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. 2020 May 25;11:2604. doi: 10.1038/s41467-020-16409-z

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© The Author(s) 2020

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. 7 — Biochemical analysis of collagen and non-collagenous proteins using whole lysate from unwounded skin (NS) and from wounds at day 3, 5, 10, and 42 post-injury. a Amount of total collagen per sample. b Amount of total non-collagenous protein per sample. c Amount of collagen per total protein relative to NS (gray dashed line). d Diagram outlining the collagen cross-linking initiation and maturation pathways (adapted from ref. ⁷⁹), the enzymes that are responsible for the number (LOX) and the pattern (LH2) of the cross-links, and the cross-links quantified in our analysis. Modifications that are increased in wounds of Act mice are in red. e Hyl^ald/Lys^ald ratio relative to NS (gray dashed line). f DHLNL/collagen ratio relative to NS (gray dashed line). g DHLNL/HLNL cross-link ratio. Graphs show mean ± SEM and P values; n = 9 biological replicates for mice of both genotypes at all time points; two-way ANOVA and Bonferroni’s multiple comparison post hoc tests; results of two-way ANOVA are shown below each graph (first factor: time point, second factor: activin overexpression). HLCC hydroxylysine aldehyde derived collagen cross-links, LCC lysine aldehyde-derived collagen cross-links, Lys lysine, Hyl hydroxylysine, LH lysyl hydroxylase, LOX lysyl oxidase, Lys^ald lysine aldehyde, Hyl^ald hydroxylysine aldehyde, ACP aldol condensation product, HLNL hydroxylysinonorleucine, DHLNL dihydroxylysinonorleucine, HHMD histidinohydroxymerodesmosine, LP lysylpyridinoline, HP hydroxylysylpyridinoline. Source data are provided as a Source Data file (Fig. 7).