By regulating the ubiquitination and deubiquitination of key proteins, ubiquitin-proteasome system mediates a variety of cellular activities. Ubiquitin C-terminal hydrolase (UCH) is a deubiquitinating enzyme which can remove ubiquitin chains at the end of ubiquited proteins. The abnormal expression of UCH has been found in a variety of tumor tissues, indicating that it participates in the process of tumor development. Here we review the characteristics of UCH members and current understanding about the role of UCH in tumor development, and the potential target for cancer treatment.
Carcinogenesis ; Disease Progression ; Humans ; Neoplasms ; Ubiquitin ; Ubiquitin Thiolesterase

Humans ; Protein Binding ; genetics ; Protein Structure, Secondary ; Ubiquitin Thiolesterase ; genetics ; metabolism ; Ubiquitin-Specific Peptidase 7

Ubiquitin C-terminal hydrolase L1 (UCH-L1) is a deubiquitinating enzyme that is highly expressed in neurons, and gathering evidence indicates that UCH-L1 may play pathogenic roles in many neurodegenerative disorders such as Alzheimer's disease and Parkinson's disease (PD). Additionally, lipid rafts have attracted interest in neurodegeneration as playing a common role in many neurodegenerative diseases. In the present study, we demonstrated that UCH-L1 associates with lipid rafts as with other PD-associated gene products. In addition, UCH-L1 regulates lipid raft-dependent endocytosis and it is not dependent on the expression and degradation of caveolin-1 or flotillin-1. Finally, UCH-L1 regulates cell-to-cell transmission of α-synuclein. This study provides evidence that many PD-associated gene products share common signaling pathways to explain the pathogenesis of PD.
alpha-Synuclein ; Alzheimer Disease ; Caveolin 1 ; Endocytosis* ; Neurodegenerative Diseases ; Neurons ; Parkinson Disease ; Prion Diseases ; Ubiquitin Thiolesterase* ; Ubiquitin*

OBJECTIVE: α-synuclein, Nogo-A and Ubiquitin C-terminal hydrolase L1 (UCH-L1) have neuromodulatory roles for human brain. Therefore, abnormalities of these molecules are associated with neuropsychiatric disorders. Although some serum studies in the other disorders have been made, serum study of α-synuclein, Nogo-A and UCH-L1 is not present in patients with schizophrenia and healthy controls. Therefore, our aim was to compare serum levels of α-synuclein, Nogo-A and UCH-L1 of the patients with schizophrenia and healthy controls. METHODS: Forty-four patients with schizophrenia who is followed by psychotic disorders unit, and 40 healthy control were included in this study. Socio-demographic form and Positive and Negative Syndrome Scale (PANSS) was applied to patients, and sociodemographic form was applied to control group. Fasting bloods were collected and the serum levels of α-synuclein, Nogo-A and UCH-L1 were measured by ELISA method. RESULTS: Serum α-synuclein [patient: 12.73 (5.18–31.84) ng/mL; control: 41.77 (15.12–66.98) ng/mL], Nogo-A [patient: 33.58 (3.09–77.26) ng/mL; control: 286.05 (136.56–346.82) ng/mL] and UCH-L1 [patient: 5.26 (1.64–10.87) ng/mL; control: 20.48 (11.01–20.81) ng/mL] levels of the patients with schizophrenia were significianly lower than healthy controls (p<0.001). CONCLUSION: Our study results added new evidence for explaining the etiopathogenesis of schizophrenia on the basis of neurochemical markers.
Biomarkers ; Brain ; Enzyme-Linked Immunosorbent Assay ; Fasting ; Humans ; Methods ; Psychotic Disorders ; Schizophrenia* ; Ubiquitin Thiolesterase

Apoptosis of abnormal oocytes is essential for defective oocyte elimination during prepubertal ovary development, and the ubiquitin system regulates the cell apoptosis via the degradation of specific proteins. Ubiquitin carboxyl-terminal hydrolase L1 (UCH-L1) is a component of the ubiquitin system, and the UCH-L1-dependent apoptosis is important for spermatogenesis. In the present study, the change in the number of follicles and the expression of UCH-L1 in oocytes were determined in prepubertal mouse ovaries by immunohistochemical techniques. A significant decrease in the follicular pool was found in prepubertal mouse ovaries during the period of day 21 to day 28 after birth, and accordingly, the UCH-L1 protein expression was increased, to some degree in association with Jun activation domain-binding protein 1 (Jab1) and cyclin-dependent kinase inhibitor p27(Kipl). The increased UCH-L1 protein, together with the corresponding changes of Jab1 was detected in morphologically abnormal oocytes of prepubertal ovaries. Through the immunofluorescent colocalization, UCH-L1 was shown concentrating in abnormal oocytes, and a parallel change in Jab1 was also seen. The affinity analysis confirmed the interaction between UCH-L1 and Jab1 in ovaries. These results suggest that UCH-L1 plays an important role, possibly in association with Jab1 and p27(Kipl), in selective elimination of abnormal oocytes during mouse prepubertal development.
Animals ; Apoptosis ; Female ; Mice ; Oocytes ; cytology ; Ovary ; enzymology ; Ubiquitin Thiolesterase ; metabolism

Bone Cysts, Aneurysmal/pathology* ; Fasciitis/pathology* ; Gene Rearrangement ; Humans ; Ubiquitin Thiolesterase

Humans ; Child ; Myeloid-Lymphoid Leukemia Protein/genetics* ; Precursor Cell Lymphoblastic Leukemia-Lymphoma ; Ubiquitin Thiolesterase

Humans ; Fasciitis/pathology* ; Fibroma/pathology* ; Gene Rearrangement ; Proto-Oncogene Proteins/genetics* ; Ubiquitin Thiolesterase

OBJECTIVETo ascertain whether a coding mutation (Ile93Met) in ubiquitin carboxy-terminal hydrolase (UCH-L1) gene plays a role in idiopathic Parkinson's disease (IPD).

METHODSPolymerase chain reaction-restriction fragment length polymorphism assay (PCR-RFLP) was used to distinguish the wild-type (two DNA fragments of 34 and 126 bp) from the variant allele (three fragments of 34, 60 and 66 bp) because the mutation created a new site for restriction endonuclease BsmF1. DNA was isolated from various blood samples using a phenolchloroform extraction.

RESULTSIle93Met substitution was found neither in PD patients nor in controls.

CONCLUSIONSOur study suggested that Ile93Met of UCH-L1 gene did not influence risk of IPD.

Aged ; Amino Acid Substitution ; Female ; Humans ; Male ; Middle Aged ; Mutation ; Parkinson Disease ; genetics ; Thiolester Hydrolases ; genetics ; physiology ; Ubiquitin Thiolesterase

Head injury is a common presenting complaint amongst emergency department patients. To date, there has been no widespread utilization of neuro-biomarkers to aid the diagnosis of traumatic brain injury. This review article explores which neuro-biomarkers could be used in the emergency department in aiding the clinical diagnosis of mild traumatic brain injury. Based on the available evidence, the most promising neuro-biomarkers appear to be Glial fibrillary acidic protein (GFAP) and Ubiquitin C-Terminal Hydrolase Isozyme L1 (UCH-L1) as these show significant rises in peripheral blood levels shortly after injury and these have been demonstrated to correlate with long-term clinical outcomes. Treatment strategies for minor traumatic brain injury in the emergency department setting are not well developed. The introduction of blood neuro-biomarkers could reduce unnecessary radiation exposure and provide an opportunity to improve the care of this patient group.
Biomarkers ; Brain Concussion ; Brain Injuries* ; Craniocerebral Trauma ; Diagnosis* ; Emergency Service, Hospital ; Glial Fibrillary Acidic Protein ; Humans ; Radiation Exposure ; Ubiquitin Thiolesterase