Two independent proteomic approaches provide a comprehensive analysis of the synovial fluid proteome response to Autologous Chondrocyte Implantation
MetadataShow full item record
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.
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 . DOI: 10.1186/s13075-018-1573-4
Arthritis Research & Therapy
© 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.
DescriptionWe 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).
Items in the St Andrews Research Repository are protected by copyright, with all rights reserved, unless otherwise indicated.