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Fibulin-4 deposition requires EMILIN-1 in the extracellular matrix of osteoblasts
Tissue microenvironments formed by extracellular matrix networks play an important role in regulating tissue structure and function. Extracellular microfibrillar networks composed of fibrillins and their associated ligands such as LTBPs, fibulins, and EMILINs are of particular interest in this regar...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5514116/ https://www.ncbi.nlm.nih.gov/pubmed/28717224 http://dx.doi.org/10.1038/s41598-017-05835-7 |
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author | Schiavinato, Alvise Keene, Douglas R. Imhof, Thomas Doliana, Roberto Sasaki, Takako Sengle, Gerhard |
author_facet | Schiavinato, Alvise Keene, Douglas R. Imhof, Thomas Doliana, Roberto Sasaki, Takako Sengle, Gerhard |
author_sort | Schiavinato, Alvise |
collection | PubMed |
description | Tissue microenvironments formed by extracellular matrix networks play an important role in regulating tissue structure and function. Extracellular microfibrillar networks composed of fibrillins and their associated ligands such as LTBPs, fibulins, and EMILINs are of particular interest in this regard since they provide a specialized cellular microenvironment guiding proper morphology and functional behavior of specialized cell types. To understand how cellular microenvironments composed of intricate microfibrillar networks influence cell fate decisions in a contextual manner, more information about the spatiotemporal localization, deposition, and function of their components is required. By employing confocal immunofluorescence and electron microscopy we investigated the localization and extracellular matrix deposition of EMILIN-1 and -2 in tissues of the skeletal system such as cartilage and bone as well as in in vitro cultures of osteoblasts. We found that upon RNAi mediated depletion of EMILIN-1 in primary calvarial osteoblasts and MC3T3-E1 cells only fibulin-4 matrix deposition was lost while other fibulin family members or LTBPs remained unaffected. Immunoprecipitation and ELISA-style binding assays confirmed a direct interaction between EMILIN-1 and fibulin-4. Our data suggest a new function for EMILIN-1 which implies the guidance of linear fibulin-4 matrix deposition and thereby fibulin-4 fiber formation. |
format | Online Article Text |
id | pubmed-5514116 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-55141162017-07-19 Fibulin-4 deposition requires EMILIN-1 in the extracellular matrix of osteoblasts Schiavinato, Alvise Keene, Douglas R. Imhof, Thomas Doliana, Roberto Sasaki, Takako Sengle, Gerhard Sci Rep Article Tissue microenvironments formed by extracellular matrix networks play an important role in regulating tissue structure and function. Extracellular microfibrillar networks composed of fibrillins and their associated ligands such as LTBPs, fibulins, and EMILINs are of particular interest in this regard since they provide a specialized cellular microenvironment guiding proper morphology and functional behavior of specialized cell types. To understand how cellular microenvironments composed of intricate microfibrillar networks influence cell fate decisions in a contextual manner, more information about the spatiotemporal localization, deposition, and function of their components is required. By employing confocal immunofluorescence and electron microscopy we investigated the localization and extracellular matrix deposition of EMILIN-1 and -2 in tissues of the skeletal system such as cartilage and bone as well as in in vitro cultures of osteoblasts. We found that upon RNAi mediated depletion of EMILIN-1 in primary calvarial osteoblasts and MC3T3-E1 cells only fibulin-4 matrix deposition was lost while other fibulin family members or LTBPs remained unaffected. Immunoprecipitation and ELISA-style binding assays confirmed a direct interaction between EMILIN-1 and fibulin-4. Our data suggest a new function for EMILIN-1 which implies the guidance of linear fibulin-4 matrix deposition and thereby fibulin-4 fiber formation. Nature Publishing Group UK 2017-07-17 /pmc/articles/PMC5514116/ /pubmed/28717224 http://dx.doi.org/10.1038/s41598-017-05835-7 Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Schiavinato, Alvise Keene, Douglas R. Imhof, Thomas Doliana, Roberto Sasaki, Takako Sengle, Gerhard Fibulin-4 deposition requires EMILIN-1 in the extracellular matrix of osteoblasts |
title | Fibulin-4 deposition requires EMILIN-1 in the extracellular matrix of osteoblasts |
title_full | Fibulin-4 deposition requires EMILIN-1 in the extracellular matrix of osteoblasts |
title_fullStr | Fibulin-4 deposition requires EMILIN-1 in the extracellular matrix of osteoblasts |
title_full_unstemmed | Fibulin-4 deposition requires EMILIN-1 in the extracellular matrix of osteoblasts |
title_short | Fibulin-4 deposition requires EMILIN-1 in the extracellular matrix of osteoblasts |
title_sort | fibulin-4 deposition requires emilin-1 in the extracellular matrix of osteoblasts |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5514116/ https://www.ncbi.nlm.nih.gov/pubmed/28717224 http://dx.doi.org/10.1038/s41598-017-05835-7 |
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