MassIVE MSV000099457

Partial Public PXD069384

Proteomic analysis of secretomes from WM9/Hs294T melanoma cells resistant and non-resistant to BRAF/MEK and from their co-cultures with adipocytes

Description

Treatment based on BRAF/MEK kinase inhibitors is currently one of the most commonly used methods in melanoma therapy. Unfortunately, in the case of advanced melanoma, patients often develop resistance to treatment at an early stage of the treatment. A thorough understanding of the causes and mechanisms may contribute to the development of new, more effective treatments. One of the ways in which treatment-resistant cells can affect other cancer cells and the tumor microenvironment is through the factors they secrete. Therefore, this study aimed to examine the protein composition of the secretome of cells resistant to vemurafenib (BRAF inhibitor) and cobimetinib (MEK inhibitor) and compare it with the secretome of non-resistant cells. Proteomic analysis, followed by gene ontology (GO) analysis, identified many differences in resistant melanoma cells' secretomes compared to controls (non-resistant) in terms of cellular compartment, molecular function, biological processes, and reactome pathways. Proteins unique to the secretomes of resistant cells were associated with, among others, integrin binding and interactions, and the extracellular matrix organization. Other interesting groups of proteins, i.e., up- or downregulated in secretomes of resistant melanoma cells vs their non-resistant variants, were directly related to cancer progression and associated with cell adhesion, actin cytoskeleton organization, matrix proteolysis, and drug resistance. Proteins included in these groups, once secreted by resistant melanoma cells, can undoubtedly influence the surrounding microenvironment in a way that promotes the formation of a pro-tumor niche. [doi:10.25345/C5WH2DT5N] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: melanoma ; drug resistance ; secretome ; BRAF inhibitor ; vemurafenib ; cobimetinib ; MEK inhibitor ; DatasetType:Proteomics

Contact

Principal Investigators:
(in alphabetical order)
Aleksandra Simiczyjew, Department of Cell Pathology, Faculty of Biotechnology, University of Wroclaw, Poland
Submitting User: msurman
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Experimental Design
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Identification Results
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Quantification Results
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Originally identified proteins that were automatically remapped by MassIVE to proteins in the SwissProt human reference database.

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Number of distinct proteins quantified across all analyses (original submission and reanalyses) associated with this dataset.

Distinct protein accessions are counted across all files submitted in the "Statistical Analysis of Quantified Analytes" category having a "Protein" column in this dataset.

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Number of distinct proteins found to be differentially abundant in at least one comparison across all analyses (original submission and reanalyses) associated with this dataset.

A protein is differentially abundant if its change in abundance across conditions is found to be statistically significant with an adjusted p-value <= 0.05 and lists no issues associated with statistical tests for differential abundance.

Distinct protein accessions are counted across all files submitted in the "Statistical Analysis of Quantified Analytes" category having a "Protein" column in this dataset.

"N/A" means no results of this type were submitted.
This dataset may not contain all raw spectra data as originally deposited in PRIDE. It has been imported to MassIVE for reanalysis purposes, so its spectra data here may consist solely of processed peak lists suitable for reanalysis with most software.