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MDA-MB-231 blebbisome proteomics

ABSTRACT: Cells secrete a large variety of extracellular vesicles (EVs) to engage in cell-to-cell and cell-to-environment intercellular communication. EVs are functionally involved in many physiological and pathological processes by interacting with cells that facilitate transfer of proteins, lipids and genetic information. However, our knowledge of EVs is incomplete. We show that cells actively release exceptionally large (up to 20 µm) membrane-enclosed vesicles that exhibit active blebbing behavior, and we therefore have termed them blebbisomes. Blebbisomes contain an array of cellular organelles that include functional mitochondria and multivesicular endosomes yet lack a definable nucleus. We provide proteomic analysis of blebbisomes, large and small EVs released from metastatic MDA-MB-231 breast cancer cells. Blebbisomes are released from normal and cancer cells, can be observed by direct imaging of cancer cells in vivo, and are present in normal bone marrow.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Breast Epithelium, Mammary Gland Epithelial Cell

DISEASE(S): Breast Adenocarcinoma

SUBMITTER: Kristie Lindsey Rose

LAB HEAD: Kristie Lindsey Rose; Dennis Jeppesen

PROVIDER: PXD059407 | Pride | 2025-01-05

REPOSITORIES: pride

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			Action	DRS
	6115_Peptide_Spectrum_Report.xlsx	Xlsx
	6115_Scaffold_Protein_Report.xlsx	Xlsx
	checksum.txt	Txt
	pQE4_pp_6115_20220519_B1_1pt1uL_4.raw	Raw
	pQE4_pp_6115_20220519_B2_1pt2uL_5.raw	Raw

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Project description:Uveal melanoma is a poor prognosis cancer with an imperative need for new treatment options. Ergolide, a sesquiterpene lactone isolated from the flowers of Inula species (a medicinal herb), exerts anti-cancer properties. The objective of this study was to 1) evaluate whether ergolide reduced metastatic uveal melanoma (MUM) cell survival/viability in vitro and in vivo; and 2) to understand the molecular mechanism of ergolide action. Ergolide treatment resulted in significant dose-dependent reduction (48.5 to 99.9%; p < 0.0001) in OMM2.5 cell survival in vitro and of normalized primary zebrafish xenograft fluorescence (56%; p< 0.0001) in vivo, compared to vehicle controls. Proteome profiling of ergolide treated OMM2.5 cells, identified 5023 proteins in total with 52 and 55 proteins significantly altered at 4 hours and 24 hours, respectively (p value <0.05; fold-change >1.2). Immunoblot analysis of heme oxygenase 1 (HMOX1), growth/differentiation factor 15 (GDF15) and macrophage migration inhibitory factor (MIF) corroborated the proteomics data. MIF was distinctly downregulated following ergolide treatment. Proteomics of EVs isolated from OMM2.5 cells treated with ergolide detected 2931 total proteins, 2679 of which are recognized as EV proteins based on the Vesiclepedia compendium. 252 additional putative novel EV proteins were also identified. Within the differentially expressed proteins, the proteasomal pathway was primarily altered. Interestingly, BRCA2 and CDKN1A Interacting Protein (BCCIP) and Chitinase Domain Containing 1 (CHID1), were the only proteins significantly differentially expressed by ergolide in both the OMM2.5 cell and EV isolates and they displayed inverse differential expression in the cells versus the EVs. In the TCGA database, no significant correlations occurred between BCCIP and CHID1 transcript levels and overall survival or disease-free survival in UM patients. Ergolide is a novel candidate that shows promise as an anti-proliferative agent for UM/MUM cells. Proteomic profiling of OMM2.5 cell lysates and EVs identified candidate pathways elucidating the action of ergolide and putative biomarkers of UM, that require further examination.

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MDA-MB-231 blebbisome proteomics

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