Mass spectrometry identification and validation of cell surfaceome associated with breast cancer cell migration and metastasis
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| Year of publication | 2019 |
| Type | Conference abstract |
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| Citation | |
| Description | Biological treatment of many cancers currently targets membrane bound receptors located on a cell surface. To identify novel membrane proteins associated with migration and metastasis of breast cancer cells, we selected and characterized a more migrating subpopulation of MDA-MB-231 breast cancer cells. We applied quantitative mass spectrometry with SILAC labeling to analyze their biotinylated surfaceome and compared it with that of parental MDA-MB-231 cells. Among 838 identified proteins (FDR < 0.01), 210 differentially abundant cell surface proteins with at least one transmembrane domain were found. Of these, (i) catechol-O-methyltransferase (COMT) was successfully verified as a protein associated with lymph node metastasis of triple negative breast cancer and tumor grade by targeted data extraction from the previously acquired SWATH-MS data set of 96 breast cancer tissues [1], and (ii) desmocollin-1 (DSC1) was verified as a protein connected with lymph node status of luminal A breast cancer, tumor grade and Her-2 status by immunohistochemistry in the same set of patients. Kaplan-Meier analysis associated COMT and DSC1 with decreased overall survival in breast cancer subsets. Our findings indicate importance of both proteins for breast cancer progression and metastasis. |
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