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August 22, 2026Scientific Reports0 citationsOpen Access

Proteome profiling of large extracellular vesicles reveals distinct molecular signatures associated with breast cancer brain metastasis

AOAyobami OluokunMFMojibola FowoweOOOdunayo O. Oluokun

Key Points

  • To profile the proteomic cargo of large extracellular vesicles across breast cancer cell lines to identify specific molecular signatures associated with brain metastasis.
  • Performed label-free quantitative liquid chromatography-tandem mass spectrometry (LC-MS/MS; false discovery rate < 1%) on large extracellular vesicles (lEVs) isolated from four breast cancer cell lines, including brain-tropic MDA-MB-231BR.
  • Compared lEV proteomic profiles with whole-cell membrane proteomes and conducted signaling pathway enrichment analyses.
  • Identified 1,708 total proteins, with 145 proteins consistently altered in brain-tropic MDA-MB-231BR lEVs, including significant upregulation of CLIC4, MSN, LDHB, RPLP2, EEF1G, and PSMD3.
  • Demonstrated predicted activation of CXCR4, Ephrin receptor, and Integrin signaling alongside inhibition of RhoGDI signaling in brain-tropic lEVs, confirming non-random cargo sorting enriched for cell adhesion and motility.

Abstract

Breast cancer brain metastasis (BCBM) remains a significant clinical challenge, with limited understanding of how tumor-derived extracellular vesicles contribute to its progression. Large extracellular vesicles (lEVs) represent a distinct EV subtype capable of carrying molecular cargo that reflects and potentially influences the metastatic behavior of tumor cells. We conducted a comprehensive quantitative proteomic analysis of lEVs from four breast cancer cell lines, including brain-tropic MDA-MB-231BR, to elucidate the role of lEVs in BCBM. Label-free LC-MS/MS identified 1,708 proteins (FDR < 1%). Analysis revealed 145 proteins consistently altered in the 231BR line compared with the other cell lines. Notably, CLIC4, MSN, LDHB, RPLP2, EEF1G, and PSMD3 were upregulated. Pathway analysis predicted activation of CXCR4 signaling and inhibition of RhoGDI signaling, pathways consistent with enhanced motility. Comparative analysis with whole-cell membrane (WCM) proteomes suggested that lEVs represent a distinct vesicular cargo compartment rather than random membrane sampling. lEVs were enriched for adhesion-related proteins and showed stronger predicted activation of Ephrin receptor and Integrin signaling compared with the WCM proteome. These findings support lEVs as a biologically informative vesicular compartment for studying tumor-associated cargo and provide a panel of protein candidates for future investigation of BCBM mechanisms and biomarker development.

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Cite This Study

Oluokun et al. (2026) studied this question.

synapsesocial.com/papers/6a895eeeca7ade938187d155https://doi.org/10.1038/s41598-026-64286-1
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