The functions of UCH-L1 and its relation to neurodegenerative diseases

Rieko Setsuie; Keiji Wada

doi:10.1016/j.neuint.2007.05.007

The functions of UCH-L1 and its relation to neurodegenerative diseases

Neurochem Int. 2007 Jul-Sep;51(2-4):105-11. doi: 10.1016/j.neuint.2007.05.007. Epub 2007 May 24.

Authors

Rieko Setsuie¹, Keiji Wada

Affiliation

¹ Department of Degenerative Neurological Diseases, National Institute of Neuroscience, National Center of Neurology and Psychiatry, Kodaira, Tokyo 187-8502, Japan.

PMID: 17586089
DOI: 10.1016/j.neuint.2007.05.007

Abstract

Parkinson's disease (PD) and Alzheimer's disease (AD), the most common neurodegenerative diseases, are caused by both genetic and environmental factors. Ubiquitin carboxy-terminal hydrolase L1 (UCH-L1) is a deubiquitinating enzyme that is involved in the pathogenesis of both of these neurodegenerative diseases. Several functions of UCH-L1, other than as an ubiquitin hydrolase, have been proposed; these include acting as an ubiquitin ligase and stabilizing mono-ubiquitin. This review focuses on recent findings on the functions and the regulation of UCH-L1, in particular those that relate to PD and AD.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Alzheimer Disease / genetics
Alzheimer Disease / metabolism*
Animals
Humans
Mice
Mice, Neurologic Mutants / genetics
Mice, Neurologic Mutants / metabolism
Mutation / genetics
Nerve Degeneration / genetics
Nerve Degeneration / metabolism
Nerve Degeneration / physiopathology
Nerve Tissue Proteins / metabolism
Oxidative Stress / physiology
Parkinson Disease / genetics
Parkinson Disease / metabolism*
Ubiquitin / metabolism
Ubiquitin Thiolesterase / genetics
Ubiquitin Thiolesterase / physiology*

Substances

Nerve Tissue Proteins
UCHL1 protein, human
Ubiquitin
Ubiquitin Thiolesterase