http://purl.uniprot.org/citations/19330798 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/19330798 | http://www.w3.org/2000/01/rdf-schema#comment | "Elevated expression of p130(Cas)/BCAR1 (breast cancer anti estrogen resistance 1) in human breast tumors is a marker of poor prognosis and poor overall survival. Specifically, p130(Cas) signaling has been associated with antiestrogen resistance, for which the mechanism is currently unknown. TAM-R cells, which were established by long-term exposure of estrogen (E(2))-dependent MCF-7 cells to tamoxifen, displayed elevated levels of total and activated p130(Cas). Here we have investigated the effects of p130(Cas) inhibition on growth factor signaling in tamoxifen resistance. To inhibit p130(Cas), a phosphorylated substrate domain of p130(Cas), that acts as a dominant-negative (DN) p130(Cas) molecule by blocking signal transduction downstream of the p130(Cas) substrate domain, as well as knockdown by siRNA was employed. Interference with p130(Cas) signaling/expression induced morphological changes, which were consistent with a more epithelial-like phenotype. The phenotypic reversion was accompanied by reduced migration, attenuation of the ERK and phosphatidylinositol 3-kinase/Akt pathways, and induction of apoptosis. Apoptosis was accompanied by downregulation of the expression of the anti-apoptotic protein Bcl-2. Importantly, these changes re-sensitized TAM-R cells to tamoxifen treatment by inducing cell death. Therefore, our findings suggest that targeting the product of the BCAR1 gene by a peptide which mimics the phosphorylated substrate domain may provide a new molecular avenue for treatment of antiestrogen resistant breast cancers."xsd:string |
http://purl.uniprot.org/citations/19330798 | http://purl.org/dc/terms/identifier | "doi:10.1002/jcb.22136"xsd:string |
http://purl.uniprot.org/citations/19330798 | http://purl.uniprot.org/core/author | "August A."xsd:string |
http://purl.uniprot.org/citations/19330798 | http://purl.uniprot.org/core/author | "Kirsch K.H."xsd:string |
http://purl.uniprot.org/citations/19330798 | http://purl.uniprot.org/core/author | "Soni S."xsd:string |
http://purl.uniprot.org/citations/19330798 | http://purl.uniprot.org/core/author | "Nicholson R.I."xsd:string |
http://purl.uniprot.org/citations/19330798 | http://purl.uniprot.org/core/author | "Lin B.T."xsd:string |
http://purl.uniprot.org/citations/19330798 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
http://purl.uniprot.org/citations/19330798 | http://purl.uniprot.org/core/name | "J Cell Biochem"xsd:string |
http://purl.uniprot.org/citations/19330798 | http://purl.uniprot.org/core/pages | "364-375"xsd:string |
http://purl.uniprot.org/citations/19330798 | http://purl.uniprot.org/core/title | "Expression of a phosphorylated p130(Cas) substrate domain attenuates the phosphatidylinositol 3-kinase/Akt survival pathway in tamoxifen resistant breast cancer cells."xsd:string |
http://purl.uniprot.org/citations/19330798 | http://purl.uniprot.org/core/volume | "107"xsd:string |
http://purl.uniprot.org/citations/19330798 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/19330798 |
http://purl.uniprot.org/citations/19330798 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/19330798 |
http://purl.uniprot.org/uniprot/#_P56945-mappedCitation-19330798 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19330798 |
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http://purl.uniprot.org/uniprot/#_Q6P5Z4-mappedCitation-19330798 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19330798 |
http://purl.uniprot.org/uniprot/#_Q96CD4-mappedCitation-19330798 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19330798 |
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http://purl.uniprot.org/uniprot/B3KW85 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/19330798 |