Abstract
Synaptic plasticity requires an activity-dependent, rapid, and long-lasting modification of synaptic character, including morphology and coupling strength. Here we show that a serine protease, neuropsin, directly and specifically modifies the synaptic adhesion molecule L1, which was localized to the presynaptic site of the asymmetric synapse in the mouse hippocampus. Increased neural activity triggered the rapid, transient activation of the precursor form of neuropsin in an NMDA receptor-dependent manner. The activated neuropsin immediately cleaved L1 and released a neuropsin-specific extracellular 180 kDa fragment. This neuropsin-specific L1-cleaving system is involved in NMDA receptor-dependent synaptic plasticity, such as the Schaffer collateral long-term potentiation.
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{'key': '2023022307583618000_23.21.7727.50', 'first-page': '405', 'volume': '3', 'year': '1999', 'journal-title': 'Int J Mol Med'}
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Dates
Type | When |
---|---|
Created | 7 years, 4 months ago (April 12, 2018, 7:25 p.m.) |
Deposited | 2 years, 6 months ago (Feb. 23, 2023, 11:09 a.m.) |
Indexed | 1 month, 1 week ago (July 30, 2025, 10:47 a.m.) |
Issued | 22 years ago (Aug. 27, 2003) |
Published | 22 years ago (Aug. 27, 2003) |
Published Online | 22 years ago (Aug. 27, 2003) |
Published Print | 22 years ago (Aug. 27, 2003) |
@article{Matsumoto_Miyai_2003, title={NMDA-Dependent Proteolysis of Presynaptic Adhesion Molecule L1 in the Hippocampus by Neuropsin}, volume={23}, ISSN={1529-2401}, url={http://dx.doi.org/10.1523/jneurosci.23-21-07727.2003}, DOI={10.1523/jneurosci.23-21-07727.2003}, number={21}, journal={The Journal of Neuroscience}, publisher={Society for Neuroscience}, author={Matsumoto-Miyai, Kazumasa and Ninomiya, Ayako and Yamasaki, Hironobu and Tamura, Hideki and Nakamura, Yukiko and Shiosaka, Sadao}, year={2003}, month=aug, pages={7727–7736} }