DECORIN EFFECTS ON PROTEOMIC PROFILING OF BREAST CANCER CELLS: AN UPDATED STUDY

The malignant carcinomas are characterized by several capabilitiesacquired by the neoplastic cells, among which the ability toinvade the extracellular matrix (ECM) and to establish acrosstalk with several ECM components.Under this respect, the extracellular microenvironment is anentity extraordinarily rich of information with opposite signals.Our group has long undertaken the study of the effects of ECMmolecules on the behavior of cancer cells in vitro. Among thestudied molecules, the decorin was found to exert a non-permissiveeffect on the growth and motility of the transfected tumorcells. The decorin, belongs to the family of small leucine-richproteoglycans (SLRP) and is involved physiologically in the fibrillogenesisof collagen. In the last few year, a new anti-oncogenicrole has been proposed for decorin1.This study aimed to implement the knowledge on the effects ofectopic decorin on breast cancer cells, using as a reference pointthe results already achieved by our research group2 on theexperimental model format. By breast cancer cell line 8701-BCand its transfected clone DEC-C2.The extension of the proteomic analysis combined with the massspectrometry, allowed to triplicate the number of identified proteinsin our model. Among the newly identified proteins weremembers of the classes of metabolic enzymes, S100 family andcell motility proteins, which revealed a net decrease in thedecorin transfected cells. Of considerable importance is theobservation that these classes of proteins are the most involvedin metastatic progression. These results confirm and reinforcethe anti-oncogenic role hypothesized for decorin.The work was co-funded by the Italian 5x1000 to COBS.