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. 2017 Sep 29;7:12412. doi: 10.1038/s41598-017-12603-0

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as 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 images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Synaptic thalamic proteome filtering and validation. (A) Dot plot demonstrating the process of proteomic data filtering. Each data point represents an individual protein identified using iTRAQ proteomic technique. LHS 1536 proteins were identified across all thalamic samples. Following filtering (see Methods) a molecular fingerprint for thalamic synaptic alterations comprising 374 candidate proteins was produced (RHS; see also Supplementary Tables S3 and S4). (B) QWB representative bands for two upregulated (β-catenin and ROCK2), two downregulated (HIBCH and α-synuclein) and one unchanged protein candidate (calretinin) verifying the proteomic data. (C and G). Quantification and statistical QWB analysis showing the magnitude of alteration in Cln3 ^−/− thalamic synaptic fractions. All the selected candidate proteins were altered as indicated by this iTRAQ analysis. Mean ± SEM; *P < 0.05; ***P < 0.001 (Student T test, n = 6 mice per each genotype).