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000153373 041__ $$aEnglish
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000153373 1001_ $$0P:(DE-HGF)0$$aSharma, Amit$$b0
000153373 245__ $$aUbiquitin Carboxyl-Terminal Hydrolases (UCHs): Potential Mediators for Cancer and Neurodegeneration.
000153373 260__ $$aBasel$$bMolecular Diversity Preservation International$$c2020
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000153373 520__ $$aEmerging evidence suggests an inverse association between cancer and neurodegenerative diseases (NDD). Although phenotypically different, both diseases display a significant imbalance in the ubiquitination/deubiquitination processes. Therefore, we particularly investigated the expression of ubiquitin C-terminal hydrolases (UCHs: UCH-L1, UCH-L3, UCH-L5 and BAP1), a subfamily of deubiquitinating enzymes (DUBs), using publically available datasets (GTEx, TCGA) and observed altered expression of UCH-L1, UCH-L3, UCH-L5 in 17 cancer types. Interestingly, UCH-L1 (known to be enriched in neurons and interacting with the Parkinson's disease-associated protein α-synuclein) appeared to be a prognostic indicator of unfavorable outcome in endometrial and urothelial cancer, while increased expression of UCH-L3 and UCH-L5 was associated with poor survival in liver and thyroid cancer, respectively. In normal tissues, UCH-L1 was found to be strongly expressed in the cerebral cortex and hypothalamus, while UCH-L3 expression was somewhat higher in the testis. The occurrence of mutation rates in UCHs also suggests that BAP1 and UCH-L5 may play a more dominant role in cancers than UCH-L1 and UCH-L3. We also characterized the functional context and configuration of the repeat elements in the promoter of DUBs genes and found that UCHs are highly discriminatory for catabolic function and are mainly enriched with LINE/CR1 repeats. Regarding the thesis of an inverse association between cancer and NDD, we observed that among all DUBs, UCHs are the one most involved in both entities. Considering a putative therapeutic potential based on presumed common mechanisms, it will be useful to determine whether other DUBs can compensate for the loss of UCH activity under physiological conditions. However, experimental evidence is required to substantiate this argument.
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000153373 650_2 $$2MeSH$$aBrain: metabolism
000153373 650_2 $$2MeSH$$aDatabases, Genetic
000153373 650_2 $$2MeSH$$aGene Expression Profiling
000153373 650_2 $$2MeSH$$aGene Expression Regulation
000153373 650_2 $$2MeSH$$aHumans
000153373 650_2 $$2MeSH$$aNeoplasms: enzymology
000153373 650_2 $$2MeSH$$aNeurodegenerative Diseases: enzymology
000153373 650_2 $$2MeSH$$aPhenotype
000153373 650_2 $$2MeSH$$aPrognosis
000153373 650_2 $$2MeSH$$aProtein Domains
000153373 650_2 $$2MeSH$$aTumor Suppressor Proteins: metabolism
000153373 650_2 $$2MeSH$$aUbiquitin Thiolesterase: genetics
000153373 650_2 $$2MeSH$$aUbiquitin Thiolesterase: metabolism
000153373 650_2 $$2MeSH$$aUbiquitination
000153373 7001_ $$0P:(DE-HGF)0$$aLiu, Hongde$$b1
000153373 7001_ $$0P:(DE-HGF)0$$aTobar-Tosse, Fabian$$b2
000153373 7001_ $$aChand Dakal, Tikam$$b3
000153373 7001_ $$0P:(DE-HGF)0$$aLudwig, Michael$$b4
000153373 7001_ $$aHolz, Frank G$$b5
000153373 7001_ $$0P:(DE-HGF)0$$aLoeffler, Karin U$$b6
000153373 7001_ $$0P:(DE-2719)2000056$$aWüllner, Ullrich$$b7$$udzne
000153373 7001_ $$0P:(DE-HGF)0$$aHerwig-Carl, Martina C$$b8$$eCorresponding author
000153373 773__ $$0PERI:(DE-600)2019364-6$$a10.3390/ijms21113910$$gVol. 21, no. 11, p. 3910 -$$n11$$p3910 -$$tInternational journal of molecular sciences$$v21$$x1422-0067$$y2020
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