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Microvesicles shed from fibroblasts act as metalloproteinase carriers in a 3-D collagen matrix
This study shows that fibroblasts migrating into a collagen matrix release numerous microvesicles into the surrounding medium. By spreading in regions of the matrix far distant from cells of origin, microvesicles carry metalloproteinase 9 (MMP-9) to act upon the collagen fibrils. As a result, the co...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
SAGE Publications
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5548308/ https://www.ncbi.nlm.nih.gov/pubmed/28936262 http://dx.doi.org/10.1177/1849454416663660 |
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author | Laghezza Masci, Valentina Taddei, Anna Rita Gambellini, Gabriella Giorgi, Franco Fausto, Anna Maria |
author_facet | Laghezza Masci, Valentina Taddei, Anna Rita Gambellini, Gabriella Giorgi, Franco Fausto, Anna Maria |
author_sort | Laghezza Masci, Valentina |
collection | PubMed |
description | This study shows that fibroblasts migrating into a collagen matrix release numerous microvesicles into the surrounding medium. By spreading in regions of the matrix far distant from cells of origin, microvesicles carry metalloproteinase 9 (MMP-9) to act upon the collagen fibrils. As a result, the collagen matrix is gradually transformed from a laminar to a fibrillar type of architecture. As shown by western blots and gelatin zymography, MMP-9 is secreted as a 92 kDa precursor and activated upon release of 82 kDa product into the culture medium. Activation is more efficient under three-dimensional than in two-dimensional culturing conditions. While MMP-9 labeling is associated with intraluminal vesicles clustered inside the microvesicles, the microvesicle’s integrin β1 marker is bound to the outer membrane. The intraluminal vesicles are recruited from the cortical cytoplasm and eventually released following uploading inside the microvesicle. Here, we propose that fusion of the intraluminal vesicles with the outer microvesicle’s membrane could work as a mechanism controlling the extent to which MMP-9 is first activated and then released extracellularly. |
format | Online Article Text |
id | pubmed-5548308 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | SAGE Publications |
record_format | MEDLINE/PubMed |
spelling | pubmed-55483082017-09-21 Microvesicles shed from fibroblasts act as metalloproteinase carriers in a 3-D collagen matrix Laghezza Masci, Valentina Taddei, Anna Rita Gambellini, Gabriella Giorgi, Franco Fausto, Anna Maria J Circ Biomark Research Article This study shows that fibroblasts migrating into a collagen matrix release numerous microvesicles into the surrounding medium. By spreading in regions of the matrix far distant from cells of origin, microvesicles carry metalloproteinase 9 (MMP-9) to act upon the collagen fibrils. As a result, the collagen matrix is gradually transformed from a laminar to a fibrillar type of architecture. As shown by western blots and gelatin zymography, MMP-9 is secreted as a 92 kDa precursor and activated upon release of 82 kDa product into the culture medium. Activation is more efficient under three-dimensional than in two-dimensional culturing conditions. While MMP-9 labeling is associated with intraluminal vesicles clustered inside the microvesicles, the microvesicle’s integrin β1 marker is bound to the outer membrane. The intraluminal vesicles are recruited from the cortical cytoplasm and eventually released following uploading inside the microvesicle. Here, we propose that fusion of the intraluminal vesicles with the outer microvesicle’s membrane could work as a mechanism controlling the extent to which MMP-9 is first activated and then released extracellularly. SAGE Publications 2016-11-07 /pmc/articles/PMC5548308/ /pubmed/28936262 http://dx.doi.org/10.1177/1849454416663660 Text en © The Author(s) 2016 http://creativecommons.org/licenses/by-nc/3.0/ This article is distributed under the terms of the Creative Commons Attribution-NonCommercial 3.0 License (http://www.creativecommons.org/licenses/by-nc/3.0/) which permits non-commercial use, reproduction and distribution of the work without further permission provided the original work is attributed as specified on the SAGE and Open Access pages (https://us.sagepub.com/en-us/nam/open-access-at-sage). |
spellingShingle | Research Article Laghezza Masci, Valentina Taddei, Anna Rita Gambellini, Gabriella Giorgi, Franco Fausto, Anna Maria Microvesicles shed from fibroblasts act as metalloproteinase carriers in a 3-D collagen matrix |
title | Microvesicles shed from fibroblasts act as metalloproteinase carriers in a 3-D collagen matrix |
title_full | Microvesicles shed from fibroblasts act as metalloproteinase carriers in a 3-D collagen matrix |
title_fullStr | Microvesicles shed from fibroblasts act as metalloproteinase carriers in a 3-D collagen matrix |
title_full_unstemmed | Microvesicles shed from fibroblasts act as metalloproteinase carriers in a 3-D collagen matrix |
title_short | Microvesicles shed from fibroblasts act as metalloproteinase carriers in a 3-D collagen matrix |
title_sort | microvesicles shed from fibroblasts act as metalloproteinase carriers in a 3-d collagen matrix |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5548308/ https://www.ncbi.nlm.nih.gov/pubmed/28936262 http://dx.doi.org/10.1177/1849454416663660 |
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