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Supramolecular Organization of Collagen Fibrils in Healthy and Osteoarthritic Human Knee and Hip Joint Cartilage
Cartilage matrix is a composite of discrete, but interacting suprastructures, i.e. cartilage fibers with microfibrillar or network-like aggregates and penetrating extrafibrillar proteoglycan matrix. The biomechanical function of the proteoglycan matrix and the collagen fibers are to absorb compressi...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5079628/ https://www.ncbi.nlm.nih.gov/pubmed/27780246 http://dx.doi.org/10.1371/journal.pone.0163552 |
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author | Gottardi, Riccardo Hansen, Uwe Raiteri, Roberto Loparic, Marko Düggelin, Marcel Mathys, Daniel Friederich, Niklaus F. Bruckner, Peter Stolz, Martin |
author_facet | Gottardi, Riccardo Hansen, Uwe Raiteri, Roberto Loparic, Marko Düggelin, Marcel Mathys, Daniel Friederich, Niklaus F. Bruckner, Peter Stolz, Martin |
author_sort | Gottardi, Riccardo |
collection | PubMed |
description | Cartilage matrix is a composite of discrete, but interacting suprastructures, i.e. cartilage fibers with microfibrillar or network-like aggregates and penetrating extrafibrillar proteoglycan matrix. The biomechanical function of the proteoglycan matrix and the collagen fibers are to absorb compressive and tensional loads, respectively. Here, we are focusing on the suprastructural organization of collagen fibrils and the degradation process of their hierarchical organized fiber architecture studied at high resolution at the authentic location within cartilage. We present electron micrographs of the collagenous cores of such fibers obtained by an improved protocol for scanning electron microscopy (SEM). Articular cartilages are permeated by small prototypic fibrils with a homogeneous diameter of 18 ± 5 nm that can align in their D-periodic pattern and merge into larger fibers by lateral association. Interestingly, these fibers have tissue-specific organizations in cartilage. They are twisted ropes in superficial regions of knee joints or assemble into parallel aligned cable-like structures in deeper regions of knee joint- or throughout hip joints articular cartilage. These novel observations contribute to an improved understanding of collagen fiber biogenesis, function, and homeostasis in hyaline cartilage. |
format | Online Article Text |
id | pubmed-5079628 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-50796282016-11-04 Supramolecular Organization of Collagen Fibrils in Healthy and Osteoarthritic Human Knee and Hip Joint Cartilage Gottardi, Riccardo Hansen, Uwe Raiteri, Roberto Loparic, Marko Düggelin, Marcel Mathys, Daniel Friederich, Niklaus F. Bruckner, Peter Stolz, Martin PLoS One Research Article Cartilage matrix is a composite of discrete, but interacting suprastructures, i.e. cartilage fibers with microfibrillar or network-like aggregates and penetrating extrafibrillar proteoglycan matrix. The biomechanical function of the proteoglycan matrix and the collagen fibers are to absorb compressive and tensional loads, respectively. Here, we are focusing on the suprastructural organization of collagen fibrils and the degradation process of their hierarchical organized fiber architecture studied at high resolution at the authentic location within cartilage. We present electron micrographs of the collagenous cores of such fibers obtained by an improved protocol for scanning electron microscopy (SEM). Articular cartilages are permeated by small prototypic fibrils with a homogeneous diameter of 18 ± 5 nm that can align in their D-periodic pattern and merge into larger fibers by lateral association. Interestingly, these fibers have tissue-specific organizations in cartilage. They are twisted ropes in superficial regions of knee joints or assemble into parallel aligned cable-like structures in deeper regions of knee joint- or throughout hip joints articular cartilage. These novel observations contribute to an improved understanding of collagen fiber biogenesis, function, and homeostasis in hyaline cartilage. Public Library of Science 2016-10-25 /pmc/articles/PMC5079628/ /pubmed/27780246 http://dx.doi.org/10.1371/journal.pone.0163552 Text en © 2016 Gottardi et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Gottardi, Riccardo Hansen, Uwe Raiteri, Roberto Loparic, Marko Düggelin, Marcel Mathys, Daniel Friederich, Niklaus F. Bruckner, Peter Stolz, Martin Supramolecular Organization of Collagen Fibrils in Healthy and Osteoarthritic Human Knee and Hip Joint Cartilage |
title | Supramolecular Organization of Collagen Fibrils in Healthy and Osteoarthritic Human Knee and Hip Joint Cartilage |
title_full | Supramolecular Organization of Collagen Fibrils in Healthy and Osteoarthritic Human Knee and Hip Joint Cartilage |
title_fullStr | Supramolecular Organization of Collagen Fibrils in Healthy and Osteoarthritic Human Knee and Hip Joint Cartilage |
title_full_unstemmed | Supramolecular Organization of Collagen Fibrils in Healthy and Osteoarthritic Human Knee and Hip Joint Cartilage |
title_short | Supramolecular Organization of Collagen Fibrils in Healthy and Osteoarthritic Human Knee and Hip Joint Cartilage |
title_sort | supramolecular organization of collagen fibrils in healthy and osteoarthritic human knee and hip joint cartilage |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5079628/ https://www.ncbi.nlm.nih.gov/pubmed/27780246 http://dx.doi.org/10.1371/journal.pone.0163552 |
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