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• W2071531606 abstract "The Akt/protein kinase B (PKB) serine/threonine kinase is well known as an important mediator of many cell survival signaling pathways. Here, we demonstrate for the first time a major role of Akt/PKB in the cell invasion properties of the highly metastatic cell line HT1080. Using confocal microscopic analyses of live samples, we found Akt/PKB to be localized in the leading edge membrane area of migrating HT1080 cells. This localization was dependent on phosphoinositide 3-kinase and required the lipid binding ability of the phosphoinositide binding pleckstrin homology domain of Akt/PKB. We examined the possible function of Akt/PKB in HT1080 invasion. Surprisingly, Akt/PKB potently promoted HT1080 invasion, by increasing cell motility and matrix metalloproteinase-9 (MMP-9) production, in a manner highly dependent on its kinase activity and membrane-translocating ability. The increase in MMP-9 production was mediated by activation of nuclear factor-kappaB transcriptional activity by Akt/PKB. However, Akt/PKB did not affect the cell-cell or cell-matrix adhesion properties of HT1080. Our findings thus establish Akt/PKB as a major factor in the invasive abilities of cancer cells." @default.
• W2071531606 created "2016-06-24" @default.
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• W2071531606 date "2001-09-01" @default.
• W2071531606 modified "2023-10-08" @default.
• W2071531606 title "Akt/PKB promotes cancer cell invasion via increased motility and metalloproteinase production" @default.
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• W2071531606 doi "https://doi.org/10.1096/fj.01-0198com" @default.
• W2071531606 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11532975" @default.
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