Exposure of tumor necrosis factor‐α to luminal membrane of bovine brain capillary endothelial cells cocultured with astrocytes induces a delayed increase of permeability and cytoplasmic stress fiber formation of actin
Identifieur interne : 001946 ( Istex/Corpus ); précédent : 001945; suivant : 001947Exposure of tumor necrosis factor‐α to luminal membrane of bovine brain capillary endothelial cells cocultured with astrocytes induces a delayed increase of permeability and cytoplasmic stress fiber formation of actin
Auteurs : M. A. Deli ; L. Descamps ; M. Dehouck ; R. Cecchelli ; F. Jo ; C. S. Ábrahám ; G. TorpierSource :
- Journal of Neuroscience Research [ 0360-4012 ] ; 1995-08-15.
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Abstract
Tumor necrosis factor‐α (TNF‐α), a proinflammatory cytokine, has long been known to be involved in the pathogenesis of central nervous system infections and of certain neurodegenerative diseases. However, the possible role of the blood‐brain barrier (BBB), the active interface between the blood circulation and brain tissue, remained unknown during these pathological conditions. In our in vitro reconstructed BBB model, 1‐hr exposure of recombinant human TNF‐α (in concentrations of 50, 250, and 500 U/ml, respectively) to the luminal membrane of bovine brain capillary endothelial cells (BBCEC) did not change significantly the transendothelia: flux of either sucrose (m.w. 342 Da), or inulin (m.w. 5 kDa) up to 4 hr (early phase), except for a slight decrease (P< 0.05) in sucrose permeation at 2–4 hr with the highest dose of TNF‐α On the other hand, at 16 hr after the 1‐hr challenge with TNF‐α (delayed phase) at all 3 concentrations, significant increase was induced in the permeability of BBCEC monolayers for both markers. These changes of permeability were accompanied by a selective reorganization of F‐actin filaments into stress fibers, while the intracellular distribution of vimentin remained similar to the control. These results suggest that BBCEC can respond directly to TNF‐α by a delayed increase of permeability and reorganization of actin filaments. ©1995 Wiley‐Liss, Inc.
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DOI: 10.1002/jnr.490410602
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ISTEX:F3F000080C8118D02C67599B7C9BF89E437C012DLe document en format XML
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Dehouck</name><affiliation><mods:affiliation>INSERM U. 325, Institut Pasteur‐Lille, Lille, France</mods:affiliation></affiliation></author><author><name sortKey="Cecchelli, R" sort="Cecchelli, R" uniqKey="Cecchelli R" first="R." last="Cecchelli">R. Cecchelli</name><affiliation><mods:affiliation>INSERM U. 325, Institut Pasteur‐Lille, Lille, France</mods:affiliation></affiliation></author><author><name sortKey="Jo, F" sort="Jo, F" uniqKey="Jo F" first="F." last="Jo">F. Jo</name><affiliation><mods:affiliation>Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary</mods:affiliation></affiliation></author><author><name sortKey="Abraham, C S" sort="Abraham, C S" uniqKey="Abraham C" first="C. S." last="Ábrahám">C. S. Ábrahám</name><affiliation><mods:affiliation>Department of Pediatrics, Albert Szent‐Györgyi Medical University, Szeged, Hungary</mods:affiliation></affiliation></author><author><name sortKey="Torpier, G" sort="Torpier, G" uniqKey="Torpier G" first="G." last="Torpier">G. Torpier</name><affiliation><mods:affiliation>INSERM U. 325, Institut Pasteur‐Lille, Lille, France</mods:affiliation></affiliation><affiliation><mods:affiliation>INSERM U.325, Institut Pasteur‐Lille, 1 Rue A. 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Deli</name><affiliation><mods:affiliation>Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary</mods:affiliation></affiliation></author><author><name sortKey="Descamps, L" sort="Descamps, L" uniqKey="Descamps L" first="L." last="Descamps">L. Descamps</name><affiliation><mods:affiliation>INSERM U. 325, Institut Pasteur‐Lille, Lille, France</mods:affiliation></affiliation></author><author><name sortKey="Dehouck, M" sort="Dehouck, M" uniqKey="Dehouck M" first="M." last="Dehouck">M. Dehouck</name><affiliation><mods:affiliation>INSERM U. 325, Institut Pasteur‐Lille, Lille, France</mods:affiliation></affiliation></author><author><name sortKey="Cecchelli, R" sort="Cecchelli, R" uniqKey="Cecchelli R" first="R." last="Cecchelli">R. Cecchelli</name><affiliation><mods:affiliation>INSERM U. 325, Institut Pasteur‐Lille, Lille, France</mods:affiliation></affiliation></author><author><name sortKey="Jo, F" sort="Jo, F" uniqKey="Jo F" first="F." last="Jo">F. Jo</name><affiliation><mods:affiliation>Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary</mods:affiliation></affiliation></author><author><name sortKey="Abraham, C S" sort="Abraham, C S" uniqKey="Abraham C" first="C. S." last="Ábrahám">C. S. Ábrahám</name><affiliation><mods:affiliation>Department of Pediatrics, Albert Szent‐Györgyi Medical University, Szeged, Hungary</mods:affiliation></affiliation></author><author><name sortKey="Torpier, G" sort="Torpier, G" uniqKey="Torpier G" first="G." last="Torpier">G. Torpier</name><affiliation><mods:affiliation>INSERM U. 325, Institut Pasteur‐Lille, Lille, France</mods:affiliation></affiliation><affiliation><mods:affiliation>INSERM U.325, Institut Pasteur‐Lille, 1 Rue A. Calmette, B.P. 245, 59019 Lille, France</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Neuroscience Research</title><title level="j" type="abbrev">J. Neurosci. Res.</title><idno type="ISSN">0360-4012</idno><idno type="eISSN">1097-4547</idno><imprint><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="1995-08-15">1995-08-15</date><biblScope unit="volume">41</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="717">717</biblScope><biblScope unit="page" to="726">726</biblScope></imprint><idno type="ISSN">0360-4012</idno></series><idno type="istex">F3F000080C8118D02C67599B7C9BF89E437C012D</idno><idno type="DOI">10.1002/jnr.490410602</idno><idno type="ArticleID">JNR490410602</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0360-4012</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>actin</term><term>astrocytes</term><term>blood‐brain barrier (BBB)</term><term>endothelial cells</term><term>stress fiber</term><term>tumor necrosis factor‐α</term><term>vascular permeability</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Tumor necrosis factor‐α (TNF‐α), a proinflammatory cytokine, has long been known to be involved in the pathogenesis of central nervous system infections and of certain neurodegenerative diseases. However, the possible role of the blood‐brain barrier (BBB), the active interface between the blood circulation and brain tissue, remained unknown during these pathological conditions. In our in vitro reconstructed BBB model, 1‐hr exposure of recombinant human TNF‐α (in concentrations of 50, 250, and 500 U/ml, respectively) to the luminal membrane of bovine brain capillary endothelial cells (BBCEC) did not change significantly the transendothelia: flux of either sucrose (m.w. 342 Da), or inulin (m.w. 5 kDa) up to 4 hr (early phase), except for a slight decrease (P< 0.05) in sucrose permeation at 2–4 hr with the highest dose of TNF‐α On the other hand, at 16 hr after the 1‐hr challenge with TNF‐α (delayed phase) at all 3 concentrations, significant increase was induced in the permeability of BBCEC monolayers for both markers. These changes of permeability were accompanied by a selective reorganization of F‐actin filaments into stress fibers, while the intracellular distribution of vimentin remained similar to the control. These results suggest that BBCEC can respond directly to TNF‐α by a delayed increase of permeability and reorganization of actin filaments. ©1995 Wiley‐Liss, Inc.</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>M. A. Deli</name><affiliations><json:string>Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary</json:string></affiliations></json:item><json:item><name>L. Descamps</name><affiliations><json:string>INSERM U. 325, Institut Pasteur‐Lille, Lille, France</json:string></affiliations></json:item><json:item><name>M.‐P. Dehouck</name><affiliations><json:string>INSERM U. 325, Institut Pasteur‐Lille, Lille, France</json:string></affiliations></json:item><json:item><name>R. Cecchelli</name><affiliations><json:string>INSERM U. 325, Institut Pasteur‐Lille, Lille, France</json:string></affiliations></json:item><json:item><name>F. Joó</name><affiliations><json:string>Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary</json:string></affiliations></json:item><json:item><name>C. S. Ábrahám</name><affiliations><json:string>Department of Pediatrics, Albert Szent‐Györgyi Medical University, Szeged, Hungary</json:string></affiliations></json:item><json:item><name>G. Torpier Ph.D.</name><affiliations><json:string>INSERM U. 325, Institut Pasteur‐Lille, Lille, France</json:string><json:string>INSERM U.325, Institut Pasteur‐Lille, 1 Rue A. Calmette, B.P. 245, 59019 Lille, France</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>blood‐brain barrier (BBB)</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>tumor necrosis factor‐α</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>actin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>stress fiber</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>vascular permeability</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>astrocytes</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>endothelial cells</value></json:item></subject><articleId><json:string>JNR490410602</json:string></articleId><language><json:string>eng</json:string></language><originalGenre><json:string>article</json:string></originalGenre><abstract>Tumor necrosis factor‐α (TNF‐α), a proinflammatory cytokine, has long been known to be involved in the pathogenesis of central nervous system infections and of certain neurodegenerative diseases. However, the possible role of the blood‐brain barrier (BBB), the active interface between the blood circulation and brain tissue, remained unknown during these pathological conditions. In our in vitro reconstructed BBB model, 1‐hr exposure of recombinant human TNF‐α (in concentrations of 50, 250, and 500 U/ml, respectively) to the luminal membrane of bovine brain capillary endothelial cells (BBCEC) did not change significantly the transendothelia: flux of either sucrose (m.w. 342 Da), or inulin (m.w. 5 kDa) up to 4 hr (early phase), except for a slight decrease (P> 0.05) in sucrose permeation at 2–4 hr with the highest dose of TNF‐α On the other hand, at 16 hr after the 1‐hr challenge with TNF‐α (delayed phase) at all 3 concentrations, significant increase was induced in the permeability of BBCEC monolayers for both markers. These changes of permeability were accompanied by a selective reorganization of F‐actin filaments into stress fibers, while the intracellular distribution of vimentin remained similar to the control. These results suggest that BBCEC can respond directly to TNF‐α by a delayed increase of permeability and reorganization of actin filaments. ©1995 Wiley‐Liss, Inc.</abstract><qualityIndicators><score>7.532</score><pdfVersion>1.3</pdfVersion><pdfPageSize>594 x 792 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractCharCount>1395</abstractCharCount><pdfWordCount>5347</pdfWordCount><pdfCharCount>33091</pdfCharCount><pdfPageCount>10</pdfPageCount><abstractWordCount>211</abstractWordCount></qualityIndicators><title>Exposure of tumor necrosis factor‐α to luminal membrane of bovine brain capillary endothelial cells cocultured with astrocytes induces a delayed increase of permeability and cytoplasmic stress fiber formation of actin</title><refBibs><json:item><author><json:item><name>A Aderem</name></json:item></author><host><volume>17</volume><pages><last>443</last><first>438</first></pages><author></author><title>TIBS</title></host><title>Signal transduction and the actin 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A.</forename><surname>Deli</surname></persName><affiliation>Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary</affiliation></author><author xml:id="author-2"><persName><forename type="first">L.</forename><surname>Descamps</surname></persName><affiliation>INSERM U. 325, Institut Pasteur‐Lille, Lille, France</affiliation></author><author xml:id="author-3"><persName><forename type="first">M.‐P.</forename><surname>Dehouck</surname></persName><affiliation>INSERM U. 325, Institut Pasteur‐Lille, Lille, France</affiliation></author><author xml:id="author-4"><persName><forename type="first">R.</forename><surname>Cecchelli</surname></persName><affiliation>INSERM U. 325, Institut Pasteur‐Lille, Lille, France</affiliation></author><author xml:id="author-5"><persName><forename type="first">F.</forename><surname>Joó</surname></persName><affiliation>Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary</affiliation></author><author xml:id="author-6"><persName><forename type="first">C. S.</forename><surname>Ábrahám</surname></persName><affiliation>Department of Pediatrics, Albert Szent‐Györgyi Medical University, Szeged, Hungary</affiliation></author><author xml:id="author-7"><persName><forename type="first">G.</forename><surname>Torpier</surname></persName><roleName type="degree">Ph.D.</roleName><affiliation>INSERM U. 325, Institut Pasteur‐Lille, Lille, France</affiliation><affiliation>INSERM U.325, Institut Pasteur‐Lille, 1 Rue A. Calmette, B.P. 245, 59019 Lille, France</affiliation></author></analytic><monogr><title level="j">Journal of Neuroscience Research</title><title level="j" type="abbrev">J. Neurosci. Res.</title><idno type="pISSN">0360-4012</idno><idno type="eISSN">1097-4547</idno><idno type="DOI">10.1002/(ISSN)1097-4547</idno><imprint><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="1995-08-15"></date><biblScope unit="volume">41</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="717">717</biblScope><biblScope unit="page" to="726">726</biblScope></imprint></monogr><idno type="istex">F3F000080C8118D02C67599B7C9BF89E437C012D</idno><idno type="DOI">10.1002/jnr.490410602</idno><idno type="ArticleID">JNR490410602</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1995</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Tumor necrosis factor‐α (TNF‐α), a proinflammatory cytokine, has long been known to be involved in the pathogenesis of central nervous system infections and of certain neurodegenerative diseases. However, the possible role of the blood‐brain barrier (BBB), the active interface between the blood circulation and brain tissue, remained unknown during these pathological conditions. In our in vitro reconstructed BBB model, 1‐hr exposure of recombinant human TNF‐α (in concentrations of 50, 250, and 500 U/ml, respectively) to the luminal membrane of bovine brain capillary endothelial cells (BBCEC) did not change significantly the transendothelia: flux of either sucrose (m.w. 342 Da), or inulin (m.w. 5 kDa) up to 4 hr (early phase), except for a slight decrease (P< 0.05) in sucrose permeation at 2–4 hr with the highest dose of TNF‐α On the other hand, at 16 hr after the 1‐hr challenge with TNF‐α (delayed phase) at all 3 concentrations, significant increase was induced in the permeability of BBCEC monolayers for both markers. These changes of permeability were accompanied by a selective reorganization of F‐actin filaments into stress fibers, while the intracellular distribution of vimentin remained similar to the control. These results suggest that BBCEC can respond directly to TNF‐α by a delayed increase of permeability and reorganization of actin filaments. ©1995 Wiley‐Liss, Inc.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>keywords</head><item><term>blood‐brain barrier (BBB)</term></item><item><term>tumor necrosis factor‐α</term></item><item><term>actin</term></item><item><term>stress fiber</term></item><item><term>vascular permeability</term></item><item><term>astrocytes</term></item><item><term>endothelial cells</term></item></list></keywords></textClass><textClass><keywords scheme="Journal Subject"><list><head>article-category</head><item><term>Article</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1994-08-15">Received</change><change when="1994-11-09">Registration</change><change when="1995-08-15">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/F3F000080C8118D02C67599B7C9BF89E437C012D/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" xml:lang="en"><header><publicationMeta level="product"><publisherInfo><publisherName>Wiley Subscription Services, Inc., A Wiley Company</publisherName><publisherLoc>Hoboken</publisherLoc></publisherInfo><doi registered="yes">10.1002/(ISSN)1097-4547</doi><issn type="print">0360-4012</issn><issn type="electronic">1097-4547</issn><idGroup><id type="product" value="JNR"></id></idGroup><titleGroup><title type="main" xml:lang="en" sort="JOURNAL OF NEUROSCIENCE RESEARCH">Journal of Neuroscience Research</title><title type="short">J. 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Calmette, B.P. 245, 59019 Lille, France</correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:JNR.JNR490410602.pdf"></link></linkGroup></publicationMeta><contentMeta><countGroup><count type="figureTotal" number="5"></count><count type="tableTotal" number="0"></count><count type="referenceTotal" number="50"></count></countGroup><titleGroup><title type="main" xml:lang="en">Exposure of tumor necrosis factor‐α to luminal membrane of bovine brain capillary endothelial cells cocultured with astrocytes induces a delayed increase of permeability and cytoplasmic stress fiber formation of actin</title><title type="short" xml:lang="en">Effects of TNF‐α on Blood‐Brain Barrier</title></titleGroup><creators><creator xml:id="au1" creatorRole="author" affiliationRef="#af1"><personName><givenNames>M. A.</givenNames><familyName>Deli</familyName></personName></creator><creator xml:id="au2" creatorRole="author" affiliationRef="#af3"><personName><givenNames>L.</givenNames><familyName>Descamps</familyName></personName></creator><creator xml:id="au3" creatorRole="author" affiliationRef="#af3"><personName><givenNames>M.‐P.</givenNames><familyName>Dehouck</familyName></personName></creator><creator xml:id="au4" creatorRole="author" affiliationRef="#af3"><personName><givenNames>R.</givenNames><familyName>Cecchelli</familyName></personName></creator><creator xml:id="au5" creatorRole="author" affiliationRef="#af1"><personName><givenNames>F.</givenNames><familyName>Joó</familyName></personName></creator><creator xml:id="au6" creatorRole="author" affiliationRef="#af2"><personName><givenNames>C. S.</givenNames><familyName>Ábrahám</familyName></personName></creator><creator xml:id="au7" creatorRole="author" affiliationRef="#af3" corresponding="yes"><personName><givenNames>G.</givenNames><familyName>Torpier</familyName><degrees>Ph.D.</degrees></personName></creator></creators><affiliationGroup><affiliation xml:id="af1" countryCode="HU" type="organization"><unparsedAffiliation>Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary</unparsedAffiliation></affiliation><affiliation xml:id="af2" countryCode="HU" type="organization"><unparsedAffiliation>Department of Pediatrics, Albert Szent‐Györgyi Medical University, Szeged, Hungary</unparsedAffiliation></affiliation><affiliation xml:id="af3" countryCode="FR" type="organization"><unparsedAffiliation>INSERM U. 325, Institut Pasteur‐Lille, Lille, France</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en" type="author"><keyword xml:id="kwd1">blood‐brain barrier (BBB)</keyword><keyword xml:id="kwd2">tumor necrosis factor‐α</keyword><keyword xml:id="kwd3">actin</keyword><keyword xml:id="kwd4">stress fiber</keyword><keyword xml:id="kwd5">vascular permeability</keyword><keyword xml:id="kwd6">astrocytes</keyword><keyword xml:id="kwd7">endothelial cells</keyword></keywordGroup><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>Tumor necrosis factor‐α (TNF‐α), a proinflammatory cytokine, has long been known to be involved in the pathogenesis of central nervous system infections and of certain neurodegenerative diseases. However, the possible role of the blood‐brain barrier (BBB), the active interface between the blood circulation and brain tissue, remained unknown during these pathological conditions. In our in vitro reconstructed BBB model, 1‐hr exposure of recombinant human TNF‐α (in concentrations of 50, 250, and 500 U/ml, respectively) to the luminal membrane of bovine brain capillary endothelial cells (BBCEC) did not change significantly the transendothelia: flux of either sucrose (m.w. 342 Da), or inulin (m.w. 5 kDa) up to 4 hr (early phase), except for a slight decrease (P< 0.05) in sucrose permeation at 2–4 hr with the highest dose of TNF‐α On the other hand, at 16 hr after the 1‐hr challenge with TNF‐α (delayed phase) at all 3 concentrations, significant increase was induced in the permeability of BBCEC monolayers for both markers. These changes of permeability were accompanied by a selective reorganization of F‐actin filaments into stress fibers, while the intracellular distribution of vimentin remained similar to the control. These results suggest that BBCEC can respond directly to TNF‐α by a delayed increase of permeability and reorganization of actin filaments. ©1995 Wiley‐Liss, Inc.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Exposure of tumor necrosis factor‐α to luminal membrane of bovine brain capillary endothelial cells cocultured with astrocytes induces a delayed increase of permeability and cytoplasmic stress fiber formation of actin</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Effects of TNF‐α on Blood‐Brain Barrier</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Exposure of tumor necrosis factor‐α to luminal membrane of bovine brain capillary endothelial cells cocultured with astrocytes induces a delayed increase of permeability and cytoplasmic stress fiber formation of actin</title></titleInfo><name type="personal"><namePart type="given">M. A.</namePart><namePart type="family">Deli</namePart><affiliation>Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">L.</namePart><namePart type="family">Descamps</namePart><affiliation>INSERM U. 325, Institut Pasteur‐Lille, Lille, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">M.‐P.</namePart><namePart type="family">Dehouck</namePart><affiliation>INSERM U. 325, Institut Pasteur‐Lille, Lille, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">R.</namePart><namePart type="family">Cecchelli</namePart><affiliation>INSERM U. 325, Institut Pasteur‐Lille, Lille, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">F.</namePart><namePart type="family">Joó</namePart><affiliation>Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">C. S.</namePart><namePart type="family">Ábrahám</namePart><affiliation>Department of Pediatrics, Albert Szent‐Györgyi Medical University, Szeged, Hungary</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">G.</namePart><namePart type="family">Torpier</namePart><namePart type="termsOfAddress">Ph.D.</namePart><affiliation>INSERM U. 325, Institut Pasteur‐Lille, Lille, France</affiliation><affiliation>INSERM U.325, Institut Pasteur‐Lille, 1 Rue A. Calmette, B.P. 245, 59019 Lille, France</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">1995-08-15</dateIssued><dateCaptured encoding="w3cdtf">1994-08-15</dateCaptured><dateValid encoding="w3cdtf">1994-11-09</dateValid><copyrightDate encoding="w3cdtf">1995</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">5</extent><extent unit="references">50</extent></physicalDescription><abstract lang="en">Tumor necrosis factor‐α (TNF‐α), a proinflammatory cytokine, has long been known to be involved in the pathogenesis of central nervous system infections and of certain neurodegenerative diseases. However, the possible role of the blood‐brain barrier (BBB), the active interface between the blood circulation and brain tissue, remained unknown during these pathological conditions. In our in vitro reconstructed BBB model, 1‐hr exposure of recombinant human TNF‐α (in concentrations of 50, 250, and 500 U/ml, respectively) to the luminal membrane of bovine brain capillary endothelial cells (BBCEC) did not change significantly the transendothelia: flux of either sucrose (m.w. 342 Da), or inulin (m.w. 5 kDa) up to 4 hr (early phase), except for a slight decrease (P< 0.05) in sucrose permeation at 2–4 hr with the highest dose of TNF‐α On the other hand, at 16 hr after the 1‐hr challenge with TNF‐α (delayed phase) at all 3 concentrations, significant increase was induced in the permeability of BBCEC monolayers for both markers. These changes of permeability were accompanied by a selective reorganization of F‐actin filaments into stress fibers, while the intracellular distribution of vimentin remained similar to the control. These results suggest that BBCEC can respond directly to TNF‐α by a delayed increase of permeability and reorganization of actin filaments. ©1995 Wiley‐Liss, Inc.</abstract><subject lang="en"><genre>keywords</genre><topic>blood‐brain barrier (BBB)</topic><topic>tumor necrosis factor‐α</topic><topic>actin</topic><topic>stress fiber</topic><topic>vascular permeability</topic><topic>astrocytes</topic><topic>endothelial cells</topic></subject><relatedItem type="host"><titleInfo><title>Journal of Neuroscience Research</title></titleInfo><titleInfo type="abbreviated"><title>J. Neurosci. Res.</title></titleInfo><genre type="journal">journal</genre><subject><genre>article-category</genre><topic>Article</topic></subject><identifier type="ISSN">0360-4012</identifier><identifier type="eISSN">1097-4547</identifier><identifier type="DOI">10.1002/(ISSN)1097-4547</identifier><identifier type="PublisherID">JNR</identifier><part><date>1995</date><detail type="volume"><caption>vol.</caption><number>41</number></detail><detail type="issue"><caption>no.</caption><number>6</number></detail><extent unit="pages"><start>717</start><end>726</end><total>10</total></extent></part></relatedItem><identifier type="istex">F3F000080C8118D02C67599B7C9BF89E437C012D</identifier><identifier type="DOI">10.1002/jnr.490410602</identifier><identifier type="ArticleID">JNR490410602</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 1995 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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