Two independent proteomic approaches provide a comprehensive analysis of the synovial fluid proteome response to Autologous Chondrocyte Implantation
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Date
02/05/2018Author
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Abstract
Autologous chondrocyte implantation (ACI) has a failure rate of approximately 20%, but it is yet to be fully understood why. Biomarkers are needed that can pre-operatively predict in which patients it is likely to fail, so that alternative or individualised therapies can be offered. We previously used label-free quantitation (LF) with a dynamic range compression proteomic approach to assess the synovial fluid (SF) of ACI responders and non-responders. However, we were able to identify only a few differentially abundant proteins at baseline. In the present study, we built upon these previous findings by assessing higher-abundance proteins within this SF, providing a more global proteomic analysis on the basis of which more of the biology underlying ACI success or failure can be understood.
Citation
Hulme , C H , Wilson , E L , Fuller , H R , Roberts , S , Richardson , J B , Gallacher , P , Peffers , M J , Shirran , S L , Botting , C H & Wright , K T 2018 , ' Two independent proteomic approaches provide a comprehensive analysis of the synovial fluid proteome response to Autologous Chondrocyte Implantation ' , Arthritis Research & Therapy , vol. 20 , 87 . https://doi.org/10.1186/s13075-018-1573-4
Publication
Arthritis Research & Therapy
Status
Peer reviewed
ISSN
1478-6362Type
Journal article
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© The Author(s). 2018 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
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We thank Arthritis Research UK for supporting this work via grants 19429, 20815 and 21122. MJP is supported through a Wellcome Trust Clinical Intermediate Fellowship. This work was supported by Wellcome Trust grant 094476/Z/10/Z, which funded the purchase of the TripleTOF 5600 mass spectrometer at the Biomedical Sciences Research Complex Mass Spectrometry and Proteomics Facility, University of St. Andrews (Fife, UK).Collections
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