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The role of fibrillin and microfibril binding proteins in elastin and elastic fibre assembly

Fibrillin is a large evolutionarily ancient extracellular glycoprotein that assembles to form beaded microfibrils which are essential components of most extracellular matrices. Fibrillin microfibrils have specific biomechanical properties to endow animal tissues with limited elasticity, a fundamenta...

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Autores principales: Godwin, Alan R.F., Singh, Mukti, Lockhart-Cairns, Michael P., Alanazi, Yasmene F., Cain, Stuart A., Baldock, Clair
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6943813/
https://www.ncbi.nlm.nih.gov/pubmed/31226403
http://dx.doi.org/10.1016/j.matbio.2019.06.006
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author Godwin, Alan R.F.
Singh, Mukti
Lockhart-Cairns, Michael P.
Alanazi, Yasmene F.
Cain, Stuart A.
Baldock, Clair
author_facet Godwin, Alan R.F.
Singh, Mukti
Lockhart-Cairns, Michael P.
Alanazi, Yasmene F.
Cain, Stuart A.
Baldock, Clair
author_sort Godwin, Alan R.F.
collection PubMed
description Fibrillin is a large evolutionarily ancient extracellular glycoprotein that assembles to form beaded microfibrils which are essential components of most extracellular matrices. Fibrillin microfibrils have specific biomechanical properties to endow animal tissues with limited elasticity, a fundamental feature of the durable function of large blood vessels, skin and lungs. They also form a template for elastin deposition and provide a platform for microfibril-elastin binding proteins to interact in elastic fibre assembly. In addition to their structural role, fibrillin microfibrils mediate cell signalling via integrin and syndecan receptors, and microfibrils sequester transforming growth factor (TGF)β family growth factors within the matrix to provide a tissue store which is critical for homeostasis and remodelling.
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spelling pubmed-69438132020-01-09 The role of fibrillin and microfibril binding proteins in elastin and elastic fibre assembly Godwin, Alan R.F. Singh, Mukti Lockhart-Cairns, Michael P. Alanazi, Yasmene F. Cain, Stuart A. Baldock, Clair Matrix Biol Article Fibrillin is a large evolutionarily ancient extracellular glycoprotein that assembles to form beaded microfibrils which are essential components of most extracellular matrices. Fibrillin microfibrils have specific biomechanical properties to endow animal tissues with limited elasticity, a fundamental feature of the durable function of large blood vessels, skin and lungs. They also form a template for elastin deposition and provide a platform for microfibril-elastin binding proteins to interact in elastic fibre assembly. In addition to their structural role, fibrillin microfibrils mediate cell signalling via integrin and syndecan receptors, and microfibrils sequester transforming growth factor (TGF)β family growth factors within the matrix to provide a tissue store which is critical for homeostasis and remodelling. Elsevier 2019-11 /pmc/articles/PMC6943813/ /pubmed/31226403 http://dx.doi.org/10.1016/j.matbio.2019.06.006 Text en © 2019 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Godwin, Alan R.F.
Singh, Mukti
Lockhart-Cairns, Michael P.
Alanazi, Yasmene F.
Cain, Stuart A.
Baldock, Clair
The role of fibrillin and microfibril binding proteins in elastin and elastic fibre assembly
title The role of fibrillin and microfibril binding proteins in elastin and elastic fibre assembly
title_full The role of fibrillin and microfibril binding proteins in elastin and elastic fibre assembly
title_fullStr The role of fibrillin and microfibril binding proteins in elastin and elastic fibre assembly
title_full_unstemmed The role of fibrillin and microfibril binding proteins in elastin and elastic fibre assembly
title_short The role of fibrillin and microfibril binding proteins in elastin and elastic fibre assembly
title_sort role of fibrillin and microfibril binding proteins in elastin and elastic fibre assembly
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6943813/
https://www.ncbi.nlm.nih.gov/pubmed/31226403
http://dx.doi.org/10.1016/j.matbio.2019.06.006
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