Comprehensive proteomic analysis of breast cancer cell membranes reveals unique proteins with potential roles in clinical cancer
| Autor: | Helen R. Poyser, Laurent Daviet, Raj Parekh, Sonal Patel, Kerry Louise Tyson, Adrian L. Harris, Alasdair Stamps, Julie A. Loader, Lindsey Hudson, Graham Steers, Matthew R. Griffiths, Paul J. Adam, Pierre Legrain, Joanne Berry, Fletcher Graham Charles, Raymond R. Townsend, Jonathan A Terrett, Robert Boyd, Nick Redpath |
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| Rok vydání: | 2002 |
| Předmět: |
Proteome
Cell Molecular Sequence Data Breast Neoplasms Biology Proteomics medicine.disease_cause Transfection Biochemistry Polymerase Chain Reaction Breast cancer medicine Tumor Cells Cultured Humans Amino Acid Sequence Cloning Molecular Molecular Biology Base Sequence Reverse Transcriptase Polymerase Chain Reaction Cancer Membrane Proteins Cell Biology medicine.disease Peptide Fragments Cell biology Neoplasm Proteins medicine.anatomical_structure Membrane protein Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Cancer cell Female Carcinogenesis |
| Zdroj: | The Journal of biological chemistry. 278(8) |
| ISSN: | 0021-9258 |
| Popis: | Proteins associated with cancer cell plasma membranes are rich in known drug and antibody targets as well as other proteins known to play key roles in the abnormal signal transduction processes required for carcinogenesis. We describe here a proteomics process that comprehensively annotates the protein content of breast tumor cell membranes and defines the clinical relevance of such proteins. Tumor-derived cell lines were used to ensure an enrichment for cancer cell-specific plasma membrane proteins because it is difficult to purify cancer cells and then obtain good membrane preparations from clinical material. Multiple cell lines with different molecular pathologies were used to represent the clinical heterogeneity of breast cancer. Peptide tandem mass spectra were searched against a comprehensive data base containing known and conceptual proteins derived from many public data bases including the draft human genome sequences. This plasma membrane-enriched proteome analysis created a data base of more than 500 breast cancer cell line proteins, 27% of which were of unknown function. The value of our approach is demonstrated by further detailed analyses of three previously uncharacterized proteins whose clinical relevance has been defined by their unique cancer expression profiles and the identification of protein-binding partners that elucidate potential functionality in cancer. |
| Databáze: | OpenAIRE |
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