MersV1, Main, Exploration, bibRecord, 004777

Distinct cellular functions mediated by different VLA integrin α subunit cytoplasmic domains

Identifieur interne : 004777 ( Main/Exploration ); précédent : 004776; suivant : 004778

Distinct cellular functions mediated by different VLA integrin α subunit cytoplasmic domains

Auteurs : Bosco M. C. Chan [États-Unis] ; Paul D. Kassner [États-Unis] ; James A. Schiro [États-Unis] ; H. Randolph Byers [États-Unis] ; Thomas S. Kupper [États-Unis] ; Martin E. Hemler [États-Unis]

Source :

Cell [ 0092-8674 ] ; 1992.

RBID : ISTEX:9DC6AA9068FAED2A72A8AB311C67CF6A217681EA

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:

https://api.istex.fr/ark:/67375/6H6-DZ5Q23KR-Z/fulltext.pdf

DOI: 10.1016/0092-8674(92)90077-P

Affiliations:

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Le document en format XML

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<author><name sortKey="Kupper, Thomas S" sort="Kupper, Thomas S" uniqKey="Kupper T" first="Thomas S." last="Kupper">Thomas S. Kupper</name>
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<author><name sortKey="Hemler, Martin E" sort="Hemler, Martin E" uniqKey="Hemler M" first="Martin E." last="Hemler">Martin E. Hemler</name>
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<author><name sortKey="Hemler, Martin E" sort="Hemler, Martin E" uniqKey="Hemler M" first="Martin E." last="Hemler">Martin E. Hemler</name>
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<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>
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<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>
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<name sortKey="Byers, H Randolph" sort="Byers, H Randolph" uniqKey="Byers H" first="H. Randolph" last="Byers">H. Randolph Byers</name>
<name sortKey="Hemler, Martin E" sort="Hemler, Martin E" uniqKey="Hemler M" first="Martin E." last="Hemler">Martin E. Hemler</name>
<name sortKey="Kassner, Paul D" sort="Kassner, Paul D" uniqKey="Kassner P" first="Paul D." last="Kassner">Paul D. Kassner</name>
<name sortKey="Kupper, Thomas S" sort="Kupper, Thomas S" uniqKey="Kupper T" first="Thomas S." last="Kupper">Thomas S. Kupper</name>
<name sortKey="Schiro, James A" sort="Schiro, James A" uniqKey="Schiro J" first="James A." last="Schiro">James A. Schiro</name>
</country>
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Distinct cellular functions mediated by different VLA integrin α subunit cytoplasmic domains

Distinct cellular functions mediated by different VLA integrin α subunit cytoplasmic domains

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri