QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

HOME  |   SEARCH  |   ARCHIVE  |   SUBSCRIBE  |   CONTACT  |   HELP

The Journal of Neuroscience, August 27, 2003, 23(21):7727-7736

This Article Full Text Full Text (PDF) Submit an eLetter Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in ISI Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via ISI Web of Science (33) Citing Articles via Google Scholar Google Scholar Articles by Matsumoto-Miyai, K. Articles by Shiosaka, S. Search for Related Content PubMed PubMed Citation Articles by Matsumoto-Miyai, K. Articles by Shiosaka, S.

 Previous Article  |  Next Article 

NMDA-Dependent Proteolysis of Presynaptic Adhesion Molecule L1 in the Hippocampus by Neuropsin

Kazumasa Matsumoto-Miyai, Ayako Ninomiya, Hironobu Yamasaki, Hideki Tamura, Yukiko Nakamura, and Sadao Shiosaka

Division of Structural Cell Biology, Nara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan

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.

Key words: serine protease; neuropsin; proteolysis; neural cell adhesion molecule L1; synaptic plasticity; hippocampus; Schaffer collateral long-term potentiation

---

Received Jan 13, 2003; revised April 21, 2003; accepted April 21, 2003.

This article has been cited by other articles:

				Y. Ishikawa, Y. Horii, H. Tamura, and S. Shiosaka Neuropsin (KLK8)-Dependent and -Independent Synaptic Tagging in the Schaffer-Collateral Pathway of Mouse Hippocampus J. Neurosci., January 23, 2008; 28(4): 843 - 849. [Abstract] [Full Text] [PDF]

				O. Bozdagi, V. Nagy, K. T. Kwei, and G. W. Huntley In Vivo Roles for Matrix Metalloproteinase-9 in Mature Hippocampal Synaptic Physiology and Plasticity J Neurophysiol, July 1, 2007; 98(1): 334 - 344. [Abstract] [Full Text] [PDF]

				M. Kishibe, Y. Bando, R. Terayama, K. Namikawa, H. Takahashi, Y. Hashimoto, A. Ishida-Yamamoto, Y.-P. Jiang, B. Mitrovic, D. Perez, et al. Kallikrein 8 Is Involved in Skin Desquamation in Cooperation with Other Kallikreins J. Biol. Chem., February 23, 2007; 282(8): 5834 - 5841. [Abstract] [Full Text] [PDF]

				Y. Nakamura, H. Tamura, K. Horinouchi, and S. Shiosaka Role of neuropsin in formation and maturation of Schaffer-collateral L1cam-immunoreactive synaptic boutons J. Cell Sci., April 1, 2006; 119(7): 1341 - 1349. [Abstract] [Full Text] [PDF]

				H. Tamura, Y. Ishikawa, N. Hino, M. Maeda, S. Yoshida, S. Kaku, and S. Shiosaka Neuropsin is essential for early processes of memory acquisition and Schaffer collateral long-term potentiation in adult mouse hippocampus in vivo J. Physiol., February 1, 2006; 570(3): 541 - 551. [Abstract] [Full Text] [PDF]

				T. Maretzky, M. Schulte, A. Ludwig, S. Rose-John, C. Blobel, D. Hartmann, P. Altevogt, P. Saftig, and K. Reiss L1 Is Sequentially Processed by Two Differently Activated Metalloproteases and Presenilin/{gamma}-Secretase and Regulates Neural Cell Adhesion, Cell Migration, and Neurite Outgrowth Mol. Cell. Biol., October 15, 2005; 25(20): 9040 - 9053. [Abstract] [Full Text] [PDF]

Home  |   Search  |   Archive  |   Subscribe  |   Contact  |   Help