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Laminin 511 partners with laminin 332 to mediate directional migration of Madin–Darby canine kidney epithelial cells

Sustained directional migration of epithelial cells is essential for regeneration of injured epithelia. Front–rear polarity of migrating cells is determined by local activation of a signaling network involving Cdc42 and other factors in response to spatial cues from the environment, the nature of wh...

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Autores principales: Greciano, Patricia G., Moyano, Jose V., Buschmann, Mary M., Tang, Jun, Lu, Yue, Rudnicki, Jean, Manninen, Aki, Matlin, Karl S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3248892/
https://www.ncbi.nlm.nih.gov/pubmed/22031290
http://dx.doi.org/10.1091/mbc.E11-08-0718
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author Greciano, Patricia G.
Moyano, Jose V.
Buschmann, Mary M.
Tang, Jun
Lu, Yue
Rudnicki, Jean
Manninen, Aki
Matlin, Karl S.
author_facet Greciano, Patricia G.
Moyano, Jose V.
Buschmann, Mary M.
Tang, Jun
Lu, Yue
Rudnicki, Jean
Manninen, Aki
Matlin, Karl S.
author_sort Greciano, Patricia G.
collection PubMed
description Sustained directional migration of epithelial cells is essential for regeneration of injured epithelia. Front–rear polarity of migrating cells is determined by local activation of a signaling network involving Cdc42 and other factors in response to spatial cues from the environment, the nature of which are obscure. We examined the roles of laminin (LM)-511 and LM-332, two structurally different laminin isoforms, in the migration of Madin–Darby canine kidney cells by suppressing expression of their α subunits using RNA interference. We determined that knockdown of LM-511 inhibits directional migration and destabilizes cell–cell contacts, in part by disturbing the localization and activity of the polarization machinery. Suppression of integrin α3, a laminin receptor subunit, in cells synthesizing normal amounts of both laminins has a similar effect as knockdown of LM-511. Surprisingly, simultaneous suppression of both laminin α5 and laminin α3 restores directional migration and cell–cell contact stability, suggesting that cells recognize a haptotactic gradient formed by a combination of laminins.
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spelling pubmed-32488922012-03-16 Laminin 511 partners with laminin 332 to mediate directional migration of Madin–Darby canine kidney epithelial cells Greciano, Patricia G. Moyano, Jose V. Buschmann, Mary M. Tang, Jun Lu, Yue Rudnicki, Jean Manninen, Aki Matlin, Karl S. Mol Biol Cell Articles Sustained directional migration of epithelial cells is essential for regeneration of injured epithelia. Front–rear polarity of migrating cells is determined by local activation of a signaling network involving Cdc42 and other factors in response to spatial cues from the environment, the nature of which are obscure. We examined the roles of laminin (LM)-511 and LM-332, two structurally different laminin isoforms, in the migration of Madin–Darby canine kidney cells by suppressing expression of their α subunits using RNA interference. We determined that knockdown of LM-511 inhibits directional migration and destabilizes cell–cell contacts, in part by disturbing the localization and activity of the polarization machinery. Suppression of integrin α3, a laminin receptor subunit, in cells synthesizing normal amounts of both laminins has a similar effect as knockdown of LM-511. Surprisingly, simultaneous suppression of both laminin α5 and laminin α3 restores directional migration and cell–cell contact stability, suggesting that cells recognize a haptotactic gradient formed by a combination of laminins. The American Society for Cell Biology 2012-01-01 /pmc/articles/PMC3248892/ /pubmed/22031290 http://dx.doi.org/10.1091/mbc.E11-08-0718 Text en © 2012 Greciano et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology.
spellingShingle Articles
Greciano, Patricia G.
Moyano, Jose V.
Buschmann, Mary M.
Tang, Jun
Lu, Yue
Rudnicki, Jean
Manninen, Aki
Matlin, Karl S.
Laminin 511 partners with laminin 332 to mediate directional migration of Madin–Darby canine kidney epithelial cells
title Laminin 511 partners with laminin 332 to mediate directional migration of Madin–Darby canine kidney epithelial cells
title_full Laminin 511 partners with laminin 332 to mediate directional migration of Madin–Darby canine kidney epithelial cells
title_fullStr Laminin 511 partners with laminin 332 to mediate directional migration of Madin–Darby canine kidney epithelial cells
title_full_unstemmed Laminin 511 partners with laminin 332 to mediate directional migration of Madin–Darby canine kidney epithelial cells
title_short Laminin 511 partners with laminin 332 to mediate directional migration of Madin–Darby canine kidney epithelial cells
title_sort laminin 511 partners with laminin 332 to mediate directional migration of madin–darby canine kidney epithelial cells
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3248892/
https://www.ncbi.nlm.nih.gov/pubmed/22031290
http://dx.doi.org/10.1091/mbc.E11-08-0718
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