6533b834fe1ef96bd129d5c5

RESEARCH PRODUCT

New protein clustering of breast cancer tissue proteomics using actin content as a cellularity indicator

Maria Rita MarabetiAntonio MarrazzoNadia Ninfa AlbaneseIda Pucci-minafraGianluca Di CaraSalvatore MinafraPatrizia Cancemi

subject

ProteomicsProteomeBlotting WesternCathepsin DBreast NeoplasmsBiologyProteomicsBiochemistryS100 proteinPeptide Mappingbreast cancer tissueAnnexinHeat shock proteinCluster AnalysisHumansElectrophoresis Gel Two-DimensionalSettore BIO/06 - Anatomia Comparata E CitologiaOncogeneReproducibility of ResultsGeneral Chemistrybreast cancer tissues; proteomicsCofilinMolecular biologyActinsSettore MED/18 - Chirurgia GeneraleSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationProteomeFemale

description

In the present study, we report the comparative proteome profiles of proteins solubilized from 37 breast cancer surgical tissues, normalized for the actin content. Blood-derived proteins were excluded from the analysis. Among the tumor-derived protein spots, a large proportion (39%) was found present in all patients. These included several glycolytic enzymes, detox and heat shock proteins, members of annexin and S100 protein families, cathepsin D, and two “rare” proteins, DDAH2 involved in the angiogenesis control, and the oncogene PARK7. Other proteins, such as psoriasin, galectin1, cofilin, peroredoxins, SH3L1, and others, showed sporadic presence and high expression level, which suggests their possible role for patient stratification.

10.1021/pr700748mhttp://hdl.handle.net/10447/36400