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

Abstract

The malignant carcinomas are characterized by several capabilities acquired by the neoplastic cells, among which the ability to invade the extracellular matrix (ECM) and to establish a crosstalk with several ECM components. Under this respect, the extracellular microenvironment is an entity extraordinarily rich of information with opposite signals. Our group has long undertaken the study of the effects of ECM molecules on the behavior of cancer cells in vitro. Among the studied molecules, the decorin was found to exert a non-permissive effect on the growth and motility of the transfected tumor cells. The decorin, belongs to the family of small leucine-rich proteoglycans (SLRP) and is involved physiologically in the fibrillogenesis of collagen. In the last few year, a new anti-oncogenic role has been proposed for decorin1. This study aimed to implement the knowledge on the effects of ectopic decorin on breast cancer cells, using as a reference point the results already achieved by our research group2 on the experimental model format. By breast cancer cell line 8701-BC and its transfected clone DEC-C2. The extension of the proteomic analysis combined with the mass spectrometry, allowed to triplicate the number of identified proteins in our model. Among the newly identified proteins were members of the classes of metabolic enzymes, S100 family and cell motility proteins, which revealed a net decrease in the decorin transfected cells. Of considerable importance is the observation that these classes of proteins are the most involved in metastatic progression. These results confirm and reinforce the anti-oncogenic role hypothesized for decorin. The work was co-funded by the Italian 5x1000 to COBS.