Mechanisms of Excitation-Contraction Coupling Relevant to Skeletal Muscle Fatigue

1995 ◽  
pp. 45-56 ◽  
Author(s):  
D. G. Stephenson ◽  
G. D. Lamb ◽  
G. M. M. Stephenson ◽  
M. W. Fryer
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fatigue ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
Skeletal Muscle Fatigue

Effect of lactate on depolarization-induced Ca2+ release in mechanically skinned skeletal muscle fibers

2000 ◽  
Vol 278 (3) ◽  
pp. C517-C525 ◽  
Author(s):  
T. L. Dutka ◽  
G. D. Lamb
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fatigue ◽  
Muscle Fibers ◽  
Inhibitory Effect ◽  
Detectable Effect ◽  
Contractile Apparatus ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
Skeletal Muscle Fibers ◽  
Intense Activity

It is unclear whether accumulation of lactate in skeletal muscle fibers during intense activity contributes to muscle fatigue. Using mechanically skinned fibers from rat and toad muscle, we were able to examine the effect of l(+)-lactate on excitation-contraction coupling independently of other metabolic changes. We investigated the effects of lactate on the contractile apparatus, caffeine-induced Ca2+ release from the sarcoplasmic reticulum, and depolarization-induced Ca2+release. Lactate (15 or 30 mM) had only a small inhibitory effect directly on the contractile apparatus and caused appreciable (20–35%) inhibition of caffeine-induced Ca2+ release, seemingly by a direct effect on the Ca2+ release channels. However, 15 mM lactate had no detectable effect on Ca2+release when it was triggered by the normal voltage sensor mechanism, and 30 mM lactate reduced such release by only <10%. These results indicate that lactate has only a relatively small inhibitory effect on normal excitation-contraction coupling, indicating that lactate accumulation per se is not a major factor in muscle fatigue.

Skeletal muscle fatigue does not affect shooting accuracy of handball players

2019 ◽  
Vol 27 (4) ◽  
pp. 253-259
Author(s):  
Beyza Akyüz ◽  
Pınar Arpınar Avşar ◽  
Murat Bilge ◽  
Gökhan Deliceoğlu ◽  
Feza Korkusuz
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fatigue ◽  
Skeletal Muscle Fatigue

scholarly journals Triadin Binding to the C-Terminal Luminal Loop of the Ryanodine Receptor is Important for Skeletal Muscle Excitation–Contraction Coupling

2007 ◽  
Vol 130 (4) ◽  
pp. 365-378 ◽  
Author(s):  
Sanjeewa A. Goonasekera ◽  
Nicole A. Beard ◽  
Linda Groom ◽  
Takashi Kimura ◽  
Alla D. Lyfenko ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Ryanodine Receptor ◽  
Calcium Release ◽  
Striated Muscle ◽  
Single Channel ◽  
Triple Mutant ◽  
Double Mutation ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
Functional Studies

Ca2+ release from intracellular stores is controlled by complex interactions between multiple proteins. Triadin is a transmembrane glycoprotein of the junctional sarcoplasmic reticulum of striated muscle that interacts with both calsequestrin and the type 1 ryanodine receptor (RyR1) to communicate changes in luminal Ca2+ to the release machinery. However, the potential impact of the triadin association with RyR1 in skeletal muscle excitation–contraction coupling remains elusive. Here we show that triadin binding to RyR1 is critically important for rapid Ca2+ release during excitation–contraction coupling. To assess the functional impact of the triadin-RyR1 interaction, we expressed RyR1 mutants in which one or more of three negatively charged residues (D4878, D4907, and E4908) in the terminal RyR1 intraluminal loop were mutated to alanines in RyR1-null (dyspedic) myotubes. Coimmunoprecipitation revealed that triadin, but not junctin, binding to RyR1 was abolished in the triple (D4878A/D4907A/E4908A) mutant and one of the double (D4907A/E4908A) mutants, partially reduced in the D4878A/D4907A double mutant, but not affected by either individual (D4878A, D4907A, E4908A) mutations or the D4878A/E4908A double mutation. Functional studies revealed that the rate of voltage- and ligand-gated SR Ca2+ release were reduced in proportion to the degree of interruption in triadin binding. Ryanodine binding, single channel recording, and calcium release experiments conducted on WT and triple mutant channels in the absence of triadin demonstrated that the luminal loop mutations do not directly alter RyR1 function. These findings demonstrate that junctin and triadin bind to different sites on RyR1 and that triadin plays an important role in ensuring rapid Ca2+ release during excitation–contraction coupling in skeletal muscle.

Monoclonal Antibodies as Probes of Triad Structure and Excitation-Contraction Coupling in Skeletal Muscle

1990 ◽  
pp. 371-382 ◽  
Author(s):  
Mario S. Rosemblatt ◽  
Gonzalo Pérez ◽  
Bojena Antoniu ◽  
Evelyn Reilley ◽  
Noriaki Ikemoto
Keyword(s):  
Skeletal Muscle ◽  
Monoclonal Antibodies ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling
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