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- W2145280442 abstract "Ubiquitin carboxyl-terminal hydrolase L1 (UCH-L1, aka PGP9.5) is an abundant, neuronal deubiquitinating enzyme that has also been suggested to possess E3 ubiquitin-protein ligase activity and/or stabilize ubiquitin monomers in vivo . Recent evidence implicates dysregulation of UCH-L1 in the pathogenesis and progression of human cancers. Although typically only expressed in neurons, high levels of UCH-L1 have been found in many nonneuronal tumors, including breast, colorectal, and pancreatic carcinomas. UCH-L1 has also been implicated in the regulation of metastasis and cell growth during the progression of nonsmall cell lung carcinoma, colorectal cancer, and lymphoma. Together these studies suggest UCH-L1 has a potent oncogenic role and drives tumor development. Conversely, others have observed promoter methylation-mediated silencing of UCH-L1 in certain tumor subtypes, suggesting a potential tumor suppressor role for UCH-L1. In this paper, we provide an overview of the evidence supporting the involvement of UCH-L1 in tumor development and discuss the potential mechanisms of action of UCH-L1 in oncogenesis." @default.
- W2145280442 created "2016-06-24" @default.
- W2145280442 creator A5000323703 @default.
- W2145280442 creator A5005707464 @default.
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- W2145280442 date "2012-01-01" @default.
- W2145280442 modified "2023-10-14" @default.
- W2145280442 title "Ubiquitin C-Terminal Hydrolase L1 in Tumorigenesis" @default.
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- W2145280442 doi "https://doi.org/10.1155/2012/123706" @default.
- W2145280442 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3395355" @default.
- W2145280442 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22811913" @default.
- W2145280442 hasPublicationYear "2012" @default.
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