Impairment of slow inactivation as a common mechanism for periodic paralysis in DIIS4-S5

@article{Bendahhou2002ImpairmentOS,
  title={Impairment of slow inactivation as a common mechanism for periodic paralysis in DIIS4-S5},
  author={Saı̈d Bendahhou and Theodore R. Cummins and Roger W. Kula and Y.-H. Fu and Louis J. Pt{\'a}{\vc}ek},
  journal={Neurology},
  year={2002},
  volume={58},
  pages={1266-1272}
}
Background Mutations in the human skeletal muscle sodium channels are associated with hyperKPP, hypoKPP, paramyotonia congenita, and potassium-aggravated myotonia. This article describes the clinical manifestations of a patient with hyperKPP carrying a mutation (L689I) occurring in the linker DIIS4-S5 and its functional expression in a mammalian system. Objective To correlate the clinical manifestations of hyperkalemic periodic paralysis (hyperKPP) with the functional expression of a sodium… Expand
View on Wolters Kluwer
ncbi.nlm.nih.gov
72 Citations
Highly Influential Citations
8
Background Citations
26
Results Citations
3

72 Citations

Citation Type

Citation Type

Altered fast and slow inactivation of the N440K Nav1.4 mutant in a periodic paralysis syndrome
TLDR
N440K causes a gain of function consistent with skeletal muscle hyperexcitability as observed in individuals with the mutation, and produces a significant depolarizing shift in the voltage dependence of fast in activation and increased persistent current and acceleration in fast inactivation recovery. Expand
New mutation of the Na channel in the severe form of potassium‐aggravated myotonia
TLDR
A new mutation of PAM with a severe phenotype was identified in a Japanese family presenting with the PAM phenotype and the importance of the C‐terminus for fast inactivation of the sodium channel is emphasized. Expand
Cold-induced defects of sodium channel gating in atypical periodic paralysis plus myotonia
TLDR
Consistent with other NaV1.4 mutations associated with a paralytic phenotype, the P1158S mutation disrupts slow inactivation and the unique temperature sensitivity of the channel defect may contribute to the unusual clinical phenotype. Expand
Mechanisms of cold sensitivity of paramyotonia congenita mutation R1448H and overlap syndrome mutation M1360V
Missense mutations of the human skeletal muscle voltage‐gated Na+ channel (hSkM1) cause a variety of neuromuscular disorders. The mutation R1448H results in paramyotonia congenita and causes… Expand
A sodium channel myotonia due to a novel SCN4A mutation accompanied by acquired autoimmune myasthenia gravis
TLDR
A functional study of the mutant channel revealed marked enhancement of activation and slight impairment of fast inactivation, which should induce muscle hyperexcitability, thus suggesting an opposing effect to myasthenia. Expand
A1152D mutation of the Na+ channel causes paramyotonia congenita and emphasizes the role of DIII/S4–S5 linker in fast inactivation
TLDR
A new PC‐associated mutation is identified, which substitutes aspartic acid for a conserved alanine in the S4–S5 linker of domain III of the human skeletal muscle Na+ channel (A1152D). Expand
Skeletal muscle channelopathies: nondystrophic myotonias and periodic paralysis.
TLDR
Recent discoveries in the skeletal muscle channelopathies have increased understanding of the genetics and pathophysiology of these diseases, and studies reporting imaging techniques raise the possibility of improved disease monitoring and better outcome measures for clinical trials. Expand
A novel mutation in SCN4A causes severe myotonia and school-age-onset paralytic episodes
TLDR
Functional analysis of the mutant channel expressed in cultured cell revealed enhancement of the activation and disruption of the slow inactivation, which were consistent with myotonia and paralytic attack. Expand
Effects of S906T polymorphism on the severity of a novel borderline mutation I692M in Nav1.4 cause periodic paralysis
TLDR
The results suggest that polymorphism S906T has effects on the clinical phenotypic and electrophysiological severity of a novel borderline Nav1.4 mutation I692M, making the borderline mutation fully penetrant. Expand
New mutations of SCN4A cause a potassium-sensitive normokalemic periodic paralysis
TLDR
A potassium-sensitive and normokalemic type of periodic paralysis caused by new SCN4A mutations at codon 675 is reported. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 32 REFERENCES
Enhanced slow inactivation by V445M: a sodium channel mutation associated with myotonia.
TLDR
The V445M mutation in transmembrane segment IS6 is recently found in a family with myotonia but no weakness and is shown to be crucial for slow inactivation, whereas previous studies have shown that disrupted slow in activation predisposes to episodic paralysis. Expand
Activation and Inactivation of the Voltage-Gated Sodium Channel: Role of Segment S5 Revealed by a Novel Hyperkalaemic Periodic Paralysis Mutation
TLDR
Results, showing that the I1495F and T704M hyperkalaemic periodic paralysis mutations both have profound effects on channel activation and fast–slow inactivation, suggest that the S5 segment maybe in a location where fast and slow inactivation converge. Expand
A double mutation in families with periodic paralysis defines new aspects of sodium channel slow inactivation.
TLDR
One allele with two novel mutations occurring simultaneously in the SCN4A gene, encoding the human skeletal muscle voltage-gated Na(+) channel, is identified, demonstrating that manifestation of HyperKPP does not necessarily require disruption of slow inactivation. Expand
Hyperkalemic periodic paralysis M1592V mutation modifies activation in human skeletal muscle Na+ channel.
TLDR
The functional properties of the M1592V mutant resemble those of the previously characterized HPP T704M mutant, both clinically similar phenotypes arise from mutations located at a distance from the putative voltage sensor of the channel. Expand
Functional consequences of a Na+ channel mutation causing hyperkalemic periodic paralysis
TLDR
Patch-clamp recordings show that the human mutation introduced into the corresponding region of the rat muscle Na+ channel cDNA shifts the voltage dependence of activation by 10-15 mV in the negative direction, which results in a persistent Na+ current that activates near -70 mV; this phenomenon could underlie the abnormal muscle activity observed in patients with HYPP. Expand
Sodium channel mutations in paramyotonia congenita exhibit similar biophysical phenotypes in vitro.
  • N. Yang, S. Ji, +4 authors A. George
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1994
TLDR
Findings help to explain the phenotypic differences between HYPP and PC at the molecular and biophysical level and contribute to the understanding of Na+ channel structure and function. Expand
Impaired slow inactivation in mutant sodium channels.
Hyperkalemic periodic paralysis (HyperPP) is a disorder in which current through Na+ channels causes a prolonged depolarization of skeletal muscle fibers, resulting in membrane inexcitability and… Expand
Defective slow inactivation of sodium channels contributes to familial periodic paralysis
TLDR
SI is defective in a subset of mutant Na channels associated with episodic weakness (HyperPP or PMC) but remains intact for mutants studied so far that cause myotonia without weakness (PAM). Expand
Sodium channel mutations in acetazolamide‐responsive myotonia congenita, paramyotonia congenita, and hyperkalemic periodic paralysis
TLDR
This report summarizes the sodium channel mutation analysis in 25 families with hyperKPP and reports the putative disease-causing mutation in acetazolamide-responsiveMyotonia congenita, a related disease in which myotonia is worsened by potassium but in which episodic weakness does not occur. Expand
Defective fast inactivation recovery and deactivation account for sodium channel myotonia in the I1160V mutant.
TLDR
The skeletal muscle sodium channel mutant I1160V cosegregates with a disease phenotype producing myotonic discharges that are worsened by elevated K+ levels but unaffected by cooling. Expand
...
1
2
3
4
...