Supramolecular organization of collagen fibrils in healthy and osteoarthritic human knee and hip joint cartilage: Supramolecular Structure and Assembly of Collagen Fibrils
Supramolecular organization of collagen fibrils in healthy and osteoarthritic human knee and hip joint cartilage: Supramolecular Structure and Assembly of Collagen Fibrils
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.
Stolz, Martin
7bfa1d59-511d-471b-96ce-679b343b5d1d
25 October 2016
Stolz, Martin
7bfa1d59-511d-471b-96ce-679b343b5d1d
Stolz, Martin
(2016)
Supramolecular organization of collagen fibrils in healthy and osteoarthritic human knee and hip joint cartilage: Supramolecular Structure and Assembly of Collagen Fibrils.
PLoS ONE, 11 (10), [e0163552].
(doi:10.1371/journal.pone.0163552).
Abstract
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.
Text
plos
- Version of Record
More information
Accepted/In Press date: 11 September 2016
e-pub ahead of print date: 25 October 2016
Published date: 25 October 2016
Organisations:
nCATS Group
Identifiers
Local EPrints ID: 408318
URI: http://eprints.soton.ac.uk/id/eprint/408318
ISSN: 1932-6203
PURE UUID: 9bd898de-7735-489a-8070-502f45aa64b4
Catalogue record
Date deposited: 19 May 2017 04:03
Last modified: 16 Mar 2024 04:02
Export record
Altmetrics
Download statistics
Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.
View more statistics