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. 2023 May 8;14:2642. doi: 10.1038/s41467-023-38171-8

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© The Author(s) 2023

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 — a Scheme of cancer cell-derived protein capture from serum: After orthotopic transplantation of MetRS*-expressing or WT (Ctrl) PDAC cells and ANL labeling, tumor-bearing mouse sera were collected, and tumor-derived proteins were enriched and analyzed. b Specifically enriched cancer cell-derived serum protein groups ranked by intensity. Proteins with cytokine function are indicated. c Exclusively identified and overlap of specifically enriched 8513 and 8661 cancer cell-derived proteins (8661: n = 4, 8513: n = 3, biological replicates). d Cancer cell-derived matrisome proteins counts, summed total and relative LFQ intensities per matrisome category. e Fold change distribution of non-matrisome, and matrisome class proteins between PDAC subtypes. P-values were determined by a two-sided Welch’s t-test. f Volcano plot of 8661 and 8513 cancer cell-derived proteins in serum. GOCC annotated Laminin complex proteins (blue), fibrillar collagens (red), and proteins with significant fold changes (dark gray) are highlighted (two-sided Student’s t-test, permutation-based FDR = 0.05, S0 = 0.1). g Fold changes of pre-metastatic niche formation-associated proteins. Proteins with significant fold changes (two-sided Student’s t-test, permutation-based FDR = 0.05, S0 = 0.1) are indicated in bold. Source data are provided as a Source Data file.