UCHL1 is a member of the peptidase C12 family and a thiol protease that hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin to generate the ubiquitin monomer. UCHL1 is expressed in the neurons and in cells of the diffuse neuroendocrine system. Mutations in UCHL1 may be associated with Parkinson disease. The ligase and hydrolase activities of UCHL1 may play roles in proteasomal protein degradation, a process critical for neuronal health. Inhibition of UCHL1 in mouse hippocampal slices reduces normal synaptic function and long-term potentiation. PKA-CREB pathway mediates the effects of UCHL1 on Amyloid-beta-induced synaptic dysfunction and Uchl1 also reversed the inhibition of CREB phosphorylation induced by Amyloid-beta.
The assumption that each enzyme expresses a single enzymatic activity in vivo is challenged by the linkage of the neuronal enzyme ubiquitin C-terminal hydrolase-L1 (UCH-L1) to Parkinson's disease (PD). UCH-L1, especially those variants linked to higher susceptibility to PD, causes
The neuronal ubiquitin/proteasomal pathway has been implicated in the pathogenesis of Alzheimer's disease (AD). We now show that a component of the pathway, ubiquitin C-terminal hydrolase L1 (Uch-L1), is required for normal synaptic and cognitive function. Transduction of Uch-L1 protein
International journal of molecular sciences, 24(12) (2023-06-28)
Aspirin (ASA) is a popular nonsteroidal anti-inflammatory drug (NSAID), which exerts its therapeutic properties through the inhibition of cyclooxygenase (COX) isoform 2 (COX-2), while the inhibition of COX-1 by ASA results in the formation of gastrointestinal side effects. Due to
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