A New Method for Investigating Osteoarthritis using Fast Field Cycling Nuclear Magnetic Resonance

Lionel Broche; James Ross; Brett Kennedy; Campbell MacEachern; David Lurie; George P. Ashcroft

doi:10.1016/j.ejmp.2021.05.034

A New Method for Investigating Osteoarthritis using Fast Field Cycling Nuclear Magnetic Resonance

Lionel Broche, James Ross^* (Corresponding Author), Brett Kennedy, Campbell MacEachern, David Lurie, George P. Ashcroft

^*Corresponding author for this work

University of Aberdeen

Research output: Contribution to journal › Article › peer-review

4 Citations (Scopus)

6 Downloads (Pure)

Abstract

Human articular hyaline cartilage is composed of a dense extracellular matrix (ECM) made up of 70% water and 30% protein. The major protein components are type II collagen and proteoglycans, with other non-collagenous proteins present in small amounts. All are regenerated slowly but continuously by chondrocyte cells through the structure [1] and it is the combination of proteoglycans held within the overall collagen structure that combines to hold water in the ECM, which is essential in the maintenance of its unique mechanical properties. The interactions between proteoglycans and collagen are elusive but known to be of electrostatic nature [2].

Original language	English
Pages (from-to)	142-147
Number of pages	6
Journal	Physica Medica
Volume	88
Early online date	7 Jul 2021
DOIs	https://doi.org/10.1016/j.ejmp.2021.05.034
Publication status	Published - Aug 2021

Bibliographical note

ACKNOWLEDGEMENTS
We acknowledge ARUK (Versus Arthritis) for funding this study (grant number 19869) and the NHS Grampian Biorepository for the access to cartilage samples. BWCK received a Foulkes Foundation Fellowship. This project has also received funding from the European Union’s Horizon 2020 research and innovation programme under grant agreement No 668119 (project “IDentIFY”) and
NHS Grampian endowments. This work received support from the EURELAX COST Action CA15209, supported by COST (European Cooperation in Science and Technology).

Keywords

Fast field-cycling NMR
Human hyaline cartilage
osteoarthritis
T1 dispersion
Quadrupolar peaks
protein interactions

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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Cite this

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title = "A New Method for Investigating Osteoarthritis using Fast Field Cycling Nuclear Magnetic Resonance",

abstract = "Human articular hyaline cartilage is composed of a dense extracellular matrix (ECM) made up of 70% water and 30% protein. The major protein components are type II collagen and proteoglycans, with other non-collagenous proteins present in small amounts. All are regenerated slowly but continuously by chondrocyte cells through the structure [1] and it is the combination of proteoglycans held within the overall collagen structure that combines to hold water in the ECM, which is essential in the maintenance of its unique mechanical properties. The interactions between proteoglycans and collagen are elusive but known to be of electrostatic nature [2]. ",

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author = "Lionel Broche and James Ross and Brett Kennedy and Campbell MacEachern and David Lurie and Ashcroft, {George P.}",

note = "ACKNOWLEDGEMENTS We acknowledge ARUK (Versus Arthritis) for funding this study (grant number 19869) and the NHS Grampian Biorepository for the access to cartilage samples. BWCK received a Foulkes Foundation Fellowship. This project has also received funding from the European Union{\textquoteright}s Horizon 2020 research and innovation programme under grant agreement No 668119 (project “IDentIFY”) and NHS Grampian endowments. This work received support from the EURELAX COST Action CA15209, supported by COST (European Cooperation in Science and Technology).",

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AU - Ross, James

AU - Kennedy, Brett

AU - MacEachern, Campbell

AU - Lurie, David

AU - Ashcroft, George P.

N1 - ACKNOWLEDGEMENTS We acknowledge ARUK (Versus Arthritis) for funding this study (grant number 19869) and the NHS Grampian Biorepository for the access to cartilage samples. BWCK received a Foulkes Foundation Fellowship. This project has also received funding from the European Union’s Horizon 2020 research and innovation programme under grant agreement No 668119 (project “IDentIFY”) and NHS Grampian endowments. This work received support from the EURELAX COST Action CA15209, supported by COST (European Cooperation in Science and Technology).

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N2 - Human articular hyaline cartilage is composed of a dense extracellular matrix (ECM) made up of 70% water and 30% protein. The major protein components are type II collagen and proteoglycans, with other non-collagenous proteins present in small amounts. All are regenerated slowly but continuously by chondrocyte cells through the structure [1] and it is the combination of proteoglycans held within the overall collagen structure that combines to hold water in the ECM, which is essential in the maintenance of its unique mechanical properties. The interactions between proteoglycans and collagen are elusive but known to be of electrostatic nature [2].

AB - Human articular hyaline cartilage is composed of a dense extracellular matrix (ECM) made up of 70% water and 30% protein. The major protein components are type II collagen and proteoglycans, with other non-collagenous proteins present in small amounts. All are regenerated slowly but continuously by chondrocyte cells through the structure [1] and it is the combination of proteoglycans held within the overall collagen structure that combines to hold water in the ECM, which is essential in the maintenance of its unique mechanical properties. The interactions between proteoglycans and collagen are elusive but known to be of electrostatic nature [2].

KW - Fast field-cycling NMR

KW - Human hyaline cartilage

KW - osteoarthritis

KW - T1 dispersion

KW - Quadrupolar peaks

KW - protein interactions

U2 - 10.1016/j.ejmp.2021.05.034

DO - 10.1016/j.ejmp.2021.05.034

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EP - 147

JO - Physica Medica

JF - Physica Medica

ER -

A New Method for Investigating Osteoarthritis using Fast Field Cycling Nuclear Magnetic Resonance

Abstract

Bibliographical note

Keywords

UN SDGs

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