| http://purl.uniprot.org/citations/24072707 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24072707 | http://www.w3.org/2000/01/rdf-schema#comment | "The vacuolar H(+) ATPases (V-ATPases) are ATP-driven proton pumps that transport protons across both intracellular and plasma membranes. Previous studies have implicated V-ATPases in the invasiveness of various cancer cell lines. In this study, we evaluated the role of V-ATPases in the invasiveness of two closely matched human breast cancer lines. MCF10a cells are a non-invasive, immortalized breast epithelial cell line, and MCF10CA1a cells are a highly invasive, H-Ras-transformed derivative of MCF10a cells selected for their metastatic potential. Using an in vitro Matrigel assay, MCF10CA1a cells showed a much higher invasion than the parental MCF10a cells. Moreover, this increased invasion was completely sensitive to the specific V-ATPase inhibitor concanamycin. MCF10CA1a cells expressed much higher levels of both a1 and a3 subunit isoforms relative to the parental line. Isoforms of subunit a are responsible for subcellular localization of V-ATPases, with a3 and a4 targeting V-ATPases to the plasma membrane of specialized cells. Knockdown of either a3 alone or a3 and a4 together using isoform-specific siRNAs inhibited invasion by MCF10CA1a cells. Importantly, overexpression of a3 but not the other a subunit isoforms greatly increased the invasiveness of the parental MCF10a cells. Similarly, overexpression of a3 significantly increased expression of V-ATPases at the plasma membrane. These studies suggest that breast tumor cells employ particular a subunit isoforms to target V-ATPases to the plasma membrane, where they function in tumor cell invasion."xsd:string |
| http://purl.uniprot.org/citations/24072707 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m113.503771"xsd:string |
| http://purl.uniprot.org/citations/24072707 | http://purl.uniprot.org/core/author | "Forgac M."xsd:string |
| http://purl.uniprot.org/citations/24072707 | http://purl.uniprot.org/core/author | "Capecci J."xsd:string |
| http://purl.uniprot.org/citations/24072707 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/24072707 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/24072707 | http://purl.uniprot.org/core/pages | "32731-32741"xsd:string |
| http://purl.uniprot.org/citations/24072707 | http://purl.uniprot.org/core/title | "The function of vacuolar ATPase (V-ATPase) a subunit isoforms in invasiveness of MCF10a and MCF10CA1a human breast cancer cells."xsd:string |
| http://purl.uniprot.org/citations/24072707 | http://purl.uniprot.org/core/volume | "288"xsd:string |
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