Distinct cellular functions mediated by different VLA integrin α subunit cytoplasmic domains
Identifieur interne : 002634 ( Istex/Corpus ); précédent : 002633; suivant : 002635Distinct cellular functions mediated by different VLA integrin α subunit cytoplasmic domains
Auteurs : Bosco M. C. Chan ; Paul D. Kassner ; James A. Schiro ; H. Randolph Byers ; Thomas S. Kupper ; Martin E. HemlerSource :
- Cell [ 0092-8674 ] ; 1992.
English descriptors
- Teeft :
- Acad, Adhesion, Amino acids, Biol, Cdna, Cell adhesion, Cell biol, Cell migration, Cell morphology, Chain cytoplasmic domains, Chan, Chem, Chimeric, Chimeric cdnas, Collagen, Collagen matrices, Collagen matrix, Cytoplasmic, Cytoplasmic domain, Cytoplasmic domains, Domain, Domain functions, Extracellular, Extracellular matrix, Fibronectin, Fibronectin receptor, Glycoprotein, Hemler, Heterodimer, Hibbs, Immunol, Integrin, Integrin family, Integrins, Laminin, Ligand, Ligand binding, Lymphocyte, Matrix, Migration, Migration rates, Monoclonal, Monoclonal antibodies, Monoclonal antibody, Natl, Physical force, Platelet, Primary structure, Proc, Rdpf, Rdpf cells, Receptor, Ruoslahti, Solowska, Stable exertion, Subunit, Subunit cytoplasmic domains, Takada, Transfectants, Transfected, Transmembrane, Wayner, Yamada.
Abstract
Abstract: To characterize VLA α subunit cytoplasmic domain functions, unaltered α2 cDNA (called X2C2) and two chimeric cDNAs (called X2C5 and X2C4) were constructed with extracellular α2 domains and cytoplasmic α2, α5, and α4 domains respectively. Upon transfection into rhabdomyosarcoma (RD) cells, each construct yielded comparable expression levels, immunoprecipitation profiles, and avidity for collagen and laminin. However, while RDX2C2 and RDX2C5 transfectants mediated collagen gel contraction, RDX2C4 and a mock transfectant (RDpF) did not. Conversely, only RDX2C4 cells (but not RDX2C2 or RDX2C5) showed enhanced cell migration on collagen and laminin compared with RDpF cells. This indicates markedly differing roles for integrin α subunit cytoplasmic domains in post-ligand binding events. Furthermore, stable exertion of physical force (collagen gel contraction) may involve fundamentally different cellular machinery than the transient adhesion occurring during cell migration. Finally, these findings provide insight into a functional flexibility perhaps resulting from multiple integrins binding to identical ligands.
Url:
DOI: 10.1016/0092-8674(92)90077-P
Links to Exploration step
ISTEX:9DC6AA9068FAED2A72A8AB311C67CF6A217681EALe document en format XML
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Schiro</name><affiliation><mods:affiliation>Division of Dermatology Washington University School of Medicine St. Louis, Missouri 63110 USA</mods:affiliation></affiliation></author><author><name sortKey="Byers, H Randolph" sort="Byers, H Randolph" uniqKey="Byers H" first="H. Randolph" last="Byers">H. Randolph Byers</name><affiliation><mods:affiliation>Department of Pathology Massachusetts General Hospital Boston, Massachusetts 02129 USA</mods:affiliation></affiliation></author><author><name sortKey="Kupper, Thomas S" sort="Kupper, Thomas S" uniqKey="Kupper T" first="Thomas S." last="Kupper">Thomas S. Kupper</name><affiliation><mods:affiliation>Division of Dermatology Washington University School of Medicine St. Louis, Missouri 63110 USA</mods:affiliation></affiliation></author><author><name sortKey="Hemler, Martin E" sort="Hemler, Martin E" uniqKey="Hemler M" first="Martin E." last="Hemler">Martin E. Hemler</name><affiliation><mods:affiliation>Tumor Virology Division Dana-Farber Cancer Institute Harvard Medical School Boston, Massachusetts 02115 USA</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:9DC6AA9068FAED2A72A8AB311C67CF6A217681EA</idno><date when="1992" year="1992">1992</date><idno type="doi">10.1016/0092-8674(92)90077-P</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-DZ5Q23KR-Z/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">002634</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">002634</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Distinct cellular functions mediated by different VLA integrin α subunit cytoplasmic domains</title><author><name sortKey="Chan, Bosco M C" sort="Chan, Bosco M C" uniqKey="Chan B" first="Bosco M. C." last="Chan">Bosco M. C. Chan</name><affiliation><mods:affiliation>Tumor Virology Division Dana-Farber Cancer Institute Harvard Medical School Boston, Massachusetts 02115 USA</mods:affiliation></affiliation></author><author><name sortKey="Kassner, Paul D" sort="Kassner, Paul D" uniqKey="Kassner P" first="Paul D." last="Kassner">Paul D. Kassner</name><affiliation><mods:affiliation>Tumor Virology Division Dana-Farber Cancer Institute Harvard Medical School Boston, Massachusetts 02115 USA</mods:affiliation></affiliation></author><author><name sortKey="Schiro, James A" sort="Schiro, James A" uniqKey="Schiro J" first="James A." last="Schiro">James A. Schiro</name><affiliation><mods:affiliation>Division of Dermatology Washington University School of Medicine St. Louis, Missouri 63110 USA</mods:affiliation></affiliation></author><author><name sortKey="Byers, H Randolph" sort="Byers, H Randolph" uniqKey="Byers H" first="H. Randolph" last="Byers">H. Randolph Byers</name><affiliation><mods:affiliation>Department of Pathology Massachusetts General Hospital Boston, Massachusetts 02129 USA</mods:affiliation></affiliation></author><author><name sortKey="Kupper, Thomas S" sort="Kupper, Thomas S" uniqKey="Kupper T" first="Thomas S." last="Kupper">Thomas S. Kupper</name><affiliation><mods:affiliation>Division of Dermatology Washington University School of Medicine St. Louis, Missouri 63110 USA</mods:affiliation></affiliation></author><author><name sortKey="Hemler, Martin E" sort="Hemler, Martin E" uniqKey="Hemler M" first="Martin E." last="Hemler">Martin E. Hemler</name><affiliation><mods:affiliation>Tumor Virology Division Dana-Farber Cancer Institute Harvard Medical School Boston, Massachusetts 02115 USA</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Cell</title><title level="j" type="abbrev">CELL</title><idno type="ISSN">0092-8674</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1992">1992</date><biblScope unit="volume">68</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="1051">1051</biblScope><biblScope unit="page" to="1060">1060</biblScope></imprint><idno type="ISSN">0092-8674</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0092-8674</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acad</term><term>Adhesion</term><term>Amino acids</term><term>Biol</term><term>Cdna</term><term>Cell adhesion</term><term>Cell biol</term><term>Cell migration</term><term>Cell morphology</term><term>Chain cytoplasmic domains</term><term>Chan</term><term>Chem</term><term>Chimeric</term><term>Chimeric cdnas</term><term>Collagen</term><term>Collagen matrices</term><term>Collagen matrix</term><term>Cytoplasmic</term><term>Cytoplasmic domain</term><term>Cytoplasmic domains</term><term>Domain</term><term>Domain functions</term><term>Extracellular</term><term>Extracellular matrix</term><term>Fibronectin</term><term>Fibronectin receptor</term><term>Glycoprotein</term><term>Hemler</term><term>Heterodimer</term><term>Hibbs</term><term>Immunol</term><term>Integrin</term><term>Integrin family</term><term>Integrins</term><term>Laminin</term><term>Ligand</term><term>Ligand binding</term><term>Lymphocyte</term><term>Matrix</term><term>Migration</term><term>Migration rates</term><term>Monoclonal</term><term>Monoclonal antibodies</term><term>Monoclonal antibody</term><term>Natl</term><term>Physical force</term><term>Platelet</term><term>Primary structure</term><term>Proc</term><term>Rdpf</term><term>Rdpf cells</term><term>Receptor</term><term>Ruoslahti</term><term>Solowska</term><term>Stable exertion</term><term>Subunit</term><term>Subunit cytoplasmic domains</term><term>Takada</term><term>Transfectants</term><term>Transfected</term><term>Transmembrane</term><term>Wayner</term><term>Yamada</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: To characterize VLA α subunit cytoplasmic domain functions, unaltered α2 cDNA (called X2C2) and two chimeric cDNAs (called X2C5 and X2C4) were constructed with extracellular α2 domains and cytoplasmic α2, α5, and α4 domains respectively. Upon transfection into rhabdomyosarcoma (RD) cells, each construct yielded comparable expression levels, immunoprecipitation profiles, and avidity for collagen and laminin. However, while RDX2C2 and RDX2C5 transfectants mediated collagen gel contraction, RDX2C4 and a mock transfectant (RDpF) did not. Conversely, only RDX2C4 cells (but not RDX2C2 or RDX2C5) showed enhanced cell migration on collagen and laminin compared with RDpF cells. This indicates markedly differing roles for integrin α subunit cytoplasmic domains in post-ligand binding events. Furthermore, stable exertion of physical force (collagen gel contraction) may involve fundamentally different cellular machinery than the transient adhesion occurring during cell migration. Finally, these findings provide insight into a functional flexibility perhaps resulting from multiple integrins binding to identical ligands.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>cytoplasmic</json:string><json:string>subunit</json:string><json:string>receptor</json:string><json:string>integrin</json:string><json:string>fibronectin</json:string><json:string>biol</json:string><json:string>laminin</json:string><json:string>hemler</json:string><json:string>rdpf</json:string><json:string>cell biol</json:string><json:string>integrins</json:string><json:string>transfectants</json:string><json:string>extracellular</json:string><json:string>matrix</json:string><json:string>cdna</json:string><json:string>cell migration</json:string><json:string>cytoplasmic domains</json:string><json:string>immunol</json:string><json:string>takada</json:string><json:string>cytoplasmic domain</json:string><json:string>transmembrane</json:string><json:string>collagen</json:string><json:string>ligand</json:string><json:string>hibbs</json:string><json:string>solowska</json:string><json:string>chimeric</json:string><json:string>glycoprotein</json:string><json:string>yamada</json:string><json:string>lymphocyte</json:string><json:string>monoclonal</json:string><json:string>rdpf cells</json:string><json:string>ruoslahti</json:string><json:string>acad</json:string><json:string>proc</json:string><json:string>ligand binding</json:string><json:string>transfected</json:string><json:string>adhesion</json:string><json:string>heterodimer</json:string><json:string>chan</json:string><json:string>wayner</json:string><json:string>natl</json:string><json:string>platelet</json:string><json:string>chem</json:string><json:string>migration rates</json:string><json:string>chain cytoplasmic domains</json:string><json:string>monoclonal antibody</json:string><json:string>fibronectin receptor</json:string><json:string>migration</json:string><json:string>physical force</json:string><json:string>integrin family</json:string><json:string>amino acids</json:string><json:string>cell adhesion</json:string><json:string>subunit cytoplasmic domains</json:string><json:string>domain</json:string><json:string>monoclonal antibodies</json:string><json:string>extracellular matrix</json:string><json:string>collagen matrices</json:string><json:string>collagen matrix</json:string><json:string>domain functions</json:string><json:string>cell morphology</json:string><json:string>stable exertion</json:string><json:string>chimeric cdnas</json:string><json:string>primary structure</json:string></teeft></keywords><author><json:item><name>Bosco M.C. Chan</name><affiliations><json:string>Tumor Virology Division Dana-Farber Cancer Institute Harvard Medical School Boston, Massachusetts 02115 USA</json:string></affiliations></json:item><json:item><name>Paul D. Kassner</name><affiliations><json:string>Tumor Virology Division Dana-Farber Cancer Institute Harvard Medical School Boston, Massachusetts 02115 USA</json:string></affiliations></json:item><json:item><name>James A. Schiro</name><affiliations><json:string>Division of Dermatology Washington University School of Medicine St. Louis, Missouri 63110 USA</json:string></affiliations></json:item><json:item><name>H.Randolph Byers</name><affiliations><json:string>Department of Pathology Massachusetts General Hospital Boston, Massachusetts 02129 USA</json:string></affiliations></json:item><json:item><name>Thomas S. Kupper</name><affiliations><json:string>Division of Dermatology Washington University School of Medicine St. Louis, Missouri 63110 USA</json:string></affiliations></json:item><json:item><name>Martin E. Hemler</name><affiliations><json:string>Tumor Virology Division Dana-Farber Cancer Institute Harvard Medical School Boston, Massachusetts 02115 USA</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-DZ5Q23KR-Z</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: To characterize VLA α subunit cytoplasmic domain functions, unaltered α2 cDNA (called X2C2) and two chimeric cDNAs (called X2C5 and X2C4) were constructed with extracellular α2 domains and cytoplasmic α2, α5, and α4 domains respectively. Upon transfection into rhabdomyosarcoma (RD) cells, each construct yielded comparable expression levels, immunoprecipitation profiles, and avidity for collagen and laminin. However, while RDX2C2 and RDX2C5 transfectants mediated collagen gel contraction, RDX2C4 and a mock transfectant (RDpF) did not. Conversely, only RDX2C4 cells (but not RDX2C2 or RDX2C5) showed enhanced cell migration on collagen and laminin compared with RDpF cells. This indicates markedly differing roles for integrin α subunit cytoplasmic domains in post-ligand binding events. Furthermore, stable exertion of physical force (collagen gel contraction) may involve fundamentally different cellular machinery than the transient adhesion occurring during cell migration. Finally, these findings provide insight into a functional flexibility perhaps resulting from multiple integrins binding to identical ligands.</abstract><qualityIndicators><score>8.812</score><pdfWordCount>7514</pdfWordCount><pdfCharCount>46989</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>10</pdfPageCount><pdfPageSize>576 x 792 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>151</abstractWordCount><abstractCharCount>1133</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>Distinct cellular functions mediated by different VLA integrin α subunit cytoplasmic domains</title><pmid><json:string>1547502</json:string></pmid><pii><json:string>0092-8674(92)90077-P</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Proc. Natl. Acad. Sci. USA</title><language><json:string>unknown</json:string></language><volume>85</volume><pages><first>497</first><last>501</last></pages></serie><host><title>Cell</title><language><json:string>unknown</json:string></language><publicationDate>1992</publicationDate><issn><json:string>0092-8674</json:string></issn><pii><json:string>S0092-8674(00)X0282-6</json:string></pii><volume>68</volume><issue>6</issue><pages><first>1051</first><last>1060</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1992</json:string><json:string>1000</json:string></date><geogName></geogName><orgName><json:string>University of Michigan</json:string><json:string>Dermatology Washington University</json:string><json:string>Medical Research Council of Canada</json:string><json:string>Bethesda Research Laboratories</json:string><json:string>National Institute of Dental Research, Bethesda, MD</json:string><json:string>University of Illinois</json:string><json:string>Dynal Co.</json:string><json:string>Nikon Diaphot</json:string><json:string>Department of Pathology Massachusetts General Hospital Eioston, Massachusetts</json:string><json:string>National Institutes of Health</json:string></orgName><orgName_funder><json:string>National Institutes of Health</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>A. Horwitz</json:string><json:string>H. Randolph</json:string><json:string>J. M. Bergelson</json:string><json:string>H. Kleinman</json:string><json:string>Martin E. Hemler</json:string><json:string>Ann Arbor</json:string><json:string>Paul D. Kassner</json:string><json:string>R. W. Finberg</json:string><json:string>Thomas S. Kupper</json:string><json:string>Having</json:string><json:string>James A. Schiro</json:string><json:string>M. Liebert</json:string></persName><placeName><json:string>CA.</json:string><json:string>Richmond</json:string><json:string>CA</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Tsuji et al., 1990</json:string><json:string>Hibbs et al., 1991a, 1991 b</json:string><json:string>Duband et al., 1988</json:string><json:string>Chan et al., 1991 a</json:string><json:string>Hemler et al., 1983</json:string><json:string>Hayashi et al., 1990</json:string><json:string>Wayner et al., 1988</json:string><json:string>Hemler et al., 1987a</json:string><json:string>Davis et al., 1990</json:string><json:string>Kiefel et al., 1969</json:string><json:string>Harris et al., 1981</json:string><json:string>Jaconi et al., 1991</json:string><json:string>Graham et al., 1989</json:string><json:string>Tapley et al., 1989</json:string><json:string>Horwitz et al., 1986</json:string><json:string>Burn et al., 1988</json:string><json:string>Altruda et al., 1990</json:string><json:string>Shimizu et al., 1990b</json:string><json:string>Ruoslahti, 1988</json:string><json:string>Ohashi et al., 1985</json:string><json:string>Lam et al., 1989</json:string><json:string>Byers et al., 1991</json:string><json:string>van Noesel et al., 1988</json:string><json:string>Klein et al., 1991</json:string><json:string>Van Kooyk et al., 1989</json:string><json:string>Sbnchez-Madrid et al., 1986</json:string><json:string>Carey, 1991</json:string><json:string>Argraves et al., 1987</json:string><json:string>Solowska et al., 1991</json:string><json:string>Marcantonio et al., 1990</json:string><json:string>Schwartz et al., 1991</json:string><json:string>Dedhar et al., 1987</json:string><json:string>Shimizu et al., 1990a</json:string><json:string>Languino et al., 1989</json:string><json:string>Pardi et al., 1989</json:string><json:string>Tucker et al., 1985</json:string><json:string>Kavanaugh et al.</json:string><json:string>Li et al., 1987</json:string><json:string>Kramer and Marks, 1989</json:string><json:string>Hibbs et al., 1991b</json:string><json:string>Kearney et al., 1979</json:string><json:string>Takada et al., 1991</json:string><json:string>Reichardt and Tomaselli, 1991</json:string><json:string>Elices et al., 1990</json:string><json:string>Schiro et al., 1991</json:string><json:string>Yamada et al., 1990</json:string><json:string>Pischel et al., 1987</json:string><json:string>Groux et al., 1989</json:string><json:string>Saito et al., 1987</json:string><json:string>Streuli and Bissell, 1990</json:string><json:string>Pircher et al., 1986</json:string><json:string>Chan et al., 1991b</json:string><json:string>Akiyama et al., 1989</json:string><json:string>Dipersio et al., 1991</json:string><json:string>Savill et al., 1990</json:string><json:string>Hibbs et al., 1991 b</json:string><json:string>Elites et al., 1990</json:string><json:string>Hynes, 1987</json:string><json:string>Holers et al., 1989</json:string><json:string>Takada and Hemler, 1989</json:string><json:string>Yuan et al., 1990</json:string><json:string>Roberts et al., 1991</json:string><json:string>Nathan and Sanchez, 1990</json:string><json:string>Fitzgerald et al., 1987</json:string><json:string>Takada et al., 1989</json:string><json:string>Singer et al., 1988</json:string><json:string>Chan et al., 1991a</json:string><json:string>Zylstra et al., 1986</json:string><json:string>Schreiner et al., 1989</json:string><json:string>Tomasek et al., 1982</json:string><json:string>Mueller et al., 1989</json:string><json:string>Tsuji et al., 1991</json:string><json:string>Hemler et al., 1984</json:string><json:string>Wayner and Carter, 1987</json:string><json:string>Hemler, 1990</json:string><json:string>Staatz et al., 1989</json:string><json:string>Dustin and Springer, 1989</json:string><json:string>Bellows et al., 1982</json:string><json:string>Fradet et al., 1984</json:string><json:string>Matsuyama et al., 1989</json:string><json:string>Hemler et al., 1987b</json:string><json:string>Neuhaus et al., 1991</json:string><json:string>Otey et al., 1990</json:string><json:string>Takada et al., 1988</json:string><json:string>Werb et al., 1989</json:string><json:string>Giancotti and Ruoslahti, 1990</json:string><json:string>Aznavoorian et al., 1990</json:string><json:string>Arnaout et al., 1983</json:string><json:string>Blum et al., 1987</json:string><json:string>Kirchhofer et al., 1990</json:string><json:string>Dana et al., 1991</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-DZ5Q23KR-Z</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - cell biology</json:string><json:string>2 - biochemistry & molecular biology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - developmental biology</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - General Biochemistry, Genetics and Molecular Biology</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences medicales</json:string></inist></categories><publicationDate>1992</publicationDate><copyrightDate>1992</copyrightDate><doi><json:string>10.1016/0092-8674(92)90077-P</json:string></doi><id>9DC6AA9068FAED2A72A8AB311C67CF6A217681EA</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-DZ5Q23KR-Z/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-DZ5Q23KR-Z/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-DZ5Q23KR-Z/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a">Distinct cellular functions mediated by different VLA integrin α subunit cytoplasmic domains</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>elsevier</p></licence></availability><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M"></p><date>1992</date></publicationStmt><notesStmt><note type="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note><note type="content">Section title: Article</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Distinct cellular functions mediated by different VLA integrin α subunit cytoplasmic domains</title><author xml:id="author-0000"><persName><forename type="first">Bosco M.C.</forename><surname>Chan</surname></persName><affiliation>Tumor Virology Division Dana-Farber Cancer Institute Harvard Medical School Boston, Massachusetts 02115 USA</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Paul D.</forename><surname>Kassner</surname></persName><affiliation>Tumor Virology Division Dana-Farber Cancer Institute Harvard Medical School Boston, Massachusetts 02115 USA</affiliation></author><author xml:id="author-0002"><persName><forename type="first">James A.</forename><surname>Schiro</surname></persName><affiliation>Division of Dermatology Washington University School of Medicine St. Louis, Missouri 63110 USA</affiliation></author><author xml:id="author-0003"><persName><forename type="first">H.Randolph</forename><surname>Byers</surname></persName><affiliation>Department of Pathology Massachusetts General Hospital Boston, Massachusetts 02129 USA</affiliation></author><author xml:id="author-0004"><persName><forename type="first">Thomas S.</forename><surname>Kupper</surname></persName><affiliation>Division of Dermatology Washington University School of Medicine St. Louis, Missouri 63110 USA</affiliation></author><author xml:id="author-0005"><persName><forename type="first">Martin E.</forename><surname>Hemler</surname></persName><affiliation>Tumor Virology Division Dana-Farber Cancer Institute Harvard Medical School Boston, Massachusetts 02115 USA</affiliation></author><idno type="istex">9DC6AA9068FAED2A72A8AB311C67CF6A217681EA</idno><idno type="ark">ark:/67375/6H6-DZ5Q23KR-Z</idno><idno type="DOI">10.1016/0092-8674(92)90077-P</idno><idno type="PII">0092-8674(92)90077-P</idno></analytic><monogr><title level="j">Cell</title><title level="j" type="abbrev">CELL</title><idno type="pISSN">0092-8674</idno><idno type="PII">S0092-8674(00)X0282-6</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1992"></date><biblScope unit="volume">68</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="1051">1051</biblScope><biblScope unit="page" to="1060">1060</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1992</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: To characterize VLA α subunit cytoplasmic domain functions, unaltered α2 cDNA (called X2C2) and two chimeric cDNAs (called X2C5 and X2C4) were constructed with extracellular α2 domains and cytoplasmic α2, α5, and α4 domains respectively. Upon transfection into rhabdomyosarcoma (RD) cells, each construct yielded comparable expression levels, immunoprecipitation profiles, and avidity for collagen and laminin. However, while RDX2C2 and RDX2C5 transfectants mediated collagen gel contraction, RDX2C4 and a mock transfectant (RDpF) did not. Conversely, only RDX2C4 cells (but not RDX2C2 or RDX2C5) showed enhanced cell migration on collagen and laminin compared with RDpF cells. This indicates markedly differing roles for integrin α subunit cytoplasmic domains in post-ligand binding events. Furthermore, stable exertion of physical force (collagen gel contraction) may involve fundamentally different cellular machinery than the transient adhesion occurring during cell migration. Finally, these findings provide insight into a functional flexibility perhaps resulting from multiple integrins binding to identical ligands.</p></abstract></profileDesc><revisionDesc><change when="1991-12-09">Modified</change><change when="1992">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-DZ5Q23KR-Z/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>CELL</jid><aid>9290077P</aid><ce:pii>0092-8674(92)90077-P</ce:pii><ce:doi>10.1016/0092-8674(92)90077-P</ce:doi><ce:copyright type="unknown" year="1992"></ce:copyright></item-info><head><ce:dochead><ce:textfn>Article</ce:textfn></ce:dochead><ce:title>Distinct cellular functions mediated by different VLA integrin α subunit cytoplasmic domains</ce:title><ce:author-group><ce:author><ce:given-name>Bosco M.C.</ce:given-name><ce:surname>Chan</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>★</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Paul D.</ce:given-name><ce:surname>Kassner</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>★</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>James A.</ce:given-name><ce:surname>Schiro</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>†</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>H.Randolph</ce:given-name><ce:surname>Byers</ce:surname><ce:cross-ref refid="AFF3"><ce:sup>‡</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Thomas S.</ce:given-name><ce:surname>Kupper</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>†</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Martin E.</ce:given-name><ce:surname>Hemler</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>★</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Tumor Virology Division Dana-Farber Cancer Institute Harvard Medical School Boston, Massachusetts 02115 USA</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>Division of Dermatology Washington University School of Medicine St. Louis, Missouri 63110 USA</ce:textfn></ce:affiliation><ce:affiliation id="AFF3"><ce:label>c</ce:label><ce:textfn>Department of Pathology Massachusetts General Hospital Boston, Massachusetts 02129 USA</ce:textfn></ce:affiliation></ce:author-group><ce:date-received day="22" month="10" year="1991"></ce:date-received><ce:date-revised day="9" month="12" year="1991"></ce:date-revised><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>To characterize VLA α subunit cytoplasmic domain functions, unaltered <ce:italic>α</ce:italic><ce:sup>2</ce:sup> cDNA (called X2C2) and two chimeric cDNAs (called X2C5 and X2C4) were constructed with extracellular <ce:italic>α</ce:italic><ce:sup>2</ce:sup> domains and cytoplasmic <ce:italic>α</ce:italic><ce:sup>2</ce:sup>, <ce:italic>α</ce:italic><ce:sup>5</ce:sup>, and <ce:italic>α</ce:italic><ce:sup>4</ce:sup> domains respectively. Upon transfection into rhabdomyosarcoma (RD) cells, each construct yielded comparable expression levels, immunoprecipitation profiles, and avidity for collagen and laminin. However, while RDX2C2 and RDX2C5 transfectants mediated collagen gel contraction, RDX2C4 and a mock transfectant (RDpF) did not. Conversely, only RDX2C4 cells (but not RDX2C2 or RDX2C5) showed enhanced cell migration on collagen and laminin compared with RDpF cells. This indicates markedly differing roles for integrin α subunit cytoplasmic domains in post-ligand binding events. Furthermore, stable exertion of physical force (collagen gel contraction) may involve fundamentally different cellular machinery than the transient adhesion occurring during cell migration. Finally, these findings provide insight into a functional flexibility perhaps resulting from multiple integrins binding to identical ligands.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Distinct cellular functions mediated by different VLA integrin α subunit cytoplasmic domains</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Distinct cellular functions mediated by different VLA integrin α subunit cytoplasmic domains</title></titleInfo><name type="personal"><namePart type="given">Bosco M.C.</namePart><namePart type="family">Chan</namePart><affiliation>Tumor Virology Division Dana-Farber Cancer Institute Harvard Medical School Boston, Massachusetts 02115 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Paul D.</namePart><namePart type="family">Kassner</namePart><affiliation>Tumor Virology Division Dana-Farber Cancer Institute Harvard Medical School Boston, Massachusetts 02115 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">James A.</namePart><namePart type="family">Schiro</namePart><affiliation>Division of Dermatology Washington University School of Medicine St. Louis, Missouri 63110 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">H.Randolph</namePart><namePart type="family">Byers</namePart><affiliation>Department of Pathology Massachusetts General Hospital Boston, Massachusetts 02129 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Thomas S.</namePart><namePart type="family">Kupper</namePart><affiliation>Division of Dermatology Washington University School of Medicine St. Louis, Missouri 63110 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Martin E.</namePart><namePart type="family">Hemler</namePart><affiliation>Tumor Virology Division Dana-Farber Cancer Institute Harvard Medical School Boston, Massachusetts 02115 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1992</dateIssued><dateModified encoding="w3cdtf">1991-12-09</dateModified><copyrightDate encoding="w3cdtf">1992</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: To characterize VLA α subunit cytoplasmic domain functions, unaltered α2 cDNA (called X2C2) and two chimeric cDNAs (called X2C5 and X2C4) were constructed with extracellular α2 domains and cytoplasmic α2, α5, and α4 domains respectively. Upon transfection into rhabdomyosarcoma (RD) cells, each construct yielded comparable expression levels, immunoprecipitation profiles, and avidity for collagen and laminin. However, while RDX2C2 and RDX2C5 transfectants mediated collagen gel contraction, RDX2C4 and a mock transfectant (RDpF) did not. Conversely, only RDX2C4 cells (but not RDX2C2 or RDX2C5) showed enhanced cell migration on collagen and laminin compared with RDpF cells. This indicates markedly differing roles for integrin α subunit cytoplasmic domains in post-ligand binding events. Furthermore, stable exertion of physical force (collagen gel contraction) may involve fundamentally different cellular machinery than the transient adhesion occurring during cell migration. Finally, these findings provide insight into a functional flexibility perhaps resulting from multiple integrins binding to identical ligands.</abstract><note type="content">Section title: Article</note><relatedItem type="host"><titleInfo><title>Cell</title></titleInfo><titleInfo type="abbreviated"><title>CELL</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1992</dateIssued></originInfo><identifier type="ISSN">0092-8674</identifier><identifier type="PII">S0092-8674(00)X0282-6</identifier><part><date>1992</date><detail type="volume"><number>68</number><caption>vol.</caption></detail><detail type="issue"><number>6</number><caption>no.</caption></detail><extent unit="issue-pages"><start>995</start><end>1175</end></extent><extent unit="pages"><start>1051</start><end>1060</end></extent></part></relatedItem><identifier type="istex">9DC6AA9068FAED2A72A8AB311C67CF6A217681EA</identifier><identifier type="ark">ark:/67375/6H6-DZ5Q23KR-Z</identifier><identifier type="DOI">10.1016/0092-8674(92)90077-P</identifier><identifier type="PII">0092-8674(92)90077-P</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-DZ5Q23KR-Z/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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