AI Article Synopsis
- The study investigates how aging affects the regulation of the ryanodine receptor (RyR1) in skeletal muscles, which is important for muscle strength and contraction.
- Researchers compared the binding of ryanodine to muscle membranes from younger (8 months) and older (26 months) rats, focusing on the roles of calcium (Ca) and calmodulin (CaM).
- Findings indicate that aging reduces the effectiveness of Ca in stimulating RyR1 in fast-twitch muscles, which may be a factor in decreased muscle function with age, especially in fast-twitch fibers.
Article Abstract
Introduction: Because impaired excitation-contraction coupling and reduced sarcoplasmic reticulum (SR) Ca release may contribute to the age-associated decline in skeletal muscle strength, we investigated the effect of aging on regulation of the skeletal muscle isoform of the ryanodine receptor (RyR1) by physiological channel ligands.
Methods: [ H]Ryanodine binding to membranes from 8- and 26-month-old Fischer 344 extensor digitorum longus (EDL) and soleus muscles was used to investigate the effects of age on RyR1 modulation by Ca and calmodulin (CaM).
Results: Aging reduced maximal Ca -stimulated binding to EDL membranes. In 0.3 μM Ca , age reduced binding and CaM increased binding to EDL membranes. In 300 μM Ca , CaM reduced binding, but the age effect was not significant. Aging did not affect Ca or CaM regulation of soleus RyR1.
Discussion: In aged fast-twitch muscle, impaired RyR1 Ca regulation may contribute to lower SR Ca release and reduced muscle function. Muscle Nerve 57: 1022-1025, 2018.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5951731 | PMC |
| http://dx.doi.org/10.1002/mus.26063 | DOI Listing |
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