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Substrate stiffness regulates solubility of cellular vimentin
The intermediate filament protein vimentin is involved in the regulation of cell behavior, morphology, and mechanical properties. Previous studies using cells cultured on glass or plastic substrates showed that vimentin is largely insoluble. Although substrate stiffness was shown to alter many aspec...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3873896/ https://www.ncbi.nlm.nih.gov/pubmed/24173714 http://dx.doi.org/10.1091/mbc.E13-06-0326 |
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author | Murray, Maria E. Mendez, Melissa G. Janmey, Paul A. |
author_facet | Murray, Maria E. Mendez, Melissa G. Janmey, Paul A. |
author_sort | Murray, Maria E. |
collection | PubMed |
description | The intermediate filament protein vimentin is involved in the regulation of cell behavior, morphology, and mechanical properties. Previous studies using cells cultured on glass or plastic substrates showed that vimentin is largely insoluble. Although substrate stiffness was shown to alter many aspects of cell behavior, changes in vimentin organization were not reported. Our results show for the first time that mesenchymal stem cells (hMSCs), endothelial cells, and fibroblasts cultured on different-stiffness substrates exhibit biphasic changes in vimentin detergent solubility, which increases from nearly 0 to 67% in hMSCs coincident with increases in cell spreading and membrane ruffling. When imaged, the detergent-soluble vimentin appears to consist of small fragments the length of one or several unit-length filaments. Vimentin detergent solubility decreases when these cells are subjected to serum starvation, allowed to form cell–cell contacts, after microtubule disruption, or inhibition of Rac1, Rho-activated kinase, or p21-activated kinase. Inhibiting myosin or actin assembly increases vimentin solubility on rigid substrates. These data suggest that in the mechanical environment in vivo, vimentin is more dynamic than previously reported and its assembly state is sensitive to stimuli that alter cellular tension and morphology. |
format | Online Article Text |
id | pubmed-3873896 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-38738962014-03-16 Substrate stiffness regulates solubility of cellular vimentin Murray, Maria E. Mendez, Melissa G. Janmey, Paul A. Mol Biol Cell Articles The intermediate filament protein vimentin is involved in the regulation of cell behavior, morphology, and mechanical properties. Previous studies using cells cultured on glass or plastic substrates showed that vimentin is largely insoluble. Although substrate stiffness was shown to alter many aspects of cell behavior, changes in vimentin organization were not reported. Our results show for the first time that mesenchymal stem cells (hMSCs), endothelial cells, and fibroblasts cultured on different-stiffness substrates exhibit biphasic changes in vimentin detergent solubility, which increases from nearly 0 to 67% in hMSCs coincident with increases in cell spreading and membrane ruffling. When imaged, the detergent-soluble vimentin appears to consist of small fragments the length of one or several unit-length filaments. Vimentin detergent solubility decreases when these cells are subjected to serum starvation, allowed to form cell–cell contacts, after microtubule disruption, or inhibition of Rac1, Rho-activated kinase, or p21-activated kinase. Inhibiting myosin or actin assembly increases vimentin solubility on rigid substrates. These data suggest that in the mechanical environment in vivo, vimentin is more dynamic than previously reported and its assembly state is sensitive to stimuli that alter cellular tension and morphology. The American Society for Cell Biology 2014-01-01 /pmc/articles/PMC3873896/ /pubmed/24173714 http://dx.doi.org/10.1091/mbc.E13-06-0326 Text en © 2014 Murray 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 Murray, Maria E. Mendez, Melissa G. Janmey, Paul A. Substrate stiffness regulates solubility of cellular vimentin |
title | Substrate stiffness regulates solubility of cellular vimentin |
title_full | Substrate stiffness regulates solubility of cellular vimentin |
title_fullStr | Substrate stiffness regulates solubility of cellular vimentin |
title_full_unstemmed | Substrate stiffness regulates solubility of cellular vimentin |
title_short | Substrate stiffness regulates solubility of cellular vimentin |
title_sort | substrate stiffness regulates solubility of cellular vimentin |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3873896/ https://www.ncbi.nlm.nih.gov/pubmed/24173714 http://dx.doi.org/10.1091/mbc.E13-06-0326 |
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