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. 2025 Dec 11;15:43626. doi: 10.1038/s41598-025-27499-4

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© The Author(s) 2025

Open Access This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License, which permits any non-commercial use, sharing, 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 you modified the licensed material. You do not have permission under this licence to share adapted material derived from this article or parts of it. 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-nc-nd/4.0/.

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Fig. 3 — Mass spectrometry proteomic analysis in bovine sMSC. (A) Comparative percentage distribution of the three replicates of sMSC analyzed by mass spectrometry. (B) Percentage distribution of proteins or peptides with the highest concentration in sMSC-derived secretome used in the present study. (C) Distribution of proteins in relation to biological processes (left) and molecular function (D) Venn diagram of the three secretome samples detected by mass spectrometry .lc-ms/ms technology.