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. 2017 Jun 30;19:150. doi: 10.1186/s13075-017-1336-7

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© The Author(s). 2017

Open AccessThis 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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Fig. 5 — Two biologically relevant proteins, matrix metalloproteinase-1 (MMP1) and S100 calcium binding protein A13 (S100-A13), that were identified by proteomic analysis as differentially abundant in the SF of non-responders between Stages I (SI) and II (SII) of the ACI procedure were validated by ELISA. a The differential abundance as measured by label-free mass-spectrometry and by biochemical ELISA. MMP1 was measured by ELISA in the SF of (b) non-responders (NR) and (c) responders (R) to ACI at cartilage harvest (Stage I; S1) and chondrocyte implantation (Stage II; S2). S100-A13 was measured by ELISA in the SF of non-responders (d) and responders (e) to ACI