Specific distribution of sodium channels in axons of rat embryo spinal motoneurones

Alessandri‐Haber, Nicole; Paillart, Christophe; Arsac, Christine; Gola, Maurice; Couraud, François; Crest, Marcel

doi:10.1111/j.1469-7793.1999.0203r.x

Cited by 41 publications

(43 citation statements)

References 41 publications

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“…Cultured spinal motoneurons are derived from an early embryonic stage (14 days in utero), are able to differentiate well characterized axonal and somato-dendritic domains in vitro, and as such, represent an adequate model for the study of sodium channel insertion and anchoring in polarized membrane domains and particularly at the axon initial segment. As soon as 18 h after plating, labeling of the cells with an iodinated ␣-scorpion toxin, a ligand of brain sodium channels, decorates only the axon with a much increased density at the axon initial segment (31). This pattern of labeling does not change qualitatively during subsequent days in culture and is identical to that observed by immunofluorescence with the pan-anti-␣ antibody at 6 days in vitro.…”

Section: Discussionsupporting

confidence: 51%

“…30 and plated on polyornithine/laminin-coated glass coverslips. Culture conditions have been previously reported (31). Immunocytochemistry on paraformaldehyde-fixed motoneurons were performed as in Ref.…”

Section: Methodsmentioning

confidence: 99%

“…7D). Labeling of these cells with an 125 I-labeled ␣ scorpion toxin, which binds to the extracellular part of the ␣ subunit, and subsequent autoradiography showed that the ␣ subunit was nevertheless expressed at the cell sur- face all along the axon, with a much increased density at the initial segment (31). When the cells were probed by immunocytochemistry using an anti-␣ antibody that recognizes all of the ␣ isoforms and the anti-ankyrin antibody, a similar pattern was observed: a high density of sodium channel and ankyrin molecules segregated at the axon initial segment (Fig.…”

Section: Tentative Mapping Of the Binding Sites For The ␣ Subunit Loomentioning

confidence: 99%

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Interaction of the Nav1.2a Subunit of the Voltage-dependent Sodium Channel with Nodal AnkyrinG

Bouzidi

Tricaud

Giraud

et al. 2002

Journal of Biological Chemistry

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Voltage-dependant sodium channels at the axon initial segment and nodes of Ranvier colocalize with the nodal isoforms of ankyrin G (Ank G node). Using fusion proteins derived from the intracellular regions of the Nav1.2a subunit and the Ank repeat domain of Ank G node, we mapped a major interaction site in the intracellular loop separating ␣ subunit domains I-II. This 57-amino acid region binds the Ank repeat region with a K D value of 69 nM. We identified another site in intracellular loop III-IV, and we mapped both Nav1.2a binding sites on the ankyrin repeat domain to the region encompassing repeats 12-22. The ankyrin repeat domain did not bind the ␤ 1 and ␤ 2 subunit cytoplasmic regions. We showed that in cultured embryonic motoneurons, expression of the ␤ 2 subunit is not necessary for the colocalization of Ank G node with functional sodium channels at the axon initial segment. Antibodies directed against the ␤ 1 subunit intracellular region, ␣ subunit loop III-IV, and Ank G node could not co-immunoprecipitate Ank G node and sodium channels from Triton X-100 solubilisates of rat brain synaptosomes. Co-immunoprecipitation of sodium channel ␣ subunit and of the 270-and 480-kDa AnkG node isoforms was obtained when solubilization conditions that maximize membrane protein extraction were used. However, we could not find conditions that allowed for co-immunoprecipitation of ankyrin with the sodium channel ␤ 1 subunit.

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Section: Discussionsupporting

confidence: 51%

Section: Methodsmentioning

confidence: 99%

Section: Tentative Mapping Of the Binding Sites For The ␣ Subunit Loomentioning

confidence: 99%

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Interaction of the Nav1.2a Subunit of the Voltage-dependent Sodium Channel with Nodal AnkyrinG

Bouzidi

Tricaud

Giraud

et al. 2002

Journal of Biological Chemistry

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“…This indicates that neurons, within synaptically interacting networks formed on SWNT substrates, engage in population firing. This is further strengthened by the appearance of fast Na ϩ current, taken to constitute an early sign of axonal differentiation (Alessandri-Haber et al, 1999).…”

Section: Discussionmentioning

confidence: 99%

Interfacing Neurons with Carbon Nanotubes: Electrical Signal Transfer and Synaptic Stimulation in Cultured Brain Circuits

Mazzatenta¹,

Giugliano²,

Campidelli³

et al. 2007

Journal of Neuroscience

322

257

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The unique properties of single-wall carbon nanotubes (SWNTs) and the application of nanotechnology to the nervous system may have a tremendous impact in the future developments of microsystems for neural prosthetics as well as immediate benefits for basic research. Despite increasing interest in neuroscience nanotechnologies, little is known about the electrical interactions between nanomaterials and neurons. We developed an integrated SWNT-neuron system to test whether electrical stimulation delivered via SWNT can induce neuronal signaling. To that aim, hippocampal cells were grown on pure SWNT substrates and patch clamped. We compared neuronal responses to voltage steps delivered either via conductive SWNT substrates or via the patch pipette. Our experimental results, supported by mathematical models to describe the electrical interactions occurring in SWNT-neuron hybrid systems, clearly indicate that SWNTs can directly stimulate brain circuit activity.

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“…AnkG also acts as a critical organizer of AISs (Zhou et al, 1998;Jenkins and Bennett, 2001;Pan et al, 2006;Hedstrom et al, 2007;Yang et al, 2007). However, unlike NRs, AISs are intrinsically specified, forming independently of glial signals (Catterall, 1981;Alessandri-Haber et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Schwannomin-Interacting Protein-1 Isoform IQCJ-SCHIP-1 Is a Late Component of Nodes of Ranvier and Axon Initial Segments

Martin¹,

Carnaud²,

Caño³

et al. 2008

Journal of Neuroscience

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Axon initial segments (AISs) and nodes of Ranvier (NRs) are essential regions for saltatory conduction of the action potential along the axon. These two domains are enriched in similar multimolecular complexes, which include voltage-gated sodium channels (Na v ), NF186 (neurofascin 186), NrCAM (neuron glia-related cell adhesion molecule), and cytoskeleton linkers ankyrin G (AnkG) and ␤IV-spectrin. Identification of novel members of these complexes is critical to better understand their formation, function, and maintenance. Here we report that IQCJ-SCHIP-1, a recently identified isoform of schwannomin-interacting protein-1 (SCHIP-1), is a novel component of both AISs and NRs in the central and peripheral nervous systems. We show that IQCJ-SCHIP-1 binds calmodulin in the absence of Ca 2ϩ and is highly enriched at AISs and NRs. IQCJ-SCHIP-1 accumulation at AISs and NRs is a late event, suggesting that IQCJ-SCHIP-1 is likely to play a role in mature AISs and NRs rather than during their formation. IQCJ-SCHIP-1 was not detected at

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Specific distribution of sodium channels in axons of rat embryo spinal motoneurones

Cited by 41 publications

References 41 publications

Interaction of the Nav1.2a Subunit of the Voltage-dependent Sodium Channel with Nodal AnkyrinG

Interaction of the Nav1.2a Subunit of the Voltage-dependent Sodium Channel with Nodal AnkyrinG

Interfacing Neurons with Carbon Nanotubes: Electrical Signal Transfer and Synaptic Stimulation in Cultured Brain Circuits

Schwannomin-Interacting Protein-1 Isoform IQCJ-SCHIP-1 Is a Late Component of Nodes of Ranvier and Axon Initial Segments

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