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. 2024 Jun 10;15:4648. doi: 10.1038/s41467-024-48604-7

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© The Author(s) 2024

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — Created in part with Biorender.com. a In the early stages of healing, a similar process occurs in injured zebrafish and murine hearts: Lysyl-oxidase- (LOX)-mediated oxidation of collagen in the wound converts lysine/hydroxylysine residues to highly reactive aldehydes (allysine/hydroxyallysine, Lys^Ald), which form cross-links. TMR-O binds to Lys^Ald, providing a readout of the initial steps in collagen cross-linking. b Natural history of collagen oxidation and cross-linking in a zebrafish cryoinjury model (n = 5 except for 21 dpi, n = 6). Adult zebrafish, with cardiomyocyte-specific expression of GFP, were injected with TMR-O (2 nmol/g, IP) and the hearts were excised and imaged 4 h after injection. The absence of GFP delineates the area of injury, which shows a steady increase in TMR-O signal from 10–21 days post-injury (dpi). c TMR-O fluorescence intensity peaked between 21–35 dpi (n = 5 except for 21 dpi, n = 6). d AFOG-stained histology sections show the collagen/elastin rich bulbus and collagen-rich healing injury at 10–35 dpi (n = 5 except for 21 dpi, n = 6). e Fluorescence microscopy of adjacent sections shows that the TMR-O signal is localized to the collagen-rich areas of the injured heart (n = 5 except for 21 dpi, n = 6). f The total area of injured myocardium, quantified by histology, decreased steadily between 10–35 dpi, consistent with the regenerative capacity of the zebrafish heart (n = 5 except for 21 dpi, n = 6). (g) Collagen content within the area of injury peaked 21–35 dpi (n = 5 except for 21 dpi, n = 6). h The hearts of injured zebrafish injected with the non-binding probe TMR-NB (2 nmol/g, IP) at 15 dpi showed no fluorescence signal in the heart or bulbus (n = 3). Data are means ± SD of five-six measurements, where each data point represents one zebrafish. P-values are shown where significant, one-way ANOVA with post hoc comparisons, two tailed. Scale bar = 300 μm. Source data are provided in the Source Data file.