AustralieFrV1, PascalFrancis, Checkpoint, bibRecord, 002A40

Involvement of calpains in Ca2+-induced disruption of excitation-contraction coupling in mammalian skeletal muscle fibers

Identifieur interne : 002A40 ( PascalFrancis/Checkpoint ); précédent : 002A39; suivant : 002A41

Involvement of calpains in Ca2+-induced disruption of excitation-contraction coupling in mammalian skeletal muscle fibers

Auteurs : Esther Verburg [Australie, Norvège] ; Robyn M. Murphy [Australie] ; Isabelle Richard [France] ; Graham D. Lamb [Australie]

Source :

American journal of physiology. Cell physiology [ 0363-6143 ] ; 2009.

RBID : Pascal:09-0226655

Descripteurs français

Pascal (Inist)
- Calcium, Disruption, Couplage excitation contraction, Muscle strié, Fibre musculaire, Fatigue, Souris.
Wicri :
- topic : Calcium.

English descriptors

KwdEn :
- Calcium, Disruption, Excitation contraction coupling, Fatigue, Mouse, Muscular fiber, Striated muscle.

Abstract

In skeletal muscle fibers, the coupling between excitation of the surface membrane and the release of Ca²⁺ from the sarcoplasmic reticulum is irreversibly disrupted if cytoplasmic Ca²⁺ concentration ([Ca²⁺]) is raised to micromolar levels for a prolonged period. This excitation-contraction (EC) uncoupling may contribute to muscle weakness after some types of exercise and in certain muscle diseases and has been linked to structural alteration of the triad junctions, but its molecular basis is unclear. Both μ-calpain, a ubiquitous Ca²⁺-activated protease, and muscle-specific calpain-3 become autolytically activated at micromolar Ca²⁺ and have been suggested to be responsible for the uncoupling. This study used controlled Ca²⁺ exposure in mechanically skinned fibers from extensor digitorum longus muscle to show that EC uncoupling still occurs in muscle fibers of calpain-3-deficient mice, with a Ca²⁺ dependence indistinguishable from that in normal mice and rats. Western blotting of muscle fibers that had been partially EC uncoupled by exposure to an intermediate Ca²⁺ level (∼5 μM Ca²⁺ for 3 min, no ATP) showed the presence of autolytic activation of a proportion of the μ-calpain present, but with little or no activation of calpain-3. Homogenates of normal and calpain-3-deficient muscles exposed to micromolar Ca²⁺ displayed similar levels of diffusible proteolytic activity, as gauged by the rate of decline of passive force in stretched, skinned muscle fibers. Exogenously added μ-calpain, preactivated by elevated [Ca²⁺] and applied in the presence of 1 μM Ca²⁺, disrupted EC coupling in a manner similar to raised [Ca²⁺]. We conclude that calpain-3 is not responsible for Ca²⁺-induced disruption of EC coupling, but that μ-calpain is a plausible candidate.

Affiliations:

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Le document en format XML

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<front><div type="abstract" xml:lang="en">In skeletal muscle fibers, the coupling between excitation of the surface membrane and the release of Ca<sup>2+</sup>
 from the sarcoplasmic reticulum is irreversibly disrupted if cytoplasmic Ca<sup>2+</sup>
 concentration ([Ca<sup>2+</sup>
]) is raised to micromolar levels for a prolonged period. This excitation-contraction (EC) uncoupling may contribute to muscle weakness after some types of exercise and in certain muscle diseases and has been linked to structural alteration of the triad junctions, but its molecular basis is unclear. Both μ-calpain, a ubiquitous Ca<sup>2+</sup>
-activated protease, and muscle-specific calpain-3 become autolytically activated at micromolar Ca<sup>2+</sup>
 and have been suggested to be responsible for the uncoupling. This study used controlled Ca<sup>2+</sup>
 exposure in mechanically skinned fibers from extensor digitorum longus muscle to show that EC uncoupling still occurs in muscle fibers of calpain-3-deficient mice, with a Ca<sup>2+</sup>
 dependence indistinguishable from that in normal mice and rats. Western blotting of muscle fibers that had been partially EC uncoupled by exposure to an intermediate Ca<sup>2+</sup>
 level (∼5 μM Ca<sup>2+</sup>
 for 3 min, no ATP) showed the presence of autolytic activation of a proportion of the μ-calpain present, but with little or no activation of calpain-3. Homogenates of normal and calpain-3-deficient muscles exposed to micromolar Ca<sup>2+</sup>
 displayed similar levels of diffusible proteolytic activity, as gauged by the rate of decline of passive force in stretched, skinned muscle fibers. Exogenously added μ-calpain, preactivated by elevated [Ca<sup>2+</sup>
] and applied in the presence of 1 μM Ca<sup>2+</sup>
, disrupted EC coupling in a manner similar to raised [Ca<sup>2+</sup>
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Involvement of calpains in Ca2+-induced disruption of excitation-contraction coupling in mammalian skeletal muscle fibers

Involvement of calpains in Ca2+-induced disruption of excitation-contraction coupling in mammalian skeletal muscle fibers

Source :

Descripteurs français

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Abstract

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