The heterotrimeric laminin coiled-coil domain exerts anti-adhesive effects and induces a pro-invasive phenotype.
Laminins are large heterotrimeric cross-shaped extracellular matrix glycoproteins with terminal globular domains and a coiled-coil region through which the three chains are assembled and covalently linked. Laminins are key components of basement membranes, and they serve as attachment sites for cell...
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2012-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3378518?pdf=render |
| _version_ | 1798045552687972352 |
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| author | Patricia Santos-Valle Irene Guijarro-Muñoz Angel M Cuesta Vanesa Alonso-Camino Maider Villate Ana Alvarez-Cienfuegos Francisco J Blanco Laura Sanz Luis Alvarez-Vallina |
| author_facet | Patricia Santos-Valle Irene Guijarro-Muñoz Angel M Cuesta Vanesa Alonso-Camino Maider Villate Ana Alvarez-Cienfuegos Francisco J Blanco Laura Sanz Luis Alvarez-Vallina |
| author_sort | Patricia Santos-Valle |
| collection | DOAJ |
| description | Laminins are large heterotrimeric cross-shaped extracellular matrix glycoproteins with terminal globular domains and a coiled-coil region through which the three chains are assembled and covalently linked. Laminins are key components of basement membranes, and they serve as attachment sites for cell adhesion, migration and proliferation. In this work, we produced a recombinant fragment comprising the entire laminin coiled-coil of the α1-, β1-, and γ1-chains that assemble into a stable heterotrimeric coiled-coil structure independently of the rest of the molecule. This domain was biologically active and not only failed to serve as a substrate for cell attachment, spreading and focal adhesion formation but also inhibited cell adhesion to laminin when added to cells in a soluble form at the time of seeding. Furthermore, gene array expression profiling in cells cultured in the presence of the laminin coiled-coil domain revealed up-regulation of genes involved in cell motility and invasion. These findings were confirmed by real-time quantitative PCR and zymography assays. In conclusion, this study shows for the first time that the laminin coiled-coil domain displays anti-adhesive functions and has potential implications for cell migration during matrix remodeling. |
| first_indexed | 2024-04-11T23:22:47Z |
| format | Article |
| id | doaj.art-086ca92b49034230814807a15afb4bf3 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-04-11T23:22:47Z |
| publishDate | 2012-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-086ca92b49034230814807a15afb4bf32022-12-22T03:57:24ZengPublic Library of Science (PLoS)PLoS ONE1932-62032012-01-0176e3909710.1371/journal.pone.0039097The heterotrimeric laminin coiled-coil domain exerts anti-adhesive effects and induces a pro-invasive phenotype.Patricia Santos-ValleIrene Guijarro-MuñozAngel M CuestaVanesa Alonso-CaminoMaider VillateAna Alvarez-CienfuegosFrancisco J BlancoLaura SanzLuis Alvarez-VallinaLaminins are large heterotrimeric cross-shaped extracellular matrix glycoproteins with terminal globular domains and a coiled-coil region through which the three chains are assembled and covalently linked. Laminins are key components of basement membranes, and they serve as attachment sites for cell adhesion, migration and proliferation. In this work, we produced a recombinant fragment comprising the entire laminin coiled-coil of the α1-, β1-, and γ1-chains that assemble into a stable heterotrimeric coiled-coil structure independently of the rest of the molecule. This domain was biologically active and not only failed to serve as a substrate for cell attachment, spreading and focal adhesion formation but also inhibited cell adhesion to laminin when added to cells in a soluble form at the time of seeding. Furthermore, gene array expression profiling in cells cultured in the presence of the laminin coiled-coil domain revealed up-regulation of genes involved in cell motility and invasion. These findings were confirmed by real-time quantitative PCR and zymography assays. In conclusion, this study shows for the first time that the laminin coiled-coil domain displays anti-adhesive functions and has potential implications for cell migration during matrix remodeling.http://europepmc.org/articles/PMC3378518?pdf=render |
| spellingShingle | Patricia Santos-Valle Irene Guijarro-Muñoz Angel M Cuesta Vanesa Alonso-Camino Maider Villate Ana Alvarez-Cienfuegos Francisco J Blanco Laura Sanz Luis Alvarez-Vallina The heterotrimeric laminin coiled-coil domain exerts anti-adhesive effects and induces a pro-invasive phenotype. PLoS ONE |
| title | The heterotrimeric laminin coiled-coil domain exerts anti-adhesive effects and induces a pro-invasive phenotype. |
| title_full | The heterotrimeric laminin coiled-coil domain exerts anti-adhesive effects and induces a pro-invasive phenotype. |
| title_fullStr | The heterotrimeric laminin coiled-coil domain exerts anti-adhesive effects and induces a pro-invasive phenotype. |
| title_full_unstemmed | The heterotrimeric laminin coiled-coil domain exerts anti-adhesive effects and induces a pro-invasive phenotype. |
| title_short | The heterotrimeric laminin coiled-coil domain exerts anti-adhesive effects and induces a pro-invasive phenotype. |
| title_sort | heterotrimeric laminin coiled coil domain exerts anti adhesive effects and induces a pro invasive phenotype |
| url | http://europepmc.org/articles/PMC3378518?pdf=render |
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