title: Comparative proteome profiling of breast tumor cell lines by gel electrophoresis and mass spectrometry reveals an epithelial mesenchymal transition associated protein signature.
abstract: The epithelial to mesenchymal transition (EMT) is a cellular program associated with the organ morphogenesis but also with the disease progression. EMT in the cancer field fuels neoplastic progression promoting the resistance to cell death, the resistance to chemotherapy and the acquisition of stem cell properties. Considering the crucial role of EMT in breast cancer metastasis, a better understanding of this process may provide new therapeutic options. Here, by using a proteomic approach we identified a set of proteins differentially expressed between an epithelial and a mesenchymal breast cancer cell line. The protein-protein network of these identified proteins was determined by an in silico analysis highlighting, in the EMT program, the role of proteins involved in cell adhesion, migration, and invasion, together with protein kinases involved in proliferation and survival, with many of these emerging as possible targets of novel biological agents. Finally, the pharmacological inhibition of some of these kinases was able to reverse the mesenchymal phenotype to an epithelial phenotype.
authors.affiliation: Laboratory of General Physiology, Department of Biological and Environmental Sciences and Technologies, University of Salento, via Monteroni 73100, Lecce, Italy.
authors.forename: Daniele
authors.initials: D
authors.lastname: Vergara
authors.forename: Pasquale
authors.initials: P
authors.lastname: Simeone
authors.forename: Piero
authors.initials: P
authors.lastname: del Boccio
authors.forename: Claudia
authors.initials: C
authors.lastname: Toto
authors.forename: Damiana
authors.initials: D
authors.lastname: Pieragostino
authors.forename: Andrea
authors.initials: A
authors.lastname: Tinelli
authors.forename: Raffaele
authors.initials: R
authors.lastname: Acierno
authors.forename: Saverio
authors.initials: S
authors.lastname: Alberti
authors.forename: Michel
authors.initials: M
authors.lastname: Salzet
authors.forename: Gianluigi
authors.initials: G
authors.lastname: Giannelli
authors.forename: Paolo
authors.initials: P
authors.lastname: Sacchetta
authors.forename: Michele
authors.initials: M
authors.lastname: Maffia
mesh_terms: D000970:Antineoplastic Agents / Q000494:pharmacology; D001943:Breast Neoplasms / Q000235:genetics / Q000378:metabolism*; D002448:Cell Adhesion; D045744:Cell Line, Tumor; D002465:Cell Movement; D049109:Cell Proliferation; D002470:Cell Survival / Q000187:drug effects; D004847:Epithelial Cells / Q000378:metabolism*; D058750:Epithelial-Mesenchymal Transition / Q000235:genetics; D005260:Female; D015870:Gene Expression; D020869:Gene Expression Profiling; D006801:Humans; D008648:Mesoderm / Q000166:cytology* / Q000378:metabolism; D009361:Neoplasm Invasiveness; D009362:Neoplasm Metastasis; D009536:Niacinamide / Q000031:analogs & derivatives / Q000494:pharmacology; D010671:Phenylurea Compounds / Q000494:pharmacology; D010880:Piperidines / Q000494:pharmacology; D060066:Protein Interaction Maps; D011494:Protein Kinases / Q000378:metabolism; D020543:Proteome / Q000235:genetics / Q000378:metabolism; D040901:Proteomics; D011799:Quinazolines / Q000494:pharmacology; D000077157:Sorafenib
chemical_list: D000970:Antineoplastic Agents; D010671:Phenylurea Compounds; D010880:Piperidines; D020543:Proteome; D011799:Quinazolines; D009536:Niacinamide; D000077157:Sorafenib; D011494:Protein Kinases; C452423:vandetanib