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1.
Elife ; 102021 03 02.
Article in English | MEDLINE | ID: mdl-33650489

ABSTRACT

Axon navigation depends on the interactions between guidance molecules along the trajectory and specific receptors on the growth cone. However, our in vitro and in vivo studies on the role of Endoglycan demonstrate that in addition to specific guidance cue - receptor interactions, axon guidance depends on fine-tuning of cell-cell adhesion. Endoglycan, a sialomucin, plays a role in axon guidance in the central nervous system of chicken embryos, but it is neither an axon guidance cue nor a receptor. Rather, Endoglycan acts as a negative regulator of molecular interactions based on evidence from in vitro experiments demonstrating reduced adhesion of growth cones. In the absence of Endoglycan, commissural axons fail to properly navigate the midline of the spinal cord. Taken together, our in vivo and in vitro results support the hypothesis that Endoglycan acts as a negative regulator of cell-cell adhesion in commissural axon guidance.


Subject(s)
Axon Guidance/physiology , Growth Cones/physiology , Mucins/pharmacology , Animals , Axons/physiology , Cell Adhesion/drug effects , Chick Embryo , HEK293 Cells , Humans , RNA Interference , Spinal Cord/embryology
2.
Dev Neurobiol ; 77(8): 963-974, 2017 09.
Article in English | MEDLINE | ID: mdl-28033683

ABSTRACT

Axonal growth and guidance rely on correct growth cone responses to guidance cues, both in the central nervous system (CNS) and in the periphery. Unlike the signaling cascades that link axonal growth to cytoskeletal dynamics, little is known about the cross-talk mechanisms between guidance and membrane dynamics and turnover in the axon. Our studies have shown that Netrin-1/deleted in colorectal cancer signaling triggers exocytosis through the SNARE Syntaxin-1 (STX-1) during the formation of commissural pathways. However, limited in vivo evidence is available about the role of SNARE proteins in motor axonal guidance. Here we show that loss-of-function of SNARE complex members results in motor axon guidance defects in fly and chick embryos. Knock-down of Syntaxin-1, VAMP-2, and SNAP-25 leads to abnormalities in the motor axon routes out of the CNS. Our data point to an evolutionarily conserved role of the SNARE complex proteins in motor axon guidance, thereby pinpointing an important function of SNARE proteins in axonal navigation in vivo. © 2016 Wiley Periodicals, Inc. Develop Neurobiol 77: 963-974, 2017.


Subject(s)
Avian Proteins/metabolism , Axons/metabolism , Drosophila Proteins/metabolism , Motor Neurons/metabolism , Neuronal Outgrowth/physiology , SNARE Proteins/metabolism , Animals , Chick Embryo , Drosophila melanogaster , Immunohistochemistry , Species Specificity
3.
Biochem J ; 453(1): 83-100, 2013 Jul 01.
Article in English | MEDLINE | ID: mdl-23560819

ABSTRACT

The serine peptidase neurotrypsin is stored in presynaptic nerve endings and secreted in an inactive zymogenic form by synaptic activity. After activation, which requires activity of postsynaptic NMDA (N-methyl-D-aspartate) receptors, neurotrypsin cleaves the heparan sulfate proteoglycan agrin at active synapses. The resulting C-terminal 22-kDa fragment of agrin induces dendritic filopodia, which are considered to be precursors of new synapses. In the present study, we investigated the role of GAGs (glycosaminoglycans) in the activation of neurotrypsin and neurotrypsin-dependent agrin cleavage. We found binding of neurotrypsin to the GAG side chains of agrin, which in turn enhanced the activation of neurotrypsin by proprotein convertases and resulted in enhanced agrin cleavage. A similar enhancement of neurotrypsin binding to agrin, neurotrypsin activation and agrin cleavage was induced by the four-amino-acid insert at the y splice site of agrin, which is crucial for the formation of a heparin-binding site. Non-agrin GAGs also contributed to binding and activation of neurotrypsin and, thereby, to agrin cleavage, albeit to a lesser extent. Binding of neurotrypsin to cell-surface glycans locally restricts its conversion from zymogen into active peptidase. This provides the molecular foundation for the local action of neurotrypsin at or in the vicinity of its site of synaptic secretion. By its local action at synapses with correlated pre- and post-synaptic activity, the neurotrypsin-agrin system fulfils the requirements for a mechanism serving experience-dependent modification of activated synapses, which is essential for adaptive structural reorganizations of neuronal circuits in the developing and/or adult brain.


Subject(s)
Agrin/metabolism , Glycosaminoglycans/pharmacology , Presynaptic Terminals/metabolism , Serine Endopeptidases/metabolism , Animals , Binding Sites , COS Cells , Chlorocebus aethiops , Enzyme Activation , Glycosaminoglycans/metabolism , HEK293 Cells , Humans , Proprotein Convertases/metabolism , Syndecan-2/pharmacology
4.
Curr Protoc Cell Biol ; 61: 9.5.1-9.5.85, 2013 Dec 02.
Article in English | MEDLINE | ID: mdl-24510806

ABSTRACT

Cell-cell adhesion is a fundamental requirement for all multicellular organisms. The calcium-independent cell adhesion molecules of the immunoglobulin superfamily (IgSF-CAMs) represent a major subgroup. They consist of immunoglobulin folds alone or in combination with other protein modules, often fibronectin type-III folds. More than 100 IgSF-CAMs have been identified in vertebrates and invertebrates. Most of the IgSF-CAMs are cell surface molecules that are membrane-anchored either by a single transmembrane segment or by a glycosylphosphatidylinositol (GPI) anchor. Some of the IgSF-CAMs also occur in soluble form, e.g., in the cerebrospinal fluid or in the vitreous fluid of the eye, due to naturally occurring cleavage of the GPI anchor or the membrane-proximal peptide segment. Some IgSF-CAMs, such as NCAM, occur in various forms that are generated by alternative splicing. This unit contains a series of protocols that have been used to study the function of IgSF-CAMs in vitro and in vivo.


Subject(s)
Biochemistry/methods , Cell Adhesion Molecules/metabolism , Fibronectins/metabolism , Immunoglobulins/metabolism , Intercellular Junctions/immunology , Nerve Growth Factors/metabolism , Animals , Cell Adhesion , Cell Adhesion Molecules/chemistry , Cell Adhesion Molecules/genetics , Cell Culture Techniques , Cell Line, Tumor , Fibronectins/chemistry , Fibronectins/genetics , HEK293 Cells , Humans , Immunoglobulins/chemistry , Immunoglobulins/genetics , Mice , Mice, Inbred BALB C , Receptor Cross-Talk , Signal Transduction
5.
Biol Open ; 1(8): 761-74, 2012 Aug 15.
Article in English | MEDLINE | ID: mdl-23213470

ABSTRACT

Endocytosis of amyloid-ß precursor protein (APP) is thought to represent the major source of substrate for the production of the amyloidogenic Aß peptide by the ß-secretase BACE1. The irreversible nature of proteolytic cleavage implies the existence of an efficient replenishment route for APP from its sites of synthesis to the cell surface. We recently found that APP exits the trans-Golgi network in intimate association with calsyntenin-1, a transmembrane cargo-docking protein for Kinesin-1-mediated vesicular transport. Here we characterized the function of calsyntenin-1 in neuronal APP transport using selective immunoisolation of intracellular trafficking organelles, immunocytochemistry, live-imaging, and RNAi. We found that APP is co-transported with calsyntenin-1 along axons to early endosomes in the central region of growth cones in carriers that exclude the α-secretase ADAM10. Intriguingly, calsyntenin-1/APP organelles contained BACE1, suggesting premature cleavage of APP along its anterograde path. However, we found that APP contained in calsyntenin-1/APP organelles was stable. We further analyzed vesicular trafficking of APP in cultured hippocampal neurons, in which calsyntenin-1 was reduced by RNAi. We found a markedly increased co-localization of APP and ADAM10 in axons and growth cones, along with increased proteolytic processing of APP and Aß secretion in these neurons. This suggested that the reduced capacity for calsyntenin-1-dependent APP transport resulted in mis-sorting of APP into additional axonal carriers and, therefore, the premature encounter of unprotected APP with its ectodomain proteases. In combination, our results characterize calsyntenin-1/APP organelles as carriers for sheltered anterograde axonal transport of APP.

6.
Neural Dev ; 7: 36, 2012 Nov 09.
Article in English | MEDLINE | ID: mdl-23140504

ABSTRACT

BACKGROUND: Axons navigate to their future synaptic targets with the help of choice points, intermediate targets that express axon guidance cues. Once they reach a choice point, axons need to switch their response from attraction to repulsion in order to move on with the next stage of their journey. The mechanisms underlying the change in axonal responsiveness are poorly understood. Commissural axons become sensitive to the repulsive activity of Slits when they cross the ventral midline of the CNS. Responsiveness to Slits depends on surface expression of Robo receptors. In Drosophila, Commissureless (Comm) plays a crucial regulatory role in midline crossing by keeping Robo levels low on precommissural axons. Interestingly, to date no vertebrate homolog of comm has been identified. Robo3/Rig1 has been shown to control Slit sensitivity before the midline, but without affecting Robo1 surface expression. RESULTS: We had identified RabGDI, a gene linked to human mental retardation and an essential component of the vesicle fusion machinery, in a screen for differentially expressed floor-plate genes. Downregulation of RabGDI by in ovo RNAi caused commissural axons to stall in the floor plate, phenocopying the effect observed after downregulation of Robo1. Conversely, premature expression of RabGDI prevented commissural axons from entering the floor plate. Furthermore, RabGDI triggered Robo1 surface expression in cultured commissural neurons. Taken together, our results identify RabGDI as a component of the switching mechanism that is required for commissural axons to change their response from attraction to repulsion at the intermediate target. CONCLUSION: RabGDI takes over the functional role of fly Comm by regulating the surface expression of Robo1 on commissural axons in vertebrates. This in turn allows commissural axons to switch from attraction to repulsion at the midline of the spinal cord.


Subject(s)
Axons/physiology , Gene Expression Regulation, Developmental , Guanine Nucleotide Dissociation Inhibitors/metabolism , Nerve Tissue Proteins/metabolism , Neurons/cytology , Receptors, Immunologic/metabolism , Spinal Cord , Animals , Cell Line, Transformed , Cell Movement/genetics , Chick Embryo , Chlorocebus aethiops , Functional Laterality/genetics , Guanine Nucleotide Dissociation Inhibitors/genetics , Humans , RNA Interference/physiology , Spinal Cord/cytology , Spinal Cord/embryology , Spinal Cord/growth & development , Transfection , Transportation , Roundabout Proteins
7.
FASEB J ; 25(12): 4378-93, 2011 Dec.
Article in English | MEDLINE | ID: mdl-21885656

ABSTRACT

Etiology and pathogenesis of sarcopenia, the progressive decline in skeletal muscle mass and strength that occurs with aging, are still poorly understood. We recently found that overexpression of the neural serine protease neurotrypsin in motoneurons resulted in the degeneration of their neuromuscular junctions (NMJ) within days. Therefore, we wondered whether neurotrypsin-dependent NMJ degeneration also affected the structure and function of the skeletal muscles. Using histological and functional analyses of neurotrypsin-overexpressing and neurotrypsin-deficient mice, we found that overexpression of neurotrypsin in motoneurons installed the full sarcopenia phenotype in young adult mice. Characteristic muscular alterations included a reduced number of muscle fibers, increased heterogeneity of fiber thickness, more centralized nuclei, fiber-type grouping, and an increased proportion of type I fibers. As in age-dependent sarcopenia, excessive fragmentation of the NMJ accompanied the muscular alterations. These results suggested the destabilization of the NMJ through proteolytic cleavage of agrin at the onset of a pathogenic pathway ending in sarcopenia. Studies of neurotrypsin-deficient and agrin-overexpressing mice revealed that old-age sarcopenia also develops without neurotrypsin and is not prevented by elevated levels of agrin. Our results define neurotrypsin- and age-dependent sarcopenia as the common final outcome of 2 etiologically distinct entities.


Subject(s)
Agrin/metabolism , Neuromuscular Junction/metabolism , Sarcopenia/etiology , Sarcopenia/metabolism , Aging/metabolism , Aging/pathology , Agrin/genetics , Animals , Female , Humans , Mice , Mice, Knockout , Mice, Transgenic , Motor Neurons/metabolism , Motor Neurons/pathology , Muscle Fibers, Fast-Twitch/metabolism , Muscle Fibers, Fast-Twitch/pathology , Muscle Fibers, Slow-Twitch/metabolism , Muscle Fibers, Slow-Twitch/pathology , Muscle, Skeletal/metabolism , Muscle, Skeletal/pathology , Neuromuscular Junction/pathology , Proteolysis , Receptors, Cholinergic/metabolism , Recombinant Proteins/genetics , Recombinant Proteins/metabolism , Sarcopenia/pathology , Serine Endopeptidases/deficiency , Serine Endopeptidases/genetics , Serine Endopeptidases/metabolism
8.
J Cell Sci ; 123(Pt 22): 3944-55, 2010 Nov 15.
Article in English | MEDLINE | ID: mdl-20980386

ABSTRACT

During the initial stage of neuromuscular junction (NMJ) formation, nerve-derived agrin cooperates with muscle-autonomous mechanisms in the organization and stabilization of a plaque-like postsynaptic specialization at the site of nerve-muscle contact. Subsequent NMJ maturation to the characteristic pretzel-like appearance requires extensive structural reorganization. We found that the progress of plaque-to-pretzel maturation is regulated by agrin. Excessive cleavage of agrin via transgenic overexpression of an agrin-cleaving protease, neurotrypsin, in motoneurons resulted in excessive reorganizational activity of the NMJs, leading to rapid dispersal of the synaptic specialization. By contrast, expression of cleavage-resistant agrin in motoneurons slowed down NMJ remodeling and delayed NMJ maturation. Neurotrypsin, which is the sole agrin-cleaving protease in the CNS, was excluded as the physiological agrin-cleaving protease at the NMJ, because NMJ maturation was normal in neurotrypsin-deficient mice. Together, our analyses characterize agrin cleavage at its proteolytic α- and ß-sites by an as-yet-unspecified protease as a regulatory access for relieving the agrin-dependent constraint on endplate reorganization during NMJ maturation.


Subject(s)
Agrin/metabolism , Neuromuscular Junction/metabolism , Serine Endopeptidases/metabolism , Animals , Cell Line , HEK293 Cells , HeLa Cells , Humans , Mice , Mice, Transgenic , Motor Neurons/metabolism , Nerve Fibers/metabolism , Serine Endopeptidases/biosynthesis , Spinal Cord/cytology , Synaptic Transmission/physiology
9.
Proteomics ; 10(21): 3775-88, 2010 Nov.
Article in English | MEDLINE | ID: mdl-20925061

ABSTRACT

Kinesin motors play crucial roles in the delivery of membranous cargo to its destination and thus for the establishment and maintenance of cellular polarization. Recently, calsyntenin-1 was identified as a cargo-docking protein for Kinesin-1-mediated axonal transport of tubulovesicular organelles along axons of central nervous system neurons. To further define the function of calsyntenin-1, we immunoisolated calsyntenin-1 organelles from murine brain homogenates and determined their proteome by MS. We found that calsyntenin-1 organelles are endowed with components of the endosomal trafficking machinery and contained the ß-amyloid precursor protein (APP). Detailed biochemical analyses of calsyntenin-1 immunoisolates in conjunction with immunocytochemical colocalization studies with cultured hippocampal neurons, using endosomal marker proteins for distinct subcompartments of the endosomal pathways, indicated that neuronal axons contain at least two distinct, nonoverlapping calsyntenin-1-containing transport packages: one characterized as early-endosomal, APP positive, the other as recycling-endosomal, APP negative. We postulate that calsyntenin-1 acts as a general mediator of anterograde axonal transportation of endosomal vesicles. In this role, calsyntenin-1 may actively contribute to axonal growth and pathfinding in the developing as well as to the maintenance of neuronal polarity in the adult nervous system; further, it may actively contribute to the stabilization of APP during its anterograde axonal trajectory.


Subject(s)
Axons/metabolism , Biological Transport/physiology , Calcium-Binding Proteins/metabolism , Endosomes/chemistry , Proteomics/methods , Amyloid beta-Protein Precursor/chemistry , Amyloid beta-Protein Precursor/metabolism , Animals , Calcium-Binding Proteins/chemistry , Electrophoresis, Polyacrylamide Gel , Endocytosis/physiology , Endosomes/metabolism , Hippocampus/cytology , Hippocampus/metabolism , Immunohistochemistry , Kinesins/chemistry , Kinesins/metabolism , Mice , Prosencephalon/cytology , Prosencephalon/metabolism
10.
Cell ; 136(6): 1161-71, 2009 Mar 20.
Article in English | MEDLINE | ID: mdl-19303856

ABSTRACT

The synaptic serine protease neurotrypsin is essential for cognitive function, as its deficiency in humans results in severe mental retardation. Recently, we demonstrated the activity-dependent release of neurotrypsin from presynaptic terminals and proteolytical cleavage of agrin at the synapse. Here we show that the activity-dependent formation of dendritic filopodia is abolished in hippocampal neurons from neurotrypsin-deficient mice. Administration of the neurotrypsin-dependent 22 kDa fragment of agrin rescues the filopodial response. Detailed analyses indicated that presynaptic action potential firing is necessary for the release of neurotrypsin, whereas postsynaptic NMDA receptor activation is necessary for the neurotrypsin-dependent cleavage of agrin. This contingency characterizes the neurotrypsin-agrin system as a coincidence detector of pre- and postsynaptic activation. As the resulting dendritic filopodia are thought to represent precursors of synapses, the neurotrypsin-dependent cleavage of agrin at the synapse may be instrumental for a Hebbian organization and remodeling of synaptic circuits in the CNS.


Subject(s)
Agrin/metabolism , Dendrites/metabolism , Hippocampus/cytology , Presynaptic Terminals , Pseudopodia/metabolism , Serine Endopeptidases/metabolism , Animals , Cell Line , Exocytosis , Hippocampus/metabolism , Humans , In Vitro Techniques , Mice , Mice, Transgenic , Mutagenesis , Serine Endopeptidases/genetics
11.
Protein Expr Purif ; 61(1): 13-21, 2008 Sep.
Article in English | MEDLINE | ID: mdl-18577456

ABSTRACT

An increasing number of studies indicate that serine proteases play an important role in structural plasticity associated with learning and memory formation. Neurotrypsin is a multidomain serine protease located at the presynaptic terminal of neurons. It is thought to be crucial for cognitive brain functions. A deletion in the neurotrypsin gene causes severe mental retardation in humans. For a biochemical characterization, we produced murine neurotrypsin recombinantly in a eukaryotic expression system using myeloma cells. From the culture medium we purified neurotrypsin using heparin-, hydrophobic interaction- and immobilized metal affinity chromatography. For an enzymological characterization two fragments of agrin containing the natural cleavages sites of neurotrypsin were used as substrates. The highest catalytic activity of neurotrypsin was observed in the pH range between 7.0 and 8.5. Calcium ions were required for neurotrypsin activity and an ionic strength exceeding 500 mM decreased substrate cleavage. Site-specific mutations of the amino acids flanking the scissile bonds showed that cleavage is highly specific and requires a basic amino acid preceded by a glutamate residue on the N-terminal side of the scissile bond. This sequence requirement argues for a unique substrate binding pocket of neurotrypsin. This observation was further substantiated by the fact that almost all tested serine protease inhibitors except dichloroisocoumarin and PMSF did not affect neurotrypsin activity.


Subject(s)
Serine Endopeptidases/isolation & purification , Amino Acid Sequence , Animals , Chromatography, Gel , Electrophoresis, Polyacrylamide Gel , Mice , Molecular Sequence Data , Recombinant Proteins/isolation & purification , Recombinant Proteins/metabolism , Serine Endopeptidases/chemistry , Serine Endopeptidases/metabolism , Substrate Specificity
12.
FASEB J ; 22(6): 1861-73, 2008 Jun.
Article in English | MEDLINE | ID: mdl-18230682

ABSTRACT

The synaptic serine protease neurotrypsin is considered to be essential for the establishment and maintenance of cognitive brain functions, because humans lacking functional neurotrypsin suffer from severe mental retardation. Neurotrypsin cleaves agrin at two homologous sites, liberating a 90-kDa and a C-terminal 22-kDa fragment from the N-terminal moiety of agrin. Morphological analyses indicate that neurotrypsin is contained in presynaptic terminals and externalized in association with synaptic activity, while agrin is localized to the extracellular space at or in the vicinity of the synapse. Here, we present a detailed biochemical analysis of neurotrypsin-mediated agrin cleavage in the murine brain. In brain homogenates, we found that neurotrypsin exclusively cleaves glycanated variants of agrin. Studies with isolated synaptosomes obtained by subcellular fractionation from brains of wild-type and neurotrypsin-overexpressing mice revealed that neurotrypsin-dependent cleavage of agrin was concentrated at synapses, where the most heavily glycanated variants of agrin predominate. Because agrin has been shown to play an important role in the formation and the maintenance of excitatory synapses in the central nervous system, its local cleavage at the synapse implicates the neurotrypsin/agrin system in the regulation of adaptive reorganizations of the synaptic circuitry in the context of cognitive functions, such as learning and memory.


Subject(s)
Agrin/metabolism , Peptide Fragments/metabolism , Serine Endopeptidases/metabolism , Synapses/metabolism , Agrin/chemistry , Animals , Brain Chemistry , Cognition , Mice , Peptide Fragments/chemistry , Polysaccharides/analysis , Serine Endopeptidases/analysis , Synapses/chemistry
13.
FASEB J ; 21(13): 3468-78, 2007 Nov.
Article in English | MEDLINE | ID: mdl-17586728

ABSTRACT

The synaptic serine protease neurotrypsin is thought to be important for adaptive synaptic processes required for cognitive functions, because humans deficient in neurotrypsin suffer from severe mental retardation. In the present study, we describe the biochemical characterization of neurotrypsin and its so far unique substrate agrin. In cell culture experiment as well as in neurotrypsin-deficient mice, we showed that agrin cleavage depends on neurotrypsin and occurs at two conserved sites. Neurotrypsin and agrin were expressed recombinantly, purified, and assayed in vitro. A catalytic efficiency of 1.3 x 10(4) M(-1) x s(-1) was determined. Neurotrypsin activity was shown to depend on calcium with an optimal activity in the pH range of 7-8.5. Mutagenesis analysis of the amino acids flanking the scissile bonds showed that cleavage is highly specific due to the unique substrate recognition pocket of neurotrypsin at the active site. The C-terminal agrin fragment released after cleavage has recently been identified as an inactivating ligand of the Na+/K+-ATPase at CNS synapses, and its binding has been demonstrated to regulate presynaptic excitability. Therefore, dysregulation of agrin processing is a good candidate for a pathogenetic mechanism underlying mental retardation. In turn, these results may also shed light on mechanisms involved in cognitive functions.


Subject(s)
Agrin/metabolism , Intellectual Disability/enzymology , Serine Endopeptidases/metabolism , Synapses/enzymology , Agrin/chemistry , Amino Acid Sequence , Animals , Catalysis , Cell Line , Humans , Hydrogen-Ion Concentration , Hydrolysis , Mice , Mice, Transgenic , Molecular Sequence Data , Mutagenesis , Sequence Homology, Amino Acid , Serine Endopeptidases/genetics , Serine Endopeptidases/isolation & purification
14.
J Biol Chem ; 277(6): 4551-7, 2002 Feb 08.
Article in English | MEDLINE | ID: mdl-11733523

ABSTRACT

The neural cell adhesion molecule axonin-1/TAG-1 mediates cell-cell interactions via homophilic and heterophilic contacts. It consists of six Ig and four fibronectin type III domains anchored to the membrane by glycosylphosphatidylinositol. The recently solved crystal structure indicates a module composed of the four N-terminal Ig domains as the contact site between trans-interacting axonin-1 molecules from apposed membranes. Here, we have tested domain-specific monoclonal antibodies for their capacity to interfere with homophilic binding in a cell aggregation assay. The results confirmed the existence of a binding region within the N-terminal Ig domains and identified a second region contributing to homophilic binding on the third and fourth fibronectin domains near the C terminus. The perturbation of each region alone resulted in a complete loss of cell aggregation, suggesting that axonin-1-mediated cell-cell contact results from a cooperative action of two homophilic binding regions. The data support that axonin-1-mediated cell-cell contact is formed by cis-assisted trans-binding. The N-terminal binding regions of axonin-1 establish a linear zipper-like string of trans-interacting axonin-1 molecules alternately provided by the two apposed membranes. The C-terminal binding regions strengthen the cell-cell contact by enhancing the expansion of the linear string into a two-dimensional array via cis-interactions. Cis-assisted trans-binding may be a basic binding mechanism common to many cell adhesion molecules.


Subject(s)
Cell Adhesion Molecules, Neuronal/physiology , Cell Adhesion/physiology , Animals , Cell Adhesion Molecules, Neuronal/metabolism , Cell Line , Chick Embryo , Contactin 2 , Mice , Mice, Inbred BALB C , Protein Binding
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