De novo synthesis of GAP-43: in situ hybridization histochemistry and light and electron microscopy immunocytochemical studies in regenerating motor neurons of cranial nerve nuclei in the rat brain
Identifieur interne : 001D19 ( Istex/Corpus ); précédent : 001D18; suivant : 001D20De novo synthesis of GAP-43: in situ hybridization histochemistry and light and electron microscopy immunocytochemical studies in regenerating motor neurons of cranial nerve nuclei in the rat brain
Auteurs : G. Palacios ; G. Mengod ; M. Sarasa ; J. Baudier ; J. M. PalaciosSource :
- Molecular Brain Research [ 0169-328X ] ; 1994.
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Abstract
Abstract: In order to investigate the modulation of the synthesis and the subcellular localization of the growth associated protein GAP-43 in neuronal cell bodies we have taken advantage of the well known regenerative properties of axotomized motor neurons of the facial and hypoglossal nuclei. Alterations in the levels of GAP-43 mRNA containing cells were studied by in situ hybridization histochemistry. The protein localization was examined using immunohistochemistry at the light and electron microscopic levels. Neurons from the control side showed undetectable levels of both GAP-43-like immunoreactivity and GAP-43 mRNA levels. Whereas axotomized neurons exhibited a marked increase in GAP-43 mRNA levels and in GAP-43-like immunoreactivity. Three to 50 days after axotomy, motor neurons ipsilateral to the lesion displayed a dense reticular or filamentous perinuclear distribution of the immunoreactivity in somata and proximal dendritic processes, corresponding to the location of the Golgi apparatus in these neurons. At the electron microscopic level the immunoreactivity was located in the cisternae of the Golgi complex and found to be associated with trans-side vesicles of these complexes. The myelinated fibers of the transectomized facial nerve also presented an intense GAP-43-like immunoreactivity. Twenty-one days after the axotomy a decay in the number of immunostained neurons and in the intensity of immunolabeled somata was observed. Our study reveals a rapid induction of GAP-43 mRNA and protein after axotomy. The localization of the newly synthesized GAP-43-like immunoreactivity to the Golgi apparatus seen in the present work suggests an early association of this protein with newly formed membranes prior to transport toward the terminals through the axons.
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DOI: 10.1016/0169-328X(94)90122-8
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<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">De novo synthesis of GAP-43: in situ hybridization histochemistry and light and electron microscopy immunocytochemical studies in regenerating motor neurons of cranial nerve nuclei in the rat brain</title><author><name sortKey="Palacios, G" sort="Palacios, G" uniqKey="Palacios G" first="G." last="Palacios">G. Palacios</name><affiliation><mods:affiliation>Department of Cellular Biology and Physiology, Subunit of Histology, Faculty of Medicine, Uniuersidad Auto´noma de Barcelona, Bellaterra, Barcelona 08193, Spain</mods:affiliation></affiliation></author><author><name sortKey="Mengod, G" sort="Mengod, G" uniqKey="Mengod G" first="G." last="Mengod">G. Mengod</name><affiliation><mods:affiliation>Department of Neurochemistry, CID-CSIC, Barcelona, Spain</mods:affiliation></affiliation></author><author><name sortKey="Sarasa, M" sort="Sarasa, M" uniqKey="Sarasa M" first="M." last="Sarasa">M. Sarasa</name><affiliation><mods:affiliation>Department of Anatomy, Embryology and Genetics, Veterinary Faculty, University of Zaragoza, Zaragoza, Spain</mods:affiliation></affiliation></author><author><name sortKey="Baudier, J" sort="Baudier, J" uniqKey="Baudier J" first="J." last="Baudier">J. Baudier</name><affiliation><mods:affiliation>Laboratoire de Biologie Moleculaire, Cycle Cellulaire, INSERM U309, 38041 Grenoble, France</mods:affiliation></affiliation></author><author><name sortKey="Palacios, J M" sort="Palacios, J M" uniqKey="Palacios J" first="J. M." last="Palacios">J. M. 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Palacios</name><affiliation><mods:affiliation>Department of Cellular Biology and Physiology, Subunit of Histology, Faculty of Medicine, Uniuersidad Auto´noma de Barcelona, Bellaterra, Barcelona 08193, Spain</mods:affiliation></affiliation></author><author><name sortKey="Mengod, G" sort="Mengod, G" uniqKey="Mengod G" first="G." last="Mengod">G. Mengod</name><affiliation><mods:affiliation>Department of Neurochemistry, CID-CSIC, Barcelona, Spain</mods:affiliation></affiliation></author><author><name sortKey="Sarasa, M" sort="Sarasa, M" uniqKey="Sarasa M" first="M." last="Sarasa">M. Sarasa</name><affiliation><mods:affiliation>Department of Anatomy, Embryology and Genetics, Veterinary Faculty, University of Zaragoza, Zaragoza, Spain</mods:affiliation></affiliation></author><author><name sortKey="Baudier, J" sort="Baudier, J" uniqKey="Baudier J" first="J." last="Baudier">J. Baudier</name><affiliation><mods:affiliation>Laboratoire de Biologie Moleculaire, Cycle Cellulaire, INSERM U309, 38041 Grenoble, France</mods:affiliation></affiliation></author><author><name sortKey="Palacios, J M" sort="Palacios, J M" uniqKey="Palacios J" first="J. M." last="Palacios">J. M. Palacios</name><affiliation><mods:affiliation>Department of Neurochemistry, CID-CSIC, Barcelona, Spain</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Molecular Brain Research</title><title level="j" type="abbrev">BRESM</title><idno type="ISSN">0169-328X</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1994">1994</date><biblScope unit="volume">24</biblScope><biblScope unit="issue">1–4</biblScope><biblScope unit="page" from="107">107</biblScope><biblScope unit="page" to="117">117</biblScope></imprint><idno type="ISSN">0169-328X</idno></series><idno type="istex">0661A17BF16D8B865EBD3C4701946D423535CF3A</idno><idno type="DOI">10.1016/0169-328X(94)90122-8</idno><idno type="PII">0169-328X(94)90122-8</idno><idno type="ArticleID">94901228</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0169-328X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Axotomy</term><term>Facial nucleus</term><term>GAP-43</term><term>Immunocytochemistry</term><term>Rat brain</term><term>mRNA</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: In order to investigate the modulation of the synthesis and the subcellular localization of the growth associated protein GAP-43 in neuronal cell bodies we have taken advantage of the well known regenerative properties of axotomized motor neurons of the facial and hypoglossal nuclei. Alterations in the levels of GAP-43 mRNA containing cells were studied by in situ hybridization histochemistry. The protein localization was examined using immunohistochemistry at the light and electron microscopic levels. Neurons from the control side showed undetectable levels of both GAP-43-like immunoreactivity and GAP-43 mRNA levels. Whereas axotomized neurons exhibited a marked increase in GAP-43 mRNA levels and in GAP-43-like immunoreactivity. Three to 50 days after axotomy, motor neurons ipsilateral to the lesion displayed a dense reticular or filamentous perinuclear distribution of the immunoreactivity in somata and proximal dendritic processes, corresponding to the location of the Golgi apparatus in these neurons. At the electron microscopic level the immunoreactivity was located in the cisternae of the Golgi complex and found to be associated with trans-side vesicles of these complexes. The myelinated fibers of the transectomized facial nerve also presented an intense GAP-43-like immunoreactivity. Twenty-one days after the axotomy a decay in the number of immunostained neurons and in the intensity of immunolabeled somata was observed. Our study reveals a rapid induction of GAP-43 mRNA and protein after axotomy. The localization of the newly synthesized GAP-43-like immunoreactivity to the Golgi apparatus seen in the present work suggests an early association of this protein with newly formed membranes prior to transport toward the terminals through the axons.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>G. Palacios</name><affiliations><json:string>Department of Cellular Biology and Physiology, Subunit of Histology, Faculty of Medicine, Uniuersidad Auto´noma de Barcelona, Bellaterra, Barcelona 08193, Spain</json:string></affiliations></json:item><json:item><name>G. Mengod</name><affiliations><json:string>Department of Neurochemistry, CID-CSIC, Barcelona, Spain</json:string></affiliations></json:item><json:item><name>M. Sarasa</name><affiliations><json:string>Department of Anatomy, Embryology and Genetics, Veterinary Faculty, University of Zaragoza, Zaragoza, Spain</json:string></affiliations></json:item><json:item><name>J. Baudier</name><affiliations><json:string>Laboratoire de Biologie Moleculaire, Cycle Cellulaire, INSERM U309, 38041 Grenoble, France</json:string></affiliations></json:item><json:item><name>J.M. Palacios</name><affiliations><json:string>Department of Neurochemistry, CID-CSIC, Barcelona, Spain</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>GAP-43</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Rat brain</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Immunocytochemistry</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>mRNA</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Axotomy</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Facial nucleus</value></json:item></subject><articleId><json:string>94901228</json:string></articleId><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: In order to investigate the modulation of the synthesis and the subcellular localization of the growth associated protein GAP-43 in neuronal cell bodies we have taken advantage of the well known regenerative properties of axotomized motor neurons of the facial and hypoglossal nuclei. Alterations in the levels of GAP-43 mRNA containing cells were studied by in situ hybridization histochemistry. The protein localization was examined using immunohistochemistry at the light and electron microscopic levels. Neurons from the control side showed undetectable levels of both GAP-43-like immunoreactivity and GAP-43 mRNA levels. Whereas axotomized neurons exhibited a marked increase in GAP-43 mRNA levels and in GAP-43-like immunoreactivity. Three to 50 days after axotomy, motor neurons ipsilateral to the lesion displayed a dense reticular or filamentous perinuclear distribution of the immunoreactivity in somata and proximal dendritic processes, corresponding to the location of the Golgi apparatus in these neurons. At the electron microscopic level the immunoreactivity was located in the cisternae of the Golgi complex and found to be associated with trans-side vesicles of these complexes. The myelinated fibers of the transectomized facial nerve also presented an intense GAP-43-like immunoreactivity. Twenty-one days after the axotomy a decay in the number of immunostained neurons and in the intensity of immunolabeled somata was observed. Our study reveals a rapid induction of GAP-43 mRNA and protein after axotomy. The localization of the newly synthesized GAP-43-like immunoreactivity to the Golgi apparatus seen in the present work suggests an early association of this protein with newly formed membranes prior to transport toward the terminals through the axons.</abstract><qualityIndicators><score>8</score><pdfVersion>1.3</pdfVersion><pdfPageSize>612 x 792 pts (letter)</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>6</keywordCount><abstractCharCount>1788</abstractCharCount><pdfWordCount>5866</pdfWordCount><pdfCharCount>35188</pdfCharCount><pdfPageCount>11</pdfPageCount><abstractWordCount>258</abstractWordCount></qualityIndicators><title>De novo synthesis of GAP-43: in situ hybridization histochemistry and light and electron microscopy immunocytochemical studies in regenerating motor neurons of cranial nerve nuclei in the rat brain</title><pii><json:string>0169-328X(94)90122-8</json:string></pii><refBibs><json:item><author><json:item><name>J. 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All rights reserved</p></availability><date>1994</date></publicationStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">De novo synthesis of GAP-43: in situ hybridization histochemistry and light and electron microscopy immunocytochemical studies in regenerating motor neurons of cranial nerve nuclei in the rat brain</title><author xml:id="author-1"><persName><forename type="first">G.</forename><surname>Palacios</surname></persName><note type="correspondence"><p>Corresponding author.</p></note><affiliation>Department of Cellular Biology and Physiology, Subunit of Histology, Faculty of Medicine, Uniuersidad Auto´noma de Barcelona, Bellaterra, Barcelona 08193, Spain</affiliation></author><author xml:id="author-2"><persName><forename type="first">G.</forename><surname>Mengod</surname></persName><affiliation>Department of Neurochemistry, CID-CSIC, Barcelona, Spain</affiliation></author><author xml:id="author-3"><persName><forename type="first">M.</forename><surname>Sarasa</surname></persName><affiliation>Department of Anatomy, Embryology and Genetics, Veterinary Faculty, University of Zaragoza, Zaragoza, Spain</affiliation></author><author xml:id="author-4"><persName><forename type="first">J.</forename><surname>Baudier</surname></persName><affiliation>Laboratoire de Biologie Moleculaire, Cycle Cellulaire, INSERM U309, 38041 Grenoble, France</affiliation></author><author xml:id="author-5"><persName><forename type="first">J.M.</forename><surname>Palacios</surname></persName><affiliation>Department of Neurochemistry, CID-CSIC, Barcelona, Spain</affiliation></author></analytic><monogr><title level="j">Molecular Brain Research</title><title level="j" type="abbrev">BRESM</title><idno type="pISSN">0169-328X</idno><idno type="PII">S0169-328X(00)X0192-1</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1994"></date><biblScope unit="volume">24</biblScope><biblScope unit="issue">1–4</biblScope><biblScope unit="page" from="107">107</biblScope><biblScope unit="page" to="117">117</biblScope></imprint></monogr><idno type="istex">0661A17BF16D8B865EBD3C4701946D423535CF3A</idno><idno type="DOI">10.1016/0169-328X(94)90122-8</idno><idno type="PII">0169-328X(94)90122-8</idno><idno type="ArticleID">94901228</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1994</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: In order to investigate the modulation of the synthesis and the subcellular localization of the growth associated protein GAP-43 in neuronal cell bodies we have taken advantage of the well known regenerative properties of axotomized motor neurons of the facial and hypoglossal nuclei. Alterations in the levels of GAP-43 mRNA containing cells were studied by in situ hybridization histochemistry. The protein localization was examined using immunohistochemistry at the light and electron microscopic levels. Neurons from the control side showed undetectable levels of both GAP-43-like immunoreactivity and GAP-43 mRNA levels. Whereas axotomized neurons exhibited a marked increase in GAP-43 mRNA levels and in GAP-43-like immunoreactivity. Three to 50 days after axotomy, motor neurons ipsilateral to the lesion displayed a dense reticular or filamentous perinuclear distribution of the immunoreactivity in somata and proximal dendritic processes, corresponding to the location of the Golgi apparatus in these neurons. At the electron microscopic level the immunoreactivity was located in the cisternae of the Golgi complex and found to be associated with trans-side vesicles of these complexes. The myelinated fibers of the transectomized facial nerve also presented an intense GAP-43-like immunoreactivity. Twenty-one days after the axotomy a decay in the number of immunostained neurons and in the intensity of immunolabeled somata was observed. Our study reveals a rapid induction of GAP-43 mRNA and protein after axotomy. The localization of the newly synthesized GAP-43-like immunoreactivity to the Golgi apparatus seen in the present work suggests an early association of this protein with newly formed membranes prior to transport toward the terminals through the axons.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head><item><term>GAP-43</term></item><item><term>Rat brain</term></item><item><term>Immunocytochemistry</term></item><item><term>mRNA</term></item><item><term>Axotomy</term></item><item><term>Facial nucleus</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1994">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/0661A17BF16D8B865EBD3C4701946D423535CF3A/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier doc found" wicri:toSee="Elsevier, no converted or simple article"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 5.0.1//EN//XML" URI="art501.dtd" name="istex:docType"></istex:docType><istex:document><article version="5.0" xml:lang="en" docsubtype="fla"><item-info><jid>BRESM</jid><aid>94901228</aid><ce:pii>0169-328X(94)90122-8</ce:pii><ce:doi>10.1016/0169-328X(94)90122-8</ce:doi><ce:copyright type="unknown" year="1994">Elsevier Science B.V. All rights reserved</ce:copyright></item-info><head><ce:title>De novo synthesis of GAP-43: in situ hybridization histochemistry and light and electron microscopy immunocytochemical studies in regenerating motor neurons of cranial nerve nuclei in the rat brain</ce:title><ce:author-group><ce:author><ce:given-name>G.</ce:given-name><ce:surname>Palacios</ce:surname><ce:cross-ref refid="cor1"><ce:sup>*</ce:sup></ce:cross-ref><ce:cross-ref refid="aff1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>G.</ce:given-name><ce:surname>Mengod</ce:surname><ce:cross-ref refid="aff2"><ce:sup>b</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>M.</ce:given-name><ce:surname>Sarasa</ce:surname><ce:cross-ref refid="aff3"><ce:sup>c</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>J.</ce:given-name><ce:surname>Baudier</ce:surname><ce:cross-ref refid="aff4"><ce:sup>d</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>J.M.</ce:given-name><ce:surname>Palacios</ce:surname><ce:cross-ref refid="aff2"><ce:sup>b</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="aff1"><ce:label>a</ce:label><ce:textfn>Department of Cellular Biology and Physiology, Subunit of Histology, Faculty of Medicine, Uniuersidad Auto´noma de Barcelona, Bellaterra, Barcelona 08193, Spain</ce:textfn></ce:affiliation><ce:affiliation id="aff2"><ce:label>b</ce:label><ce:textfn>Department of Neurochemistry, CID-CSIC, Barcelona, Spain</ce:textfn></ce:affiliation><ce:affiliation id="aff3"><ce:label>c</ce:label><ce:textfn>Department of Anatomy, Embryology and Genetics, Veterinary Faculty, University of Zaragoza, Zaragoza, Spain</ce:textfn></ce:affiliation><ce:affiliation id="aff4"><ce:label>d</ce:label><ce:textfn>Laboratoire de Biologie Moleculaire, Cycle Cellulaire, INSERM U309, 38041 Grenoble, France</ce:textfn></ce:affiliation><ce:correspondence id="cor1"><ce:label>*</ce:label><ce:text>Corresponding author.</ce:text></ce:correspondence></ce:author-group><ce:date-accepted day="28" month="12" year="1993"></ce:date-accepted><ce:abstract id="ab1" class="author" xml:lang="en"><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>In order to investigate the modulation of the synthesis and the subcellular localization of the growth associated protein GAP-43 in neuronal cell bodies we have taken advantage of the well known regenerative properties of axotomized motor neurons of the facial and hypoglossal nuclei. Alterations in the levels of GAP-43 mRNA containing cells were studied by in situ hybridization histochemistry. The protein localization was examined using immunohistochemistry at the light and electron microscopic levels. Neurons from the control side showed undetectable levels of both GAP-43-like immunoreactivity and GAP-43 mRNA levels. Whereas axotomized neurons exhibited a marked increase in GAP-43 mRNA levels and in GAP-43-like immunoreactivity. Three to 50 days after axotomy, motor neurons ipsilateral to the lesion displayed a dense reticular or filamentous perinuclear distribution of the immunoreactivity in somata and proximal dendritic processes, corresponding to the location of the Golgi apparatus in these neurons. At the electron microscopic level the immunoreactivity was located in the cisternae of the Golgi complex and found to be associated with trans-side vesicles of these complexes. The myelinated fibers of the transectomized facial nerve also presented an intense GAP-43-like immunoreactivity. Twenty-one days after the axotomy a decay in the number of immunostained neurons and in the intensity of immunolabeled somata was observed. Our study reveals a rapid induction of GAP-43 mRNA and protein after axotomy. The localization of the newly synthesized GAP-43-like immunoreactivity to the Golgi apparatus seen in the present work suggests an early association of this protein with newly formed membranes prior to transport toward the terminals through the axons.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords class="keyword" xml:lang="en"><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>GAP-43</ce:text></ce:keyword><ce:keyword><ce:text>Rat brain</ce:text></ce:keyword><ce:keyword><ce:text>Immunocytochemistry</ce:text></ce:keyword><ce:keyword><ce:text>mRNA</ce:text></ce:keyword><ce:keyword><ce:text>Axotomy</ce:text></ce:keyword><ce:keyword><ce:text>Facial nucleus</ce:text></ce:keyword></ce:keywords></head><tail><ce:bibliography><ce:section-title>Reference</ce:section-title><ce:bibliography-sec><ce:bib-reference id="bib1"><ce:label>[1]</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:surname>Baudier</ce:surname><ce:given-name>J.</ce:given-name></sb:author><sb:author><ce:surname>Bronner</ce:surname><ce:given-name>C.</ce:given-name></sb:author><sb:author><ce:surname>Kligman</ce:surname><ce:given-name>D.</ce:given-name></sb:author><sb:author><ce:surname>Cole</ce:surname><ce:given-name>R.D.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Protein kinase C substrates from bovine brain</sb:maintitle></sb:title></sb:contribution><sb:host><sb:edited-book><sb:title><sb:maintitle>Purification and characterization of neuromodulin, a neuron-specific calmodulin-binding protein</sb:maintitle></sb:title><sb:edition>2nd edn.</sb:edition><sb:book-series><sb:series><sb:title><sb:maintitle>J. 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Neurosci.</sb:maintitle></sb:title><sb:volume-nr>12</sb:volume-nr></sb:series><sb:date>1992</sb:date></sb:issue><sb:pages><sb:first-page>3999</sb:first-page><sb:last-page>4010</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference></ce:bibliography-sec></ce:bibliography></tail></article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>De novo synthesis of GAP-43: in situ hybridization histochemistry and light and electron microscopy immunocytochemical studies in regenerating motor neurons of cranial nerve nuclei in the rat brain</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>De novo synthesis of GAP-43: in situ hybridization histochemistry and light and electron microscopy immunocytochemical studies in regenerating motor neurons of cranial nerve nuclei in the rat brain</title></titleInfo><name type="personal"><namePart type="given">G.</namePart><namePart type="family">Palacios</namePart><affiliation>Department of Cellular Biology and Physiology, Subunit of Histology, Faculty of Medicine, Uniuersidad Auto´noma de Barcelona, Bellaterra, Barcelona 08193, Spain</affiliation><description>Corresponding author.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">G.</namePart><namePart type="family">Mengod</namePart><affiliation>Department of Neurochemistry, CID-CSIC, Barcelona, Spain</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">M.</namePart><namePart type="family">Sarasa</namePart><affiliation>Department of Anatomy, Embryology and Genetics, Veterinary Faculty, University of Zaragoza, Zaragoza, Spain</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">J.</namePart><namePart type="family">Baudier</namePart><affiliation>Laboratoire de Biologie Moleculaire, Cycle Cellulaire, INSERM U309, 38041 Grenoble, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">J.M.</namePart><namePart type="family">Palacios</namePart><affiliation>Department of Neurochemistry, CID-CSIC, Barcelona, Spain</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article"></genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1994</dateIssued><copyrightDate encoding="w3cdtf">1994</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract lang="en">Abstract: In order to investigate the modulation of the synthesis and the subcellular localization of the growth associated protein GAP-43 in neuronal cell bodies we have taken advantage of the well known regenerative properties of axotomized motor neurons of the facial and hypoglossal nuclei. Alterations in the levels of GAP-43 mRNA containing cells were studied by in situ hybridization histochemistry. The protein localization was examined using immunohistochemistry at the light and electron microscopic levels. Neurons from the control side showed undetectable levels of both GAP-43-like immunoreactivity and GAP-43 mRNA levels. Whereas axotomized neurons exhibited a marked increase in GAP-43 mRNA levels and in GAP-43-like immunoreactivity. Three to 50 days after axotomy, motor neurons ipsilateral to the lesion displayed a dense reticular or filamentous perinuclear distribution of the immunoreactivity in somata and proximal dendritic processes, corresponding to the location of the Golgi apparatus in these neurons. At the electron microscopic level the immunoreactivity was located in the cisternae of the Golgi complex and found to be associated with trans-side vesicles of these complexes. The myelinated fibers of the transectomized facial nerve also presented an intense GAP-43-like immunoreactivity. Twenty-one days after the axotomy a decay in the number of immunostained neurons and in the intensity of immunolabeled somata was observed. Our study reveals a rapid induction of GAP-43 mRNA and protein after axotomy. The localization of the newly synthesized GAP-43-like immunoreactivity to the Golgi apparatus seen in the present work suggests an early association of this protein with newly formed membranes prior to transport toward the terminals through the axons.</abstract><subject lang="en"><genre>Keywords</genre><topic>GAP-43</topic><topic>Rat brain</topic><topic>Immunocytochemistry</topic><topic>mRNA</topic><topic>Axotomy</topic><topic>Facial nucleus</topic></subject><relatedItem type="host"><titleInfo><title>Molecular Brain Research</title></titleInfo><titleInfo type="abbreviated"><title>BRESM</title></titleInfo><genre type="journal">journal</genre><originInfo><dateIssued encoding="w3cdtf">199407</dateIssued></originInfo><identifier type="ISSN">0169-328X</identifier><identifier type="PII">S0169-328X(00)X0192-1</identifier><part><date>199407</date><detail type="volume"><number>24</number><caption>vol.</caption></detail><detail type="issue"><number>1–4</number><caption>no.</caption></detail><extent unit="issue pages"><start>1</start><end>360</end></extent><extent unit="pages"><start>107</start><end>117</end></extent></part></relatedItem><identifier type="istex">0661A17BF16D8B865EBD3C4701946D423535CF3A</identifier><identifier type="DOI">10.1016/0169-328X(94)90122-8</identifier><identifier type="PII">0169-328X(94)90122-8</identifier><identifier type="ArticleID">94901228</identifier><accessCondition type="use and reproduction" contentType="copyright">©1994 Elsevier Science B.V. 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