Fibulin-4 deposition requires EMILIN-1 in the extracellular matrix of osteoblasts

Abstract 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 t...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Alvise Schiavinato, Douglas R. Keene, Thomas Imhof, Roberto Doliana, Takako Sasaki, Gerhard Sengle
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/4e2df407579f405a88492894bdb5b824
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:4e2df407579f405a88492894bdb5b824
record_format	dspace
spelling	oai:doaj.org-article:4e2df407579f405a88492894bdb5b8242021-12-02T12:32:30ZFibulin-4 deposition requires EMILIN-1 in the extracellular matrix of osteoblasts10.1038/s41598-017-05835-72045-2322https://doaj.org/article/4e2df407579f405a88492894bdb5b8242017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-05835-7https://doaj.org/toc/2045-2322Abstract 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.Alvise SchiavinatoDouglas R. KeeneThomas ImhofRoberto DolianaTakako SasakiGerhard SengleNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-12 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Alvise Schiavinato Douglas R. Keene Thomas Imhof Roberto Doliana Takako Sasaki Gerhard Sengle Fibulin-4 deposition requires EMILIN-1 in the extracellular matrix of osteoblasts
description	Abstract 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	article
author	Alvise Schiavinato Douglas R. Keene Thomas Imhof Roberto Doliana Takako Sasaki Gerhard Sengle
author_facet	Alvise Schiavinato Douglas R. Keene Thomas Imhof Roberto Doliana Takako Sasaki Gerhard Sengle
author_sort	Alvise Schiavinato
title	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_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_sort	fibulin-4 deposition requires emilin-1 in the extracellular matrix of osteoblasts
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/4e2df407579f405a88492894bdb5b824
work_keys_str_mv	AT alviseschiavinato fibulin4depositionrequiresemilin1intheextracellularmatrixofosteoblasts AT douglasrkeene fibulin4depositionrequiresemilin1intheextracellularmatrixofosteoblasts AT thomasimhof fibulin4depositionrequiresemilin1intheextracellularmatrixofosteoblasts AT robertodoliana fibulin4depositionrequiresemilin1intheextracellularmatrixofosteoblasts AT takakosasaki fibulin4depositionrequiresemilin1intheextracellularmatrixofosteoblasts AT gerhardsengle fibulin4depositionrequiresemilin1intheextracellularmatrixofosteoblasts
_version_	1718394034254249984

Fibulin-4 deposition requires EMILIN-1 in the extracellular matrix of osteoblasts

Ejemplares similares