Ubiquitin carboxy-terminal hydrolase L1 - physiology and pathology.
UCHL1
human
ubiquitin carboxy-terminal hydrolase L1
Journal
Cell biochemistry and function
ISSN: 1099-0844
Titre abrégé: Cell Biochem Funct
Pays: England
ID NLM: 8305874
Informations de publication
Date de publication:
Jul 2020
Jul 2020
Historique:
received:
21
11
2019
revised:
20
02
2020
accepted:
11
03
2020
pubmed:
25
3
2020
medline:
21
5
2021
entrez:
25
3
2020
Statut:
ppublish
Résumé
Ubiquitin C-terminal hydrolase 1 (UCHL1) is an enzyme unique for its multiple activity - both ligase and hydrolase. UCHL1 was first identified as an abundant protein found in the brain and testes, however its expression is not limited to the neuronal compartment. UCHL1 is also highly expressed in carcinomas of various tissue origins, including those from brain, lung, breast, kidney, colon, prostate, pancreas and mesenchymal tissues. Loss-of-function studies and an inhibitor for UCHL1 confirmed the importance of UCHL1 for cancer therapy. So far biological significance of UCHL1 was described in the following processes: spermatogenesis, oncogenesis, angiogenesis, cell proliferation and differentiation in skeletal muscle, inflammation, tissue injury, neuronal injury and neurodegeneration.
Substances chimiques
UCHL1 protein, human
0
Ubiquitin Thiolesterase
EC 3.4.19.12
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
533-540Informations de copyright
© 2020 John Wiley & Sons Ltd.
Références
Matuszczak E, Tylicka M, Debek W, Hermanowicz A, Ostrowska H. The comparison of C-proteasome activity in the plasma of children after burn injury, mild head injury and blunt abdominal trauma. Adv Med Sci. 2015;60(2):253-258.
Tylicka M, Matuszczak E, Dębek W, Hermanowicz A, Ostrowska H. Circulating proteasome activity following mild head injury in children. Childs Nerv Syst. 2014;30(7):1191-1196. https://doi.org/10.1007/s00381-014-2409-4.
Matuszczak E, Tylicka M, Hermanowicz A, Debek W, Sankiewicz A, Gorodkiewicz E. Application of SPR imaging biosensor for the measurement of 20S proteasomes in blood plasma of children with thermal injury. Ann Clin Lab Sci. 2016;46(4):407-411.
Matuszczak E, Tylicka M, Dębek W, Sankiewicz A, Gorodkiewicz E, Hermanowicz A. Overexpression of ubiquitin carboxyl-terminal hydrolase L1 (UCHL1) in serum of children after thermal injury. Adv Med Sci. 2017;62(1):83-86. https://doi.org/10.1016/j.advms.2016.07.004.
Matuszczak E, Tylicka M, Dębek W, Tokarzewicz A, Gorodkiewicz E, Hermanowicz A. Concentration of UHCL1 in the serum of children with acute appendicitis, before and after surgery, and its correlation with CRP and prealbumin. J Invest Surg. 2018;31(2):136-141. https://doi.org/10.1080/08941939.2017.1282559.
Matuszczak E, Sankiewicz A, Debek W, Gorodkiewicz E, Milewski R, Hermanowicz A. Immunoproteasome in the blood plasma of children with acute appendicitis, and its correlation with proteasome and UCHL1 measured by SPR imaging biosensors. Clin Exp Immunol. 2018;191(1):125-132. https://doi.org/10.1111/cei.13056.
Toliczenko-Bernatowicz D, Matuszczak E, Tylicka M, et al. Overexpression of ubiquitin carboxyl-terminal hydrolase 1 (UCHL1) in boys with cryptorchidism. PLoS One. 2018;13(2):e0191806. https://doi.org/10.1371/journal.pone.0191806 eCollection 2018.
Matuszczak E, Weremijewicz A, Komarowska M, et al. Immunoproteasome in the plasma of pediatric patients with moderate and major burns, and its correlation with proteasome and UCHL1 measured by SPR imaging biosensors. J Burn Care Res. 2018;39(6):948-953. https://doi.org/10.1093/jbcr/iry011.
Jara JH, Frank DD, Özdinler PH. Could dysregulation of UPS be a common underlying mechanism for cancer and neurodegeneration? Lessons from UCHL1. Cell Biochem Biophys. 2013;67(1):45-53. https://doi.org/10.1007/s12013-013-9631-7.
Weathington N, Mallampalli RK. Emerging therapies targeting the ubiquitin proteasome system in cancer. J Clin Invest. 2014;124(1):6-12.
Câmara ML, Almeida TB, de Santi F, et al. Fluoxetine-induced androgenic failure impairs the seminiferous tubules integrity and increases ubiquitin carboxyl-terminal hydrolase L1 (UCHL1): possible androgenic control of UCHL1 in germ cell death? Biomed Pharmacother. 2019;109:1126-1139. https://doi.org/10.1016/j.biopha.2018.10.034.
Toliczenko-Bernatowicz D, Matuszczak E, Tylicka M, et al. 20S proteasome in the blood plasma of boys with cryptorchidism. J Endocrinol Invest. 2018;41(9):1103-1106. https://doi.org/10.1007/s40618-018-0851-y.
Kwon J. The new function of two ubiquitin C-terminal hydrolase isozymes as re-ciprocal modulators of germ cell apoptosis. Exp Anim. 2007;56:71-77.
Kwon J, Wang YL, Setsuie R, et al. Two closely related ubiquitin C-terminal hydrolase iso-zymes function as reciprocal modulators of germ cell apoptosis in cryptorchid testis. Am J Pathol. 2004;165:1367-1374. https://doi.org/10.1016/S0002-9440(10)63394-9.
Wang YL, Liu W, Sun YJ, et al. Overexpression of ubiquitin carboxyl-terminal hydrolase L1 arrests spermatogenesis in transgenic mice. Mol Reprod Dev. 2006;73:40-49.
Hershko A. Ubiquitin-mediated protein degradation. J Biol Chem. 1988;263:15237-15240.
Fang Y, Shen X. Ubiquitin carboxyl-terminal hydrolases: involvement in cancer progression and clinical implications. Cancer Metastasis Rev. 2017;36(4):669-682. https://doi.org/10.1007/s10555-017-9702-0.
Reyes-Turcu FE, Ventii KH, Wilkinson KD. Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes. Annu Rev Biochem. 2009;78:363-397.
Sowa ME, Bennett EJ, Gygi SP, Harper JW. Defining the human deubiquitinating enzyme interaction landscape. Cell. 2009;138(2):389-403.
Hussain S, Foreman O, Perkins SL, et al. The de-ubiquitinase UCH-L1 is an oncogene that drives the development of lymphoma in vivo by deregulating PHLPP1 and Akt signaling. Leukemia. 2010;24(9):1641-1655.
Bishop P, Rocca D, Henley JM. Ubiquitin C-terminal hydrolase L1 (UCH-L1): structure, distribution and roles in brain function and dysfunction. Biochem J. 2016;473(16):2453-2462.
Tezel E, Hibi K, Nagasaka T, Nakao A. PGP9.5 as a prognostic factor in pancreatic cancer. Clin Cancer Res. 2000;6:4764-4767.
Yamazaki T, Hibi K, Takase T, et al. PGP9.5 as a marker for invasive colorectal cancer. Clin Cancer Res. 2002;8:192-195.
Miyoshi Y, Nakayama S, Torikoshi Y, et al. High expression of ubiquitin carboxy-terminal hydrolase-L1 and -L3 mRNA predicts early recurrence in patients with invasive breast cancer. Cancer Sci. 2006;97:523-529. https://doi.org/10.1111/j.1349-7006.2006.00202.x.
Yu J, Tao Q, Cheung KF, et al. Epigenetic identification of ubiquitin carboxyl-terminal hydrolase L1 as a functional tumor suppressor and biomarker for hepatocellular carcinoma and other digestive tumors. Hepatology. 2008;48(2):508-518. https://doi.org/10.1002/hep.22343.
Yamashita K, Park HL, Kim MS, et al. PGP9.5 methylation in diffuse-type gastric cancer. Cancer Res. 2006;66(7):3921-3927. https://doi.org/10.1158/0008-5472.CAN-05-1511.
Jin C, Yu W, Lou X, et al. UCHL1 is a putative tumor suppressor in ovarian cancer cells and contributes to cisplatin resistance. J Cancer. 2013;4(8):662-670. https://doi.org/10.7150/jca.6641.
Li L, Tao Q, Jin H, et al. The tumor suppressor UCHL1 forms a complex with p53/MDM2/ARF to promote p53 signaling and is frequently silenced in nasopharyngeal carcinoma. Clin Cancer Res. 2010;16(11):2949-2958. https://doi.org/10.1158/1078-0432.CCR-09-3178.
Ummanni R, Jost E, Braig M, et al. Ubiquitin carboxyl-terminal hydrolase 1 (UCHL1) is a potential tumour suppressor in prostate cancer and is frequently silenced by promoter methylation. Mol Cancer. 2011;10:129. https://doi.org/10.1186/1476-4598-10-129.
Mandelker DL, Yamashita K, Tokumaru Y, et al. PGP9.5 promoter methylation is an independent prognostic factor for esophageal squamous cell carcinoma. Cancer Res. 2005;65(11):4963-4968. https://doi.org/10.1158/0008-5472.CAN-04-3923.
Xiang T, Li L, Yin X, et al. The ubiquitin peptidase UCHL1 induces G0/G1 cell cycle arrest and apoptosis through stabilizing p53 and is frequently silenced in breast cancer. PLoS One. 2012;7(1):e29783. https://doi.org/10.1371/journal.pone.0029783.
Kagara I, Enokida H, Kawakami K, et al. CpG hypermethylation of the UCHL1 gene promoter is associated with pathogenesis and poor prognosis in renal cell carcinoma. J Urol. 2008;180(1):343-351.
Seliger B, Handke D, Schabel E, Bukur J, Lichtenfels R, Dammann R. Epigenetic control of the ubiquitin carboxyl terminal hydrolase 1 in renal cell carcinoma. J Transl Med. 2009;7:90.
Tokumaru Y, Yamashita K, Kim MS, et al. The role of PGP9.5 as a tumor suppressor gene in human cancer. Int J Cancer. 2008;123(4):753-759.
Fukutomi S, Seki N, Koda K, Miyazaki M. Identification of methylation-silenced genes in colorectal cancer cell lines: genomic screening using oligonucleotide arrays. Scand J Gastroenterol. 2007;42(12):1486-1494.
Mizukami H, Shirahata A, Goto T, Sakata M, Saito M, et al. PGP9.5 methylation as a marker for metastatic colorectal cancer. Anticancer Res. 2008;28(5A):2697-2700.
Abdelmaksoud-Dammak R, Saadallah-Kallel A, MiladiAbdennadher I, Ayedi L, Khabir A, et al. CpG methylation of ubiquitin carboxyl-terminal hydrolase 1 (UCHL1) and P53 mutation pattern in sporadic colorectal cancer. Tumour Biol. 2016;37(2):1707-1714.
Hibi K, Liu Q, Beaudry GA, et al. Serial analysis of gene expression in non-small cell lung cancer. Cancer Res. 1998;58(24):5690-5694.
Kusakabe M, Kutomi T, Watanabe K, et al. Identification of G0S2 as a gene frequently methylated in squamous lung cancer by combination of in silico and experimental approaches. Int J Cancer. 2010;126(8):1895-1902.
Finnerty BM, Moore M, Verma A, et al. UCHL1 loss alters the cell-cycle in metastatic pancreatic neuroendocrine tumors. Endocr Relat Cancer. 2019;26(4):411-423. https://doi.org/10.1530/ERC-18-0507.
Hibi K, Kodera Y, Ito K, Akiyama S, Shirane M, Nakao A. Plasminogen activator inhibitor-1 is a downstream mediator of the PGP9.5-related oncogenic pathway in esophageal squamous cell carcinoma. Anticancer Res. 2004;24(6):3731-3734.
Yang H, Zhang C, Fang S, Ou R, Li W, Xu Y. UCH-LI acts as a novel prognostic biomarker in gastric cardiac adenocarcinoma. Int J Clin Exp Pathol. 2015;8(11):13957-13967.
Orr KS, Shi Z, Brown WM, et al. Potential prognostic marker ubiquitin carboxyl-terminal hydrolase-L1 does not predict patient survival in non-small cell lung carcinoma. J Exp Clin Cancer Res. 2011;30:79.
Akishima-Fukasawa Y, Ino Y, Nakanishi Y, et al. Significance of PGP9.5 expression in cancer-associated fibroblasts for prognosis of colorectal carcinoma. Am J Clin Pathol. 2010;134(1):71-79.
Zhong J, Zhao M, Ma Y, et al. UCHL1 acts as a colorectal cancer oncogene via activation of the β-catenin/TCF pathway through its deubiquitinating activity. Int J Mol Med. 2012;30(2):430-436.
Mastoraki A, Ioannidis E, Apostolaki A, Patsouris E, Aroni K. PGP 9.5 and cyclin D1 coexpression in cutaneous squamous cell carcinomas. Int J Surg Pathol. 2009;17(6):413-420.
Truran PP, Johnson SJ, Bliss RD, Lennard TW, Aspinall SR. Parafibromin, galectin-3, PGP9.5, Ki67, and cyclin D1: using an immunohistochemical panel to aid in the diagnosis of parathyroid cancer. World J Surg. 2014;38(11):2845-2854.
Kim HJ, Magesh V, Lee JJ, Kim S, Knaus UG, Lee KJ. Ubiquitin C-terminal hydrolase-L1 increases cancer cell invasion by modulating hydrogen peroxide generated via NADPH oxidase 4. Oncotarget. 2015;6(18):16287-16303.
Zheng S, Qiao G, Min D, et al. Heterogeneous expression and biological function of ubiquitin carboxy-terminal hydrolase-L1 in osteosarcoma. Cancer Lett. 2015;359(1):36-46.
Nakao K, Hirakawa T, Suwa H, et al. High expression of ubiquitin C-terminal hydrolase L1 is associated with poor prognosis in endometrial cancer patients. Int J Gynecol Cancer. 2018;28(4):675-683. https://doi.org/10.1097/IGC.0000000000001201.
Sanchez-Diaz PC, Chang JC, Moses ES, Dao T, Chen Y, Hung JY. Ubiquitin carboxyl-terminal esterase L1 (UCHL1) is associated with stem-like cancer cell functions in pediatric high-grade glioma. PLoS One. 2017;12(5):e0176879. https://doi.org/10.1371/journal.pone.0176879 eCollection 2017.
Goto Y, Zeng L, Yeom CJ, et al. UCHL1 provides diagnostic and antimetastatic strategies due to its deubiquitinating effect on HIF-1α. Nat Commun. 2015;6:6153. https://doi.org/10.1038/ncomms7153.
Jin Y, Zhang W, Xu J, et al. UCH-L1 involved in regulating the degradation of EGFR and promoting malignant properties in drug-resistant breast cancer. Int J Clin Exp Pathol. 2015;8(10):12500-12508.
Shang D, Han T, Xu X, Liu Y. Decitabine induces G2/M cell cycle arrest by suppressing p38/NF-κB signaling in human renal clear cell carcinoma. Int J Clin Exp Pathol. 2015;8(9):11140-11148.
Brinkmann K, Zigrino P, Witt A, et al. Ubiquitin C-terminal hydrolase-L1 potentiates cancer chemosensitivity by stabilizing NOXA. Cell Rep. 2013;3(3):881-891. https://doi.org/10.1016/j.celrep.2013.02.014.
Gu Y, Lv F, Xue M, et al. The deubiquitinating enzyme UCHL1 is a favorable prognostic marker in neuroblastoma as it promotes neuronal differentiation. J Exp Clin Cancer Res. 2018;37(1):258. https://doi.org/10.1186/s13046-018-0931-z.
Moore MD, Finnerty B, Gray KD, et al. Decreased UCHL1 expression as a cytologic biomarker for aggressive behavior in pancreatic neuroendocrine tumors. Surgery. 2018;163(1):226-231. https://doi.org/10.1016/j.surg.2017.04.040.
Song IK, Kim HJ, Magesh V, Lee KJ. Ubiquitin C-terminal hydrolase-L1 plays a key role in angiogenesis by regulating hydrogen peroxide generated by NADPH oxidase 4. Biochem Biophys Res Commun. 2018;495(1):1567-1572. https://doi.org/10.1016/j.bbrc.2017.11.051.
Pan Y, Appukuttan B, Mohs K, Ashander LM, Smith JR. Ubiquitin carboxyl-terminal esterase L1 promotes proliferation of human choroidal and retinal endothelial cells. Asia Pac J Ophthalmol. 2015;4(1):51-55. https://doi.org/10.1097/APO.0000000000000109.
Gao H, Freeling J, Wu P, Liang AP, Wang X, Li Y. UCHL1 regulates muscle fibers and mTORC1 activity in skeletal muscle. Life Sci. 2019;233:116699. https://doi.org/10.1016/j.lfs.2019.116699.
Vasu VT, Ott S, Hobson B, et al. Sarcolipin and ubiquitin carboxy-terminal hydrolase 1 mRNAs are over-expressed in skeletal muscles of alpha-tocopherol deficient mice. Free Radic Res. 2009;43(2):106-116. https://doi.org/10.1080/10715760802616676.
Powis RA, Mutsaers CA, Wishart TM, Hunter G, Wirth B, Gillingwater TH. Increased levels of UCHL1 are a compensatory response to disrupted ubiquitin homeostasis in spinal muscular atrophy and do not represent a viable therapeutic target. Neuropathol Appl Neurobiol. 2014;40(7):873-887. https://doi.org/10.1111/nan.12168.
Gao H, Hartnett S, Li Y. Ubiquitin C-terminal hydrolase L1 regulates myoblast proliferation and differentiation. Biochem Biophys Res Commun. 2017;492(1):96-102. https://doi.org/10.1016/j.bbrc.2017.08.027.
Ichikawa T, Li J, Dong X, et al. Ubiquitin carboxyl terminal hydrolase L1 negatively regulates TNFalpha-mediated vascular smooth muscle cell proliferation via suppressing ERK activation. Biochem Biophys Res Commun. 2010;391(1):852-856. https://doi.org/10.1016/j.bbrc.2009.11.151.
Gu Y, Ding X, Huang J, et al. The deubiquitinating enzyme UCHL1 negatively regulates the immunosuppressive capacity and survival of multipotent mesenchymal stromal cells. Cell Death Dis. 2018;9(5):459. https://doi.org/10.1038/s41419-018-0532-y.
Fellenberg J, Lehner B, Witte D. Silencing of the UCHL1 gene in giant cell tumors of bone. Int J Cancer. 2010;127:1804-1812. https://doi.org/10.1002/ijc.2520.
Karim R, Tummers B, Meyers C, et al. Human papillomavirus (HPV) upregulates the cellular deubiquitinase UCHL1 to suppress the keratinocyte's innate immune response. PLoS Pathog. 2013;9:e1003384. https://doi.org/10.1371/journal.ppat.1003384.
Takami Y, Nakagami H, Morishita R, et al. Ubiquitin carboxyl-terminal hydrolase L1, a novel deubiquitinating enzyme in the vasculature, attenuates NF-kappaB activation. Arterioscler Thromb Vasc Biol. 2007;27:2184-2190. https://doi.org/10.1161/ATVBAHA.107.142505.
Lefaki M, Papaevgeniou N, Chondrogianni N. Redox regulation of proteasome function. Redox Biol. 2017;13:452-458. https://doi.org/10.1016/j.redox.2017.07.005.
Liu Y, Wu J, Wu H, et al. UCH-L1 expression of podocytes in diseased glomeruli and in vitro. J Pathol. 2009;217(5):642-653. https://doi.org/10.1002/path.2511.
Zhang H, Mao X, Sun Y, et al. NF-κB upregulates ubiquitin C-terminal hydrolase 1 in diseased podocytes in glomerulonephritis. Mol Med Rep. 2015;12(2):2893-2901. https://doi.org/10.3892/mmr.2015.3780.
Brackeva B, De Punt V, Kramer G, et al. Potential of UCHL1 as biomarker for destruction of pancreatic beta cells. J Proteomics. 2015;117:156-167. https://doi.org/10.1016/j.jprot.2015.01.009.
Higashi T, Friedman SL, Hoshida Y. Hepatic stellate cells as key target in liver fibrosis. Adv Drug Deliv Rev. 2017;121:27-42. https://doi.org/10.1016/j.addr.2017.05.007.
Liu H, Povysheva N, Rose ME, et al. Role of UCHL1 in axonal injury and functional recovery after cerebral ischemia. Proc Natl Acad Sci U S A. 2019;116:4643-4650. https://doi.org/10.1073/pnas.1821282116.
Pukaß K, Richter-Landsberg C. Inhibition of UCH-L1 in oligodendroglial cells results in microtubule stabilization and prevents α-synuclein aggregate formation by activating the autophagic pathway: implications for multiple system atrophy. Front Cell Neurosci. 2015;9:163.
Liu H, Li W, Rose ME, et al. The point mutation UCH-L1 C152A protects primary neurons against cyclopentenone prostaglandin-induced cytotoxicity: implications for post-ischemic neuronal injury. Cell Death Dis. 2015;6:e1966.
Sakurai M, Sekiguchi M, Zushida K, et al. Reduction in memory in passive avoidance learning, exploratory behaviour and synaptic plasticity in mice with a spontaneous deletion in the ubiquitin C-terminal hydrolase L1 gene. Eur J Neurosci. 2008;27:691-701.
Liu H, Li W, Ahmad M, et al. Modification of ubiquitin-C-terminal hydrolase-L1 by cyclopentenone prostaglandins exacerbates hypoxic injury. Neurobiol Dis. 2011;41:318-328.
Singh GP, Nigam R, Tomar GS, et al. Early and rapid detection of UCHL1 in the serum of brain-trauma patients: a novel gold nanoparticle-based method for diagnosing the severity of brain injury. Analyst. 2018;143(14):3366-3373. https://doi.org/10.1039/c8an00533h.
Gong B, Cao Z, Zheng P, et al. Ubiquitin hydrolase Uch-L1 rescues beta-amyloid-induced decreases in synaptic function and contextual memory. Cell. 2006;126:775-788.
Calzada B, Naves FJ, Del Valle ME, et al. Distribution of protein gene product 9.5 (PGP 9.5) immunoreactivity in the dorsal root ganglia of adult rat. Ann Anat. 1994;176(5):437-441.
Schofield JN, Day IN, Thompso RJ, et al. PGP9.5, a ubiquitin C-terminal hydrolase; pattern of mRNA and protein expression during neural development in the mouse. Brain Res. 1995;85(2):229-238.
Todi SV, Paulson HL. Balancing act: Deubiquitinating enzymes in the nervous system. Trends Neurosci. 2011;34(7):370-382.
Gestwicki JE, Garza D. Protein quality control in neurodegenerative disease. Prog Mol Biol Transl Sci. 2012;107:327-353.
Gong B, Radulovic M, Figueiredo-Pereira ME, Cardozo C. The ubiquitin-proteasome system: potential therapeutic targets for alzheimer's disease and spinal cord injury. Front Mol Neurosci. 2016;9:4.
Yamazaki K, Wakasugi N, Tomita T, Kikuchi T, Mukoyama M, Ando K. Gracile axonal dystrophy (GAD), a new neurological mutant in the mouse. Proc Soc Exp Biol Med. 1988;187:209-215.
Bilguvar K, Tyagi NK, Ozkara C, et al. Recessive loss of function of the neuronal ubiquitin hydrolase UCHL1 leads to early-onset progressive neurodegeneration. Proc Natl Acad Sci U S A. 2013;110:3489-3494.
Goto A, Wang YL, Kabuta T, et al. Proteomic and histochemical analysis of proteins involved in the dying-back-type of axonal degeneration in the gracile axonal dystrophy (gad) mouse. Neurochem Int. 2009;54:330-338.
Ross CA, Poirier MA. Protein aggregation and neurodegenerative disease. Nat Med. 2004;10(Suppl):S10-S17. https://doi.org/10.1038/nm1066.
Tofaris GK, Spillantini MG. Alpha-synuclein dysfunction in Lewy body diseases. Mov Disord. 2005;20(Suppl 12):S37-S44. https://doi.org/10.1002/mds.20538.
Nagamine S, Kabuta T, Furuta A, Yamamoto K, Takahashi A, Wada K. Deficiency of ubiquitin carboxy-terminal hydrolase-L1 (UCH-L1) leads to vulnerability to lipid peroxidation. Neurochem Int. 2010;57:102-110. https://doi.org/10.1016/j.neuint.2010.04.015.
Das C, Hoang QQ, Kreinbring CA, et al. Structural basis for conformational plasticity of the Parkinson's disease-associated ubiquitin hydrolase UCH-L1. Proc Natl Acad Sci U S A. 2006;103:4675-4680. https://doi.org/10.1073/pnas.0510403103.
Barrachina M, Castano E, Dalfo E, Maes T, Buesa C, Ferrer I. Reduced ubiquitin C-terminal hydrolase-1 expression levels in dementia with Lewy bodies. Neurobiol Dis. 2006;22(2):265-273.
Cartier AE, Djakovic SN, Salehi A, Wilson SM, Masliah E, Patrick GN. Regulation of synaptic structure by ubiquitin C-terminal hydrolase L1. J Neurosci. 2009;29(24):7857-7868.
Zhu S, Wuolikainen A, Wu J, et al. Targeted multiple reaction monitoring analysis of CSF identifies UCHL1 and GPNMB as candidate biomarkers for ALS. J Mol Neurosci. 2019;69(4):643-657.
Donovan LE, Higginbotham L, Dammer EB, et al. Analysis of a membrane-enriched proteome from postmortem human brain tissue in Alzheimer's disease. Proteomics Clin Appl. 2012;6:201-211. https://doi.org/10.1002/prca.201100068.
Kim HJ, Kim HJ, Jeong JE, et al. N-terminal truncated UCH-L1 prevents Parkinson's disease associated damage. PLoS One. 2014;9:e99654. https://doi.org/10.1371/journal.pone.0099654.
Leroy E, Boyer R, Auburger G, et al. The ubiquitin pathway in Parkinson's disease. Nature. 1998;395:451-452. https://doi.org/10.1038/26652.