, Glutarédoxines.
- métabolisme : Alcaloïdes indoliques, Chromogranine B, Glutarédoxines, Neuroprotecteurs, Pipérazines.
- pharmacologie : Alcaloïdes indoliques, Neuroprotecteurs, Pipérazines.
- Animaux, Banque de peptides, Cellules PC12, Extinction de l'expression des gènes, Liaison aux protéines, Rats.
English descriptors
- KwdEn :
- Animals (MeSH), Chromogranin B (deficiency), Chromogranin B (genetics), Chromogranin B (metabolism), Gene Silencing (MeSH), Glutaredoxins (deficiency), Glutaredoxins (genetics), Glutaredoxins (metabolism), Indole Alkaloids (metabolism), Indole Alkaloids (pharmacology), Neuroprotective Agents (metabolism), Neuroprotective Agents (pharmacology), PC12 Cells (MeSH), Peptide Library (MeSH), Piperazines (metabolism), Piperazines (pharmacology), Protein Binding (MeSH), Rats (MeSH).
- MESH :
- chemical , deficiency : Chromogranin B, Glutaredoxins.
- chemical , genetics : Chromogranin B, Glutaredoxins.
- chemical , metabolism : Chromogranin B, Glutaredoxins, Indole Alkaloids, Neuroprotective Agents, Piperazines.
- chemical , pharmacology : Indole Alkaloids, Neuroprotective Agents, Piperazines.
- Animals, Gene Silencing, PC12 Cells, Peptide Library, Protein Binding, Rats.
Abstract
Neoechinulin A is an indole alkaloid with several biological activities. We previously reported that this compound protects neuronal PC12 cells from cytotoxicity induced by the peroxynitrite generator 3-morpholinosydnonimine (SIN-1), but the target proteins and precise mechanism of action of neoechinulin A were unclear. Here, we employed a phage display screen to identify proteins that bind directly with neoechinulin A. Our findings identified two proteins, chromogranin B and glutaredoxin 3, as candidate target binding partners for the alkaloid. QCM analyses revealed that neoechinulin A displays high affinity for both chromogranin B and glutaredoxin 3. RNA interference-mediated depletion of chromogranin B decreased the sensitivity of PC12 cells against SIN-1. Our results suggested chromogranin B is a plausible target of neoechinulin A.
DOI: 10.1080/09168451.2018.1433018
PubMed: 29447077
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<author><name sortKey="Sugawara, Fumio" sort="Sugawara, Fumio" uniqKey="Sugawara F" first="Fumio" last="Sugawara">Fumio Sugawara</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term>
<term>Chromogranin B (deficiency)</term>
<term>Chromogranin B (genetics)</term>
<term>Chromogranin B (metabolism)</term>
<term>Gene Silencing (MeSH)</term>
<term>Glutaredoxins (deficiency)</term>
<term>Glutaredoxins (genetics)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Indole Alkaloids (metabolism)</term>
<term>Indole Alkaloids (pharmacology)</term>
<term>Neuroprotective Agents (metabolism)</term>
<term>Neuroprotective Agents (pharmacology)</term>
<term>PC12 Cells (MeSH)</term>
<term>Peptide Library (MeSH)</term>
<term>Piperazines (metabolism)</term>
<term>Piperazines (pharmacology)</term>
<term>Protein Binding (MeSH)</term>
<term>Rats (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Alcaloïdes indoliques (métabolisme)</term>
<term>Alcaloïdes indoliques (pharmacologie)</term>
<term>Animaux (MeSH)</term>
<term>Banque de peptides (MeSH)</term>
<term>Cellules PC12 (MeSH)</term>
<term>Chromogranine B (déficit)</term>
<term>Chromogranine B (génétique)</term>
<term>Chromogranine B (métabolisme)</term>
<term>Extinction de l'expression des gènes (MeSH)</term>
<term>Glutarédoxines (déficit)</term>
<term>Glutarédoxines (génétique)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Neuroprotecteurs (métabolisme)</term>
<term>Neuroprotecteurs (pharmacologie)</term>
<term>Pipérazines (métabolisme)</term>
<term>Pipérazines (pharmacologie)</term>
<term>Rats (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="deficiency" xml:lang="en"><term>Chromogranin B</term>
<term>Glutaredoxins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Chromogranin B</term>
<term>Glutaredoxins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Chromogranin B</term>
<term>Glutaredoxins</term>
<term>Indole Alkaloids</term>
<term>Neuroprotective Agents</term>
<term>Piperazines</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Indole Alkaloids</term>
<term>Neuroprotective Agents</term>
<term>Piperazines</term>
</keywords>
<keywords scheme="MESH" qualifier="déficit" xml:lang="fr"><term>Chromogranine B</term>
<term>Glutarédoxines</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Chromogranine B</term>
<term>Glutarédoxines</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Alcaloïdes indoliques</term>
<term>Chromogranine B</term>
<term>Glutarédoxines</term>
<term>Neuroprotecteurs</term>
<term>Pipérazines</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Alcaloïdes indoliques</term>
<term>Neuroprotecteurs</term>
<term>Pipérazines</term>
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<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Gene Silencing</term>
<term>PC12 Cells</term>
<term>Peptide Library</term>
<term>Protein Binding</term>
<term>Rats</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Banque de peptides</term>
<term>Cellules PC12</term>
<term>Extinction de l'expression des gènes</term>
<term>Liaison aux protéines</term>
<term>Rats</term>
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<front><div type="abstract" xml:lang="en">Neoechinulin A is an indole alkaloid with several biological activities. We previously reported that this compound protects neuronal PC12 cells from cytotoxicity induced by the peroxynitrite generator 3-morpholinosydnonimine (SIN-1), but the target proteins and precise mechanism of action of neoechinulin A were unclear. Here, we employed a phage display screen to identify proteins that bind directly with neoechinulin A. Our findings identified two proteins, chromogranin B and glutaredoxin 3, as candidate target binding partners for the alkaloid. QCM analyses revealed that neoechinulin A displays high affinity for both chromogranin B and glutaredoxin 3. RNA interference-mediated depletion of chromogranin B decreased the sensitivity of PC12 cells against SIN-1. Our results suggested chromogranin B is a plausible target of neoechinulin A.</div>
</front>
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<DateCompleted><Year>2018</Year>
<Month>07</Month>
<Day>12</Day>
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<DateRevised><Year>2018</Year>
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<Title>Bioscience, biotechnology, and biochemistry</Title>
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<ArticleTitle>Identification of proteins that bind to the neuroprotective agent neoechinulin A.</ArticleTitle>
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<Abstract><AbstractText>Neoechinulin A is an indole alkaloid with several biological activities. We previously reported that this compound protects neuronal PC12 cells from cytotoxicity induced by the peroxynitrite generator 3-morpholinosydnonimine (SIN-1), but the target proteins and precise mechanism of action of neoechinulin A were unclear. Here, we employed a phage display screen to identify proteins that bind directly with neoechinulin A. Our findings identified two proteins, chromogranin B and glutaredoxin 3, as candidate target binding partners for the alkaloid. QCM analyses revealed that neoechinulin A displays high affinity for both chromogranin B and glutaredoxin 3. RNA interference-mediated depletion of chromogranin B decreased the sensitivity of PC12 cells against SIN-1. Our results suggested chromogranin B is a plausible target of neoechinulin A.</AbstractText>
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<ForeName>Shinji</ForeName>
<Initials>S</Initials>
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<ForeName>Natsumi</ForeName>
<Initials>N</Initials>
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</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Tsurukawa</LastName>
<ForeName>Yukine</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>a School of Veterinary Medicine , Azabu University , Kanagawa , Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Kusayanagi</LastName>
<ForeName>Tomoe</ForeName>
<Initials>T</Initials>
<AffiliationInfo><Affiliation>b Department of Applied Biological Science , Tokyo University of Science , Chiba , Japan.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Takeno</LastName>
<ForeName>Masahiro</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>b Department of Applied Biological Science , Tokyo University of Science , Chiba , Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Kamakura</LastName>
<ForeName>Takashi</ForeName>
<Initials>T</Initials>
<AffiliationInfo><Affiliation>b Department of Applied Biological Science , Tokyo University of Science , Chiba , Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Kuramochi</LastName>
<ForeName>Kouji</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>b Department of Applied Biological Science , Tokyo University of Science , Chiba , Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Sugawara</LastName>
<ForeName>Fumio</ForeName>
<Initials>F</Initials>
<AffiliationInfo><Affiliation>b Department of Applied Biological Science , Tokyo University of Science , Chiba , Japan.</Affiliation>
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<Month>02</Month>
<Day>15</Day>
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<MedlineJournalInfo><Country>England</Country>
<MedlineTA>Biosci Biotechnol Biochem</MedlineTA>
<NlmUniqueID>9205717</NlmUniqueID>
<ISSNLinking>0916-8451</ISSNLinking>
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<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D053378">Chromogranin B</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance>
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<NameOfSubstance UI="D026121">Indole Alkaloids</NameOfSubstance>
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<NameOfSubstance UI="D010879">Piperazines</NameOfSubstance>
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<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C490266">neoechinulin A</NameOfSubstance>
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<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D053378" MajorTopicYN="N">Chromogranin B</DescriptorName>
<QualifierName UI="Q000172" MajorTopicYN="N">deficiency</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020868" MajorTopicYN="N">Gene Silencing</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName>
<QualifierName UI="Q000172" MajorTopicYN="N">deficiency</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
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<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
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<MeshHeading><DescriptorName UI="D018696" MajorTopicYN="N">Neuroprotective Agents</DescriptorName>
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<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016716" MajorTopicYN="N">PC12 Cells</DescriptorName>
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<MeshHeading><DescriptorName UI="D019151" MajorTopicYN="Y">Peptide Library</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010879" MajorTopicYN="N">Piperazines</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D051381" MajorTopicYN="N">Rats</DescriptorName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Neuroprotective agent</Keyword>
<Keyword MajorTopicYN="N">phage display</Keyword>
<Keyword MajorTopicYN="N">reactive nitrogen species</Keyword>
<Keyword MajorTopicYN="N">target identification</Keyword>
</KeywordList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2018</Year>
<Month>2</Month>
<Day>16</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2018</Year>
<Month>7</Month>
<Day>13</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2018</Year>
<Month>2</Month>
<Day>16</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">29447077</ArticleId>
<ArticleId IdType="doi">10.1080/09168451.2018.1433018</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>Japon</li>
</country>
</list>
<tree><country name="Japon"><noRegion><name sortKey="Kamisuki, Shinji" sort="Kamisuki, Shinji" uniqKey="Kamisuki S" first="Shinji" last="Kamisuki">Shinji Kamisuki</name>
</noRegion>
<name sortKey="Himeno, Natsumi" sort="Himeno, Natsumi" uniqKey="Himeno N" first="Natsumi" last="Himeno">Natsumi Himeno</name>
<name sortKey="Kamakura, Takashi" sort="Kamakura, Takashi" uniqKey="Kamakura T" first="Takashi" last="Kamakura">Takashi Kamakura</name>
<name sortKey="Kuramochi, Kouji" sort="Kuramochi, Kouji" uniqKey="Kuramochi K" first="Kouji" last="Kuramochi">Kouji Kuramochi</name>
<name sortKey="Kusayanagi, Tomoe" sort="Kusayanagi, Tomoe" uniqKey="Kusayanagi T" first="Tomoe" last="Kusayanagi">Tomoe Kusayanagi</name>
<name sortKey="Sugawara, Fumio" sort="Sugawara, Fumio" uniqKey="Sugawara F" first="Fumio" last="Sugawara">Fumio Sugawara</name>
<name sortKey="Takeno, Masahiro" sort="Takeno, Masahiro" uniqKey="Takeno M" first="Masahiro" last="Takeno">Masahiro Takeno</name>
<name sortKey="Tsurukawa, Yukine" sort="Tsurukawa, Yukine" uniqKey="Tsurukawa Y" first="Yukine" last="Tsurukawa">Yukine Tsurukawa</name>
</country>
</tree>
</affiliations>
</record>
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