November 18, 2003The Journal of PhysiologyOpen Access

Functional characterization and cold sensitivity of T1313A, a new mutation of the skeletal muscle sodium channel causing paramyotonia congenita in humans

View Full Paper

Ask AI

Bookmark

Population

HEK293 cells stably expressing T1313A or wild-type (hSkM1) skeletal muscle Na+ channels

Comparison

T1313A mutation in the SCN4A gene vs Wild-type (hSkM1) channels

Design

Preclinical

Authors

MBMagali BouhoursMount Sinai Hospital DSDamien SternbergChildren's Hospital of Philadelphia CDClaire‐Sophie DavoineCentre National de la Recherche Scientifique

Discussion

Member takes

Implication

Mechanistic data on T1313A gating; leaves open translation to human paramyotonia congenita therapy.

Structured PICO

Population

HEK293 cells stably expressing T1313A or wild-type (hSkM1) skeletal muscle Na+ channels

Intervention

T1313A mutation in the SCN4A gene

Comparator

Wild-type (hSkM1) channels

Outcome

Na+ channel gating defects (fast inactivation, slow inactivation, deactivation, and temperature sensitivity) assessed by whole-cell patch-clamp techniquesurrogate

The novel T1313A mutation in the skeletal muscle Na+ channel impairs fast inactivation and alters gating kinetics, which are further exacerbated by cooling, providing a mechanistic basis for paramyotonia congenita.

Cite This Study

Bouhours et al. (2003) studied this question.

synapsesocial.com/papers/6a70a248ac440176ef294cb4 https://doi.org/10.1113/jphysiol.2003.053082

View Full Paper

Ask AI

Bookmark

Functional characterization and cold sensitivity of T1313A, a new mutation of the skeletal muscle sodium channel causing paramyotonia congenita in humans

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Functional characterization and cold sensitivity of T1313A, a new mutation of the skeletal muscle sodium channel causing paramyotonia congenita in humans

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider