0000000000584296
AUTHOR
S. Minafra
Decorin transfection induces proteomic modulation and cytoskeletal rioganization in breast cancer cells (8701-BC)
LARGE-SCALE COMPARATIVE PROTEOMICS OF BREAST CANCER SURGICAL TISSUES
Gene ontology-based annotation and comparative analysis of proteins extracted from proteomics of 100 breast cancer patients.
Background: Current clinical parameters for breast cancer diagnosis and therapy are: tumour size, axillary lymph node status, histological grading and presence or absence of metastases. Prognostic/predictive properties, such as oestrogen and progesterone receptor status, and human epidermal growth factor receptor (HER-2/neu) status are currently used for therapeutic decision. Conversely, it is now emerging that the number of genetic mutations and epigenetic deregulations in cancer is far more higher than previously thought. Therefore, proteomic screening for differential protein expression in subsets of tumor samples is an essential tool for generating data bases and biomarker discovery. Th…
NEW PROTEOMIC EVIDENCE ON DECORIN EFFECTS ON BREAST CANCER CELLS
The estabilishment of a dinamic crosstyalk between the malignant cells and several components of the ECM is a crucial step of the tumor progression. The aim of the present study was to improve the knowledge about the effects of ectopic decorin on the breast cancer cells, starting from our previous proteomic studies. The new proteomic evidences strenghteh the anti-oncogenic effects of decorin and hilight the attention on the decreased expression of the majority of the members of three protein classes closely related to the malignant phenotype: the metabolic enzymes, the S100 family and the cell motility proteins
DECORIN EFFECTS ON PROTEOMIC PROFILING OF BREAST CANCER CELLS: AN UPDATED STUDY
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 involv…
BEHAVIOVRAL CHANGES OF BREAST CANCER CELLS IN VITRO
Decorin transfection induces proteomic and phenotypic modulation in breast cancer cells 8701-BC
Decorin is a prototype member of the small leucine-rich proteoglycan family widely distributed in the extracellular matrices of many connective tissues, where it has been shown to play multiple important roles in the matrix assembly process, as well as in some cellular activities. A major interest for decorin function concerns its role in tumorigenesis, as growth-inhibitor of different neoplastic cells, and potential antimetastatic agent. The aim of our research was to investigate wide-ranged effects of transgenic decorin on breast cancer cells. To this purpose we utilized the well-characterized 8701-BC cell line, isolated from a ductal infiltrating carcinoma of the breast, and two derived …
Large-scale comparative proteomics of breast surgical tissues
Permissive and restrictive influences from breast cancer stroma
The turn-over of extracellular matrix is a physiological process, that in normal conditions and in wound healing respond to spatial and temporal regulatory mechanisms, involving several cell-matrix interaction pathways. Profound changes occur both at cellular and extracellular level, during the progression of various forms of invasive carcinomas. Collagen alterations and cellular effects. The ultrastructural and biochemical analyses of the collagenous stroma of invasive ductal breast carcinoma have demonstrated the occurrence of extensive fragmentation of pre-existing collagen fibrils and new deposition of thinner fibrils formed mostly by 1(I)3 homotrimer collagen of type I [1-3], which app…