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. 2019 Feb 27;10:963. doi: 10.1038/s41467-019-08831-9

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© The Author(s) 2019

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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Fig. 6 — Proteome-wide detergent solubility profiling reveals changes in the extracellular matrix (ECM) architecture. a Experimental design—extraction of proteins from whole lung homogenates with increasing detergent stringency results in four distinct protein fractions, which are analyzed by mass spectrometry (MS). b The projections of a principal component analysis (PCA) of 432 proteins with the annotation ‘secreted' in the Uniprot and/or Matrisome database separate the four protein fractions, indicated by symbol shape, in component 1 and the age groups, as indicated by color, in component 4. c The loadings of the PCA are shown. d–f Relative differences in MS intensity (abundance) of the indicated proteins. g–i The normalized MS intensity across the four protein fractions from differential detergent extraction highlights changes in protein solubility between young and old mice for the indicated proteins. Error bars represent the standard error of the means (n = 4)