Primary structure of Electrophorus electricus sodium channel deduced from cDNA sequence

Noda, Masaharu; Shimizu, Shin; Tanabe, Tsutomu; Takai, Toshiyuki; Kayano, Toshiaki; Ikeda, Takayuki; Takahashi, Hideo; Nakayama, Hitoshi; Kanaoka, Yuichi; Minamino, Naoto; Kangawa, Kenji; Matsuo, Hisayuki; Raftery, Michael A.; Hirose, Tatsuro; Inayama, Seiichi; Hayashida, Hidenori; Miyata, Takashi; Numa, Shosaku

doi:10.1038/312121a0

Cited by 1,288 publications

(636 citation statements)

References 56 publications

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“…The a-subunit consists of 4 homologous domains (DI-DIV), and each domain contains 6 transmembrane segments designated S1-S6. 6 Mutations that decrease Na C channel function generally lead to periodic paralysis phenotypes, while increased channel activity, or non-inactivatable channels, results in non-dystrophic myotonia phenotypes. Mutations in SCN4A gene have been shown to be responsible for approximately 10% of cases of hypokalemic periodic paralysis.…”

Section: Dicussionmentioning

confidence: 99%

Mutations of SCN4A gene cause different diseases: 2 case reports and literature review

Liu

Huang²,

Luan³

et al. 2015

Channels

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Section: Dicussionmentioning

confidence: 99%

Mutations of SCN4A gene cause different diseases: 2 case reports and literature review

Liu

Huang²,

Luan³

et al. 2015

Channels

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“…Molecular biology has further subclassified Na+ channels, and has identified several members of a mammalian Na+ channel multigene family. Those include several isoforms of TTX-S Na+ channels expressed in neurons and muscle and at least two TTX-R Na+ channels expressed in heart and denervated muscle (Noda et al, 1984;Barchi, 1987;Auld et al, 1988;Rogart et al, 1989;Gibbs et al, 1990;Kallen et al, 1990;see Catterall, 1988, for review). Using site-directed mutagenesis and subsequent expression of rat brain II Na+ channel in Xenopus oocytes (Noda et al, 1989;Yang et al, 1992), it was possible to identify the amino acid residues that constitute the TTX-binding site of this TTX-S Na+ channel.…”

Section: Ttx-sensitivementioning

confidence: 99%

Differential modulation of TTX-sensitive and TTX-resistant Na+ channels in spinal cord astrocytes following activation of protein kinase C

Thio

Sontheimer

1993

J. Neurosci.

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TTX-sensitive (TTX-S) and TTX-resistant (TTX-R) Na+ currents are expressed in high densities (2–8 channels/microns2) in astrocytes cultured from neonatal rat spinal cord. The two Na+ current types differ up to 1000-fold in their TTX sensitivity and additionally have different steady-state activation (g-V) and inactivation (h infinity) curves. Expression of TTX-S and TTX-R Na+ currents is confined to morphologically distinguishable subtypes of astrocytes, allowing characterization of the two types of Na+ currents in isolation: stellate cells express TTX-S Na+ currents and flat pancake cells express TTX-R Na+ currents. Activation of protein kinase C (PKC) by phorbol 12-myristate 13-acetate (PMA) exhibited different effects on TTX-S and TTX-R Na+ currents. PMA reduced peak TTX-S Na+ currents by 25– 60%; in contrast, PMA potentiated peak TTX-R Na+ currents by 60–150%. These effects developed within minutes, and were typically not reversible. PMA effects were voltage dependent, and shifted steady- state Na+ current activation of TTX-R and TTX-S currents by 6 and 18 mV, respectively, but without affecting their steady-state current inactivation (h infinity). PMA treatment also changed Na+ current kinetics. TTX-R current activation (tau m) was faster and current inactivation (tau h) changed from a single- to a bi-exponential after PMA exposure, suggesting that PKC phosphorylation may have activated formerly quiescent Na+ channels. In contrast, TTX-S current activation (tau m) was unchanged, and current inactivation (tau h), on average, decreased by 50% following PMA exposure.(ABSTRACT TRUNCATED AT 250 WORDS)

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“…The major subunits of the sodium channels of the electric eel [1] and rat brain [2], the potassium channels of Drosophila [3] and mouse brain [4], and the calcium channel of rabbit skeletal muscle [5] share significant sequence homology, suggesting that these and other voltagesensitive ion channels arose by divergence from a common ancestral sequence.…”

Section: Cloning Approachmentioning

confidence: 99%

“…L-type calcium channels are members of a family of voltage-sensitive ion channels which share structural similarities and sequence homology [1][2][3][4][5][6]. They are found in a variety of tissues, including skeletal muscle, heart, and brain.…”

Section: Introductionmentioning

confidence: 99%

Polymerase chain reaction cloning of L‐type calcium channel sequences from the heart and the brain

1990

FEBS Letters

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The sequences of the highly conserved $4 regions of voltage-sensitive ion channels were used to design oligonucleotide primers for the polymerase chain reaction. Specific fragments of the cDNA encoding L-type calcium channels from the heart, brain, and skeletal muscle were amplified and cloned. The nucleotide sequences of the cardiac and brain calcium channels obtained are identical over this region, and share 78% homology with the skeletal muscle calcium channel. Comparison of the predicted amino acid sequences of our clones with those of other calcium channels reveals unexpected patterns of conservation which suggest alternative exon use.

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Primary structure of Electrophorus electricus sodium channel deduced from cDNA sequence

Cited by 1,288 publications

References 56 publications

Mutations of SCN4A gene cause different diseases: 2 case reports and literature review

Mutations of SCN4A gene cause different diseases: 2 case reports and literature review

Differential modulation of TTX-sensitive and TTX-resistant Na+ channels in spinal cord astrocytes following activation of protein kinase C

Polymerase chain reaction cloning of L‐type calcium channel sequences from the heart and the brain

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