Similarities and Differences in the Protein Composition of Cutaneous Melanoma Cells and Their Exosomes Identified by Mass Spectrometry.

LC-MS/MS cancer exosomes extracellular vesicles melanoma proteomics

Journal

Cancers
ISSN: 2072-6694
Titre abrégé: Cancers (Basel)
Pays: Switzerland
ID NLM: 101526829

Informations de publication

Date de publication:
08 Feb 2023
Historique:
received: 21 12 2022
revised: 31 01 2023
accepted: 05 02 2023
entrez: 25 2 2023
pubmed: 26 2 2023
medline: 26 2 2023
Statut: epublish

Résumé

Intercellular transport of proteins mediated by extracellular vesicles (EVs)-exosomes and ectosomes-is one of the factors facilitating carcinogenesis. Therefore, the research on protein cargo of melanoma-derived EVs may provide a better understanding of the mechanisms involved in melanoma progression and contribute to the development of alternative biomarkers. Proteomic data on melanoma-derived EVs are very limited. The shotgun nanoLC-MS/MS approach was applied to analyze the protein composition of primary (WM115, WM793) and metastatic (WM266-4, WM1205Lu) cutaneous melanoma cells and exosomes released by them. All cells secreted homogeneous populations of exosomes that shared a characteristic set of proteins. In total, 3514 and 1234 unique proteins were identified in melanoma cells and exosomes, respectively. Gene ontology analysis showed enrichment in several cancer-related categories, including cell proliferation, migration, negative regulation of apoptosis, and angiogenesis. The obtained results broaden our knowledge on the role of selected proteins in exosome biology, as well as their functional role in the development and progression of cutaneous melanoma. The results may also inspire future studies on the clinical potential of exosomes.

Identifiants

pubmed: 36831440
pii: cancers15041097
doi: 10.3390/cancers15041097
pmc: PMC9954195
pii:
doi:

Types de publication

Journal Article

Langues

eng

Subventions

Organisme : BioS Priority Research Area under the program "Excellence Initiative -Research University" at the Jagiellonian University in Krakow
ID : U1U/P03/DO/64.22

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Auteurs

Magdalena Surman (M)

Department of Glycoconjugate Biochemistry, Institute of Zoology and Biomedical Research, Faculty of Biology, Jagiellonian University, 30-387 Krakow, Poland.

Urszula Jankowska (U)

Proteomics and Mass Spectrometry Core Facility, Malopolska Centre of Biotechnology, Jagiellonian University, 30-387 Krakow, Poland.

Magdalena Wilczak (M)

Department of Glycoconjugate Biochemistry, Institute of Zoology and Biomedical Research, Faculty of Biology, Jagiellonian University, 30-387 Krakow, Poland.
Doctoral School of Exact and Natural Sciences, Jagiellonian University, 30-348 Krakow, Poland.

Małgorzata Przybyło (M)

Department of Glycoconjugate Biochemistry, Institute of Zoology and Biomedical Research, Faculty of Biology, Jagiellonian University, 30-387 Krakow, Poland.

Classifications MeSH