Abstract:
:The major breakthrough discovery of enkephalins as endogenous opiates led our attempts to determine their inactivation mechanisms. Because the NH2-terminal tyrosine is absolutely necessary for the neuropeptides to exert analgesic effects, and aminopeptidase activities are extraordinarily high in the brain, a specific "amino-enkephalinase" should exist. Several aminopeptidases were identified in the central nervous system during the search. In fact, our laboratory found two novel neuron-specific aminopeptidases: NAP and NAP-2. NAP is the only functionally active brain-specific enzyme known. Its synaptic location coupled with its limited substrate specificity could constitute a "functional" specificity and contribute to enkephalin-specific functions. In addition, NAP was found to be essential for neuron growth, differentiation, and death. Thus, aminopeptidases are likely important for mental health and neurological diseases. Recently, puromycin-sensitive aminopeptidase (PSA) was identified as a modifier of tau-induced neurodegeneration. Because the enzymatic similarity between PSA and NAP, we believe that the depletion of NAP in Alzheimer's disease (AD) brains plays a causal role in the development of AD pathology. Therefore, use of the puromycin-sensitive neuron-aminopeptidase NAP could provide neuroprotective mechanisms in AD and similar neurodegenerative diseases.
journal_name
Neurochem Resjournal_title
Neurochemical researchauthors
Hui KSdoi
10.1007/s11064-007-9356-3subject
Has Abstractpub_date
2007-12-01 00:00:00pages
2062-71issue
12eissn
0364-3190issn
1573-6903journal_volume
32pub_type
杂志文章,评审abstract::Calcium-naive synaptosomes were used to assess the effects of divalent cations on [3H]acetylcholine release from rat hippocampal homogenates. Following equilibration with calcium-free buffer (containing 10 microM EGTA), calcium reversibly increased [3H]acetylcholine efflux (up to five-fold) while causing no measurable...
journal_title:Neurochemical research
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