First visualization of cholinergic cells and fibers by immunohistochemistry for choline acetyltransferase of the common type in the optic lobe and peduncle complex of Octopus vulgaris
Identifieur interne : 001334 ( Istex/Corpus ); précédent : 001333; suivant : 001335First visualization of cholinergic cells and fibers by immunohistochemistry for choline acetyltransferase of the common type in the optic lobe and peduncle complex of Octopus vulgaris
Auteurs : Loredana D'Este ; Shin Kimura ; Arianna Casini ; Akinori Matsuo ; Jean-Pierre Bellier ; Hiroshi Kimura ; Tindaro G. RendaSource :
- Journal of Comparative Neurology [ 0021-9967 ] ; 2008-08-20.
English descriptors
Abstract
This study provides the first immunohistochemical evidence visualizing cholinergic octopus neurons containing choline acetyltransferase (ChAT), the synthetic enzyme of acetylcholine. Because the antiserum applied here was raised against a recombinant protein encoded by exons 7 and 8 of the rat gene for ChAT, and initially used for studies in mammals, to validate antibody specificity for the octopus counterpart enzyme we therefore used three methods. Immunoprecipitation using Pansorbin indicated that immunoreactive octopus brain molecules were capable of synthesizing acetylcholine. Western blot analysis after denatured gel electrophoresis of octopus brain extracts revealed a single band at ≈81 kDa. A gel slice containing the 81‐kDa protein after native (nondenatured) gel electrophoresis exhibited high ChAT activity. All findings obtained with these three methods clearly indicated that the antiserum effectively recognizes octopus ChAT. The immunohistochemical use of the antiserum in the retina, optic lobe, and its neighboring peduncle complex detected enzyme‐containing neuronal cell bodies in only two regions, the cell islands of the optic lobe medulla and the cortical layer of the posterior olfactory lobule. Immunoreactive fibers and probable nerve terminals were also found in the plexiform layer of the deep retina, within the stroma of the optic gland, and the neuropils of the optic lobe, peduncle lobe, and olfactory lobe. These results provide information on the morphology and distribution patterns of cholinergic neurons in the octopus visual system, a useful invertebrate model for learning and memory where the cholinergic system, as in higher vertebrates including mammals, plays an important role. J. Comp. Neurol. 509:566–579, 2008. © 2008 Wiley‐Liss, Inc.
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DOI: 10.1002/cne.21761
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The immunohistochemical use of the antiserum in the retina, optic lobe, and its neighboring peduncle complex detected enzyme‐containing neuronal cell bodies in only two regions, the cell islands of the optic lobe medulla and the cortical layer of the posterior olfactory lobule. Immunoreactive fibers and probable nerve terminals were also found in the plexiform layer of the deep retina, within the stroma of the optic gland, and the neuropils of the optic lobe, peduncle lobe, and olfactory lobe. These results provide information on the morphology and distribution patterns of cholinergic neurons in the octopus visual system, a useful invertebrate model for learning and memory where the cholinergic system, as in higher vertebrates including mammals, plays an important role. J. Comp. 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Because the antiserum applied here was raised against a recombinant protein encoded by exons 7 and 8 of the rat gene for ChAT, and initially used for studies in mammals, to validate antibody specificity for the octopus counterpart enzyme we therefore used three methods. Immunoprecipitation using Pansorbin indicated that immunoreactive octopus brain molecules were capable of synthesizing acetylcholine. Western blot analysis after denatured gel electrophoresis of octopus brain extracts revealed a single band at ≈81 kDa. A gel slice containing the 81‐kDa protein after native (nondenatured) gel electrophoresis exhibited high ChAT activity. All findings obtained with these three methods clearly indicated that the antiserum effectively recognizes octopus ChAT. The immunohistochemical use of the antiserum in the retina, optic lobe, and its neighboring peduncle complex detected enzyme‐containing neuronal cell bodies in only two regions, the cell islands of the optic lobe medulla and the cortical layer of the posterior olfactory lobule. Immunoreactive fibers and probable nerve terminals were also found in the plexiform layer of the deep retina, within the stroma of the optic gland, and the neuropils of the optic lobe, peduncle lobe, and olfactory lobe. These results provide information on the morphology and distribution patterns of cholinergic neurons in the octopus visual system, a useful invertebrate model for learning and memory where the cholinergic system, as in higher vertebrates including mammals, plays an important role. J. Comp. 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No. MUR, 60% Ateneo 2004‐06, 1st Medical Faculty 2005‐06;</note><note>MEXT of Japan</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">First visualization of cholinergic cells and fibers by immunohistochemistry for choline acetyltransferase of the common type in the optic lobe and peduncle complex of Octopus vulgaris</title><author xml:id="author-1"><persName><forename type="first">Loredana</forename><surname>D'Este</surname></persName><affiliation>Department of Human Anatomy, Sapienza University of Rome, 00161 Rome, Italy</affiliation><affiliation>Research Center “Daniel Bovet,” Sapienza University of Rome, 00161 Rome, Italy</affiliation></author><author xml:id="author-2"><persName><forename type="first">Shin</forename><surname>Kimura</surname></persName><affiliation>Molecular Neuroscience Research Center, Shiga University of Medical Science, Otsu 520‐2192, Japan</affiliation></author><author xml:id="author-3"><persName><forename type="first">Arianna</forename><surname>Casini</surname></persName><affiliation>Department of Human Anatomy, Sapienza University of Rome, 00161 Rome, Italy</affiliation><affiliation>Research Center “Daniel Bovet,” Sapienza University of Rome, 00161 Rome, Italy</affiliation></author><author xml:id="author-4"><persName><forename type="first">Akinori</forename><surname>Matsuo</surname></persName><affiliation>Molecular Neuroscience Research Center, Shiga University of Medical Science, Otsu 520‐2192, Japan</affiliation></author><author xml:id="author-5"><persName><forename type="first">Jean‐Pierre</forename><surname>Bellier</surname></persName><affiliation>Molecular Neuroscience Research Center, Shiga University of Medical Science, Otsu 520‐2192, Japan</affiliation></author><author xml:id="author-6"><persName><forename type="first">Hiroshi</forename><surname>Kimura</surname></persName><affiliation>Molecular Neuroscience Research Center, Shiga University of Medical Science, Otsu 520‐2192, Japan</affiliation></author><author xml:id="author-7"><persName><forename type="first">Tindaro G.</forename><surname>Renda</surname></persName><affiliation>Department of Human Anatomy, Sapienza University of Rome, 00161 Rome, Italy</affiliation><affiliation>Research Center “Daniel Bovet,” Sapienza University of Rome, 00161 Rome, Italy</affiliation><affiliation>Department of Human Anatomy, Via Alfonso Borelli, 50–00161 Rome, Italy</affiliation></author></analytic><monogr><title level="j">Journal of Comparative Neurology</title><title level="j" type="abbrev">J. 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Because the antiserum applied here was raised against a recombinant protein encoded by exons 7 and 8 of the rat gene for ChAT, and initially used for studies in mammals, to validate antibody specificity for the octopus counterpart enzyme we therefore used three methods. Immunoprecipitation using Pansorbin indicated that immunoreactive octopus brain molecules were capable of synthesizing acetylcholine. Western blot analysis after denatured gel electrophoresis of octopus brain extracts revealed a single band at ≈81 kDa. A gel slice containing the 81‐kDa protein after native (nondenatured) gel electrophoresis exhibited high ChAT activity. All findings obtained with these three methods clearly indicated that the antiserum effectively recognizes octopus ChAT. The immunohistochemical use of the antiserum in the retina, optic lobe, and its neighboring peduncle complex detected enzyme‐containing neuronal cell bodies in only two regions, the cell islands of the optic lobe medulla and the cortical layer of the posterior olfactory lobule. Immunoreactive fibers and probable nerve terminals were also found in the plexiform layer of the deep retina, within the stroma of the optic gland, and the neuropils of the optic lobe, peduncle lobe, and olfactory lobe. These results provide information on the morphology and distribution patterns of cholinergic neurons in the octopus visual system, a useful invertebrate model for learning and memory where the cholinergic system, as in higher vertebrates including mammals, plays an important role. J. Comp. 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type="referenceTotal" number="88"></count><count type="wordTotal" number="11016"></count></countGroup><titleGroup><title type="main" xml:lang="en">First visualization of cholinergic cells and fibers by immunohistochemistry for choline acetyltransferase of the common type in the optic lobe and peduncle complex of <i>Octopus vulgaris</i></title><title type="short" xml:lang="en"><sc>C</sc>Chat in Octopus</title></titleGroup><creators><creator xml:id="au1" creatorRole="author" affiliationRef="#af1 #af2"><personName><givenNames>Loredana</givenNames><familyName>D'Este</familyName></personName></creator><creator xml:id="au2" creatorRole="author" affiliationRef="#af3"><personName><givenNames>Shin</givenNames><familyName>Kimura</familyName></personName></creator><creator xml:id="au3" creatorRole="author" affiliationRef="#af1 #af2"><personName><givenNames>Arianna</givenNames><familyName>Casini</familyName></personName></creator><creator xml:id="au4" creatorRole="author" affiliationRef="#af3"><personName><givenNames>Akinori</givenNames><familyName>Matsuo</familyName></personName></creator><creator xml:id="au5" creatorRole="author" affiliationRef="#af3"><personName><givenNames>Jean‐Pierre</givenNames><familyName>Bellier</familyName></personName></creator><creator xml:id="au6" creatorRole="author" affiliationRef="#af3"><personName><givenNames>Hiroshi</givenNames><familyName>Kimura</familyName></personName></creator><creator xml:id="au7" creatorRole="author" affiliationRef="#af1 #af2" corresponding="yes"><personName><givenNames>Tindaro G.</givenNames><familyName>Renda</familyName></personName><contactDetails><email>loredana.deste@uniroma1.it</email></contactDetails></creator></creators><affiliationGroup><affiliation xml:id="af1" countryCode="IT" type="organization"><unparsedAffiliation>Department of Human Anatomy, Sapienza University of Rome, 00161 Rome, Italy</unparsedAffiliation></affiliation><affiliation xml:id="af2" countryCode="IT" type="organization"><unparsedAffiliation>Research Center “Daniel Bovet,” Sapienza University of Rome, 00161 Rome, Italy</unparsedAffiliation></affiliation><affiliation xml:id="af3" countryCode="JP" type="organization"><unparsedAffiliation>Molecular Neuroscience Research Center, Shiga University of Medical Science, Otsu 520‐2192, Japan</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en" type="author"><keyword xml:id="kwd1">cephalopods</keyword><keyword xml:id="kwd2">invertebrates</keyword><keyword xml:id="kwd3">visual pathways</keyword><keyword xml:id="kwd4">cChAT</keyword><keyword xml:id="kwd5">acetylcholine</keyword><keyword xml:id="kwd6">immunohistochemistry</keyword></keywordGroup><fundingInfo><fundingAgency>Italian Ministry for the University and Sapienza University of Rome</fundingAgency><fundingNumber>MUR, 60% Ateneo 2004‐06, 1st Medical Faculty 2005‐06</fundingNumber></fundingInfo><fundingInfo><fundingAgency>MEXT of Japan</fundingAgency></fundingInfo><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>This study provides the first immunohistochemical evidence visualizing cholinergic octopus neurons containing choline acetyltransferase (ChAT), the synthetic enzyme of acetylcholine. Because the antiserum applied here was raised against a recombinant protein encoded by exons 7 and 8 of the rat gene for ChAT, and initially used for studies in mammals, to validate antibody specificity for the octopus counterpart enzyme we therefore used three methods. Immunoprecipitation using Pansorbin indicated that immunoreactive octopus brain molecules were capable of synthesizing acetylcholine. Western blot analysis after denatured gel electrophoresis of octopus brain extracts revealed a single band at ≈81 kDa. A gel slice containing the 81‐kDa protein after native (nondenatured) gel electrophoresis exhibited high ChAT activity. All findings obtained with these three methods clearly indicated that the antiserum effectively recognizes octopus ChAT. The immunohistochemical use of the antiserum in the retina, optic lobe, and its neighboring peduncle complex detected enzyme‐containing neuronal cell bodies in only two regions, the cell islands of the optic lobe medulla and the cortical layer of the posterior olfactory lobule. Immunoreactive fibers and probable nerve terminals were also found in the plexiform layer of the deep retina, within the stroma of the optic gland, and the neuropils of the optic lobe, peduncle lobe, and olfactory lobe. These results provide information on the morphology and distribution patterns of cholinergic neurons in the octopus visual system, a useful invertebrate model for learning and memory where the cholinergic system, as in higher vertebrates including mammals, plays an important role. J. Comp. Neurol. 509:566–579, 2008. © 2008 Wiley‐Liss, Inc.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>First visualization of cholinergic cells and fibers by immunohistochemistry for choline acetyltransferase of the common type in the optic lobe and peduncle complex of Octopus vulgaris</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>CChat in Octopus</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>First visualization of cholinergic cells and fibers by immunohistochemistry for choline acetyltransferase of the common type in the optic lobe and peduncle complex of Octopus vulgaris</title></titleInfo><name type="personal"><namePart type="given">Loredana</namePart><namePart type="family">D'Este</namePart><affiliation>Department of Human Anatomy, Sapienza University of Rome, 00161 Rome, Italy</affiliation><affiliation>Research Center “Daniel Bovet,” Sapienza University of Rome, 00161 Rome, Italy</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Shin</namePart><namePart type="family">Kimura</namePart><affiliation>Molecular Neuroscience Research Center, Shiga University of Medical Science, Otsu 520‐2192, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Arianna</namePart><namePart type="family">Casini</namePart><affiliation>Department of Human Anatomy, Sapienza University of Rome, 00161 Rome, Italy</affiliation><affiliation>Research Center “Daniel Bovet,” Sapienza University of Rome, 00161 Rome, Italy</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Akinori</namePart><namePart type="family">Matsuo</namePart><affiliation>Molecular Neuroscience Research Center, Shiga University of Medical Science, Otsu 520‐2192, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jean‐Pierre</namePart><namePart type="family">Bellier</namePart><affiliation>Molecular Neuroscience Research Center, Shiga University of Medical Science, Otsu 520‐2192, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Hiroshi</namePart><namePart type="family">Kimura</namePart><affiliation>Molecular Neuroscience Research Center, Shiga University of Medical Science, Otsu 520‐2192, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Tindaro G.</namePart><namePart type="family">Renda</namePart><affiliation>Department of Human Anatomy, Sapienza University of Rome, 00161 Rome, Italy</affiliation><affiliation>Research Center “Daniel Bovet,” Sapienza University of Rome, 00161 Rome, Italy</affiliation><affiliation>Department of Human Anatomy, Via Alfonso Borelli, 50–00161 Rome, Italy</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article"></genre><originInfo><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><place><placeTerm type="text">Hoboken</placeTerm></place><dateIssued encoding="w3cdtf">2008-08-20</dateIssued><dateCaptured encoding="w3cdtf">2007-12-07</dateCaptured><dateValid encoding="w3cdtf">2008-04-21</dateValid><copyrightDate encoding="w3cdtf">2008</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType><extent unit="figures">6</extent><extent unit="references">88</extent><extent unit="words">11016</extent></physicalDescription><abstract lang="en">This study provides the first immunohistochemical evidence visualizing cholinergic octopus neurons containing choline acetyltransferase (ChAT), the synthetic enzyme of acetylcholine. Because the antiserum applied here was raised against a recombinant protein encoded by exons 7 and 8 of the rat gene for ChAT, and initially used for studies in mammals, to validate antibody specificity for the octopus counterpart enzyme we therefore used three methods. Immunoprecipitation using Pansorbin indicated that immunoreactive octopus brain molecules were capable of synthesizing acetylcholine. Western blot analysis after denatured gel electrophoresis of octopus brain extracts revealed a single band at ≈81 kDa. A gel slice containing the 81‐kDa protein after native (nondenatured) gel electrophoresis exhibited high ChAT activity. All findings obtained with these three methods clearly indicated that the antiserum effectively recognizes octopus ChAT. The immunohistochemical use of the antiserum in the retina, optic lobe, and its neighboring peduncle complex detected enzyme‐containing neuronal cell bodies in only two regions, the cell islands of the optic lobe medulla and the cortical layer of the posterior olfactory lobule. Immunoreactive fibers and probable nerve terminals were also found in the plexiform layer of the deep retina, within the stroma of the optic gland, and the neuropils of the optic lobe, peduncle lobe, and olfactory lobe. These results provide information on the morphology and distribution patterns of cholinergic neurons in the octopus visual system, a useful invertebrate model for learning and memory where the cholinergic system, as in higher vertebrates including mammals, plays an important role. J. Comp. Neurol. 509:566–579, 2008. © 2008 Wiley‐Liss, Inc.</abstract><note type="funding">Italian Ministry for the University and Sapienza University of Rome - No. MUR, 60% Ateneo 2004‐06, 1st Medical Faculty 2005‐06; </note><note type="funding">MEXT of Japan</note><subject lang="en"><genre>keywords</genre><topic>cephalopods</topic><topic>invertebrates</topic><topic>visual pathways</topic><topic>cChAT</topic><topic>acetylcholine</topic><topic>immunohistochemistry</topic></subject><relatedItem type="host"><titleInfo><title>Journal of Comparative Neurology</title></titleInfo><titleInfo type="abbreviated"><title>J. Comp. Neurol.</title></titleInfo><genre type="journal">journal</genre><subject><genre>article-category</genre><topic>Article</topic></subject><identifier type="ISSN">0021-9967</identifier><identifier type="eISSN">1096-9861</identifier><identifier type="DOI">10.1002/(ISSN)1096-9861</identifier><identifier type="PublisherID">CNE</identifier><part><date>2008</date><detail type="volume"><caption>vol.</caption><number>509</number></detail><detail type="issue"><caption>no.</caption><number>6</number></detail><extent unit="pages"><start>566</start><end>579</end><total>14</total></extent></part></relatedItem><identifier type="istex">7BE795D76885EA502811AA3BFF78788B80ED2D52</identifier><identifier type="DOI">10.1002/cne.21761</identifier><identifier type="ArticleID">CNE21761</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 2008 Wiley‐Liss, Inc.</accessCondition><recordInfo><recordContentSource>WILEY</recordContentSource><recordOrigin>Wiley Subscription Services, Inc., A Wiley Company</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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