NMDA-Dependent Proteolysis of Presynaptic Adhesion Molecule L1 in the Hippocampus by Neuropsin
| Autor: | Ayako Ninomiya, Hironobu Yamasaki, Hideki Tamura, Yukiko Nakamura, Kazumasa Matsumoto-Miyai, Sadao Shiosaka |
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| Rok vydání: | 2003 |
| Předmět: |
Male
N-Methylaspartate Long-Term Potentiation Presynaptic Terminals Hippocampus Neural Cell Adhesion Molecule L1 Biology Receptors N-Methyl-D-Aspartate Cell Line Mice Asymmetric synapse Synaptic augmentation medicine Animals Pyramidal Cells General Neuroscience Long-term potentiation Rats Cell biology medicine.anatomical_structure Synaptic fatigue Schaffer collateral Synapses Synaptic plasticity NMDA receptor Kallikreins Neuroscience Cellular/Molecular |
| Zdroj: | The Journal of Neuroscience. 23:7727-7736 |
| ISSN: | 1529-2401 0270-6474 |
| DOI: | 10.1523/jneurosci.23-21-07727.2003 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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