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

Matsumoto‐Miyai, Kazumasa; Ninomiya, Ayako; Yamasaki, Hironobu; Tamura, Hideki; Nakamura, Yukiko; Shiosaka, Sadao

doi:10.1523/jneurosci.23-21-07727.2003

Cited by 128 publications

(130 citation statements)

References 51 publications

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“…Labeling for Nr-CAM, a member of the L1 family of cell adhesion molecules (Crossin and Krushel, 2000;Hortsch, 2000), often was seen in clusters of gold particles in the synaptic cleft, suggesting that the antibodies label molecules linked together across the synaptic cleft. Previous studies have indicated that both Nr-CAM and L1 are presynaptic (Lustig et al, 2001;Matsumoto-Miyai et al, 2003), and these proteins commonly form homophilic bonds between cell processes (Hortsch, 2000;Alberts and Galli, 2003). Furthermore, postsynaptic expression of another L1-family member, neurofascin, may be necessary for the establishment of basket cell axon terminal synapses on cerebellar Purkinje cells (Ango et al, 2004); also another family member is found in dendrites of developing cortical neurons and modulates neuronal positioning and dendrite orientation (Demyanenko et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

“…Another Nr-CAM antibody that was used in our study was characterized bySuter et al (1995; affinity-purified; recognizes extracellular domain; this did not work as well for immunogold and was used in our study for biochemistry only). L1 antibody was characterized byAppel et al (1995;rat monoclonal;amino-acids 818-832; recognizes extracellular domain); L1 distribution in hippocampus was described using a different antibody (Matsumoto-Miyai et al, 2003). Purchased antibodies included SynGAP (see above), N-cadherin (amino acids 802-819; recognizes intracellular domain) and β-catenin (amino acids 571-781); BD/Transduction Laboratories; Lexington, KY, USA and Mississauga, ON, Canada), α-CaMKII (alpha subunit; Stressgen Biotechnologies; Victoria, British Columbia, Canada), and neuroligin (amino acids 1-695; recognizes extracellular domain; Synaptic Systems, Göttingen, Germany); the latter 4 antibodies are mouse monoclonals.…”

Section: Antibodies and Their Characterizationmentioning

confidence: 99%

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Ontogeny of postsynaptic density proteins at glutamatergic synapses

Petralia

Sans

Wang

et al. 2005

Molecular and Cellular Neuroscience

209

196

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In glutamatergic synapses, glutamate receptors (GluRs) associate with many other proteins involved in scaffolding and signal transduction. The ontogeny of these postsynaptic density (PSD) proteins involves changes in their composition during development, paralleling changes in GluR type and function. In the CA1 region of the hippocampus, at postnatal day 2 (P2), many synapses already have a distinct PSD. We used immunoblot analysis, subcellular fractionation, and quantitative immunogold electron microscopy to examine the distribution of PSD proteins during development of the hippocampus. Synapses at P2 contained substantial levels of NR1 and NR2B and most GluRassociated proteins, including SAP102, SynGAP, the chain of proteins from GluRs/SAP102 through GKAP/Shank/Homer and metabotropic glutamate receptors, and the adhesion factors, cadherin, catenin, neuroligin, and Nr-CAM. Development was marked by substantial decreases in NR2B and SAP102 and increases in NR2A, PSD-95, AMPA receptors and CaMKII. Other components showed more moderate changes.

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Section: Discussionmentioning

confidence: 99%

Section: Antibodies and Their Characterizationmentioning

confidence: 99%

Ontogeny of postsynaptic density proteins at glutamatergic synapses

Petralia

Sans

Wang

et al. 2005

Molecular and Cellular Neuroscience

209

196

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“…Each epidermis was homogenized with the extraction buffer containing 60 mM Tris-HCl (pH 8.0), 150 mM NaCl, 1% Nonidet P-40, and 5 mM EDTA and centrifuged at 15,000 ϫ g for 20 min at 4°C. The proteolytic activity of the supernatant was measured as described previously (20,21) with a slight modification. Briefly, 10 g of protein of the epidermal extract was incubated with 100 mM synthetic substrate Boc-Val-Pro-Arg-MCA (VPR-MCA) (Peptide Institute), Boc-Phe-Ser-Arg-MCA (FSR-MCA) (Peptide Institute), and Meo-Suc-Arg-Pro-Tyr-pNA-HCl (RPY-pNA) (Chromogenix AB) in a total volume of 1 ml at 37°C for 2 h with shaking.…”

Section: Methodsmentioning

confidence: 99%

Kallikrein 8 Is Involved in Skin Desquamation in Cooperation with Other Kallikreins

Kishibe

Bandô²,

Terayama³

et al. 2007

Journal of Biological Chemistry

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Kallikrein type serine proteases, KLK8/neuropsin, KLK6, and KLK7, have been implicated in the proliferation and differentiation of epidermal keratinocytes and in the pathogenesis of psoriasis. However, their mechanistic roles in these processes remain largely unknown. We applied 12-O-tetradecanoylphorbol-13-acetate on the wild type (WT) and the Klk8 gene-disrupted (Klk8 ؊/؊ ) mouse skin, inducing keratinocyte proliferation similar to the human psoriatic lesion. Klk8 mRNA as well as Klk6 and Klk7 mRNA were up-regulated after 12-O-tetradecanoylphorbol-13-acetate application in the WT mice. In contrast, Klk8؊/؊ mice showed minimum increases of Klk6 and Klk7 transcripts, the proteins, and enzymatic activities. Relative to the WT, the Klk8 ؊/؊ skin showed less proliferation and an increase in the number of cell layers in the stratum corneum. However, overexpression of Klk8 by adenovirus vector in knock-out keratinocytes did not result in an increase in Klk6 or Klk7 mRNA. The inefficient cleavage of adhesion molecules DSG1 and CDSN in Klk8 ؊/؊ skin contributes to a delay in corneocyte shedding, resulting in the hyperkeratosis phenotype. We propose that in psoriatic lesion, KLK8 modulates hyperproliferation and prevents excessive hyperkeratosis by shedding the corneocytes.

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“…These data suggest that there must be mechanisms for coordinating functional and structural remodeling of synaptic connectivity. Although such mechanisms remain incompletely understood, recent studies indicate that regulated extracellular proteolysis may be important for coupling functional and structural changes in synaptic architecture (Baranes et al 1998;Huang et al 1996;Komai et al 2000;Madani et al 1999;Mataga et al 2004;Matsumoto-Miyai et al 2003;Oray et al 2004;Pang et al 2004;Tamura et al 2006).…”

Section: Introductionmentioning

confidence: 99%

In Vivo Roles for Matrix Metalloproteinase-9 in Mature Hippocampal Synaptic Physiology and Plasticity

Bozdagi

Nagy²,

Kwei³

et al. 2007

Journal of Neurophysiology

159

179

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Bozdagi O, Nagy V, Kwei KT, Huntley GW. In vivo roles for matrix metalloproteinase-9 in mature hippocampal synaptic physiology and plasticity. J Neurophysiol 98: 334 -344, 2007. First published May 9, 2007; doi:10.1152/jn.00202.2007. Extracellular proteolysis is an important regulatory nexus for coordinating synaptic functional and structural plasticity, but the identity of such proteases is incompletely understood. Matrix metalloproteinases (MMPs) have wellknown, mostly deleterious roles in remodeling after injury or stroke, but their role in nonpathological synaptic plasticity and function in intact adult brains has not been extensively investigated. Here we address the role of MMP-9 in hippocampal synaptic plasticity using both gain-and loss-of-function approaches in urethane-anesthetized adult rats. Acute blockade of MMP-9 proteolytic activity with inhibitors or neutralizing antibodies impairs maintenance, but not induction, of long-term potentiation (LTP) at synapses formed between Schaffer-collaterals and area CA1 dendrites. LTP is associated with significant increases in levels of MMP-9 and proteolytic activity within the potentiated neuropil. By introducing a novel application of gelatin-substrate zymography in vivo, we find that LTP is associated with significantly elevated numbers of gelatinolytic puncta in the potentiated neuropil that codistribute with immunolabeling for MMP-9 and for markers of synapses and dendrites. Such increases in proteolytic activity require NMDA receptor activation. Exposing intact area CA1 neurons to recombinant-active MMP-9 induces a slow synaptic potentiation that mutually occludes, and is occluded by, tetanically evoked potentiation. Taken together, our data reveal novel roles for MMP-mediated proteolysis in regulating nonpathological synaptic function and plasticity in mature hippocampus.

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

Cited by 128 publications

References 51 publications

Ontogeny of postsynaptic density proteins at glutamatergic synapses

Ontogeny of postsynaptic density proteins at glutamatergic synapses

Kallikrein 8 Is Involved in Skin Desquamation in Cooperation with Other Kallikreins

In Vivo Roles for Matrix Metalloproteinase-9 in Mature Hippocampal Synaptic Physiology and Plasticity

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