Key result
Mutations in RyR1 that disrupt FKBP12 binding reduced maximal voltage-gated Ca2+ release by approximately 50% compared with wild-type RyR1 (deltaF/Fmax = 1.6 +/- 0.2 vs 3.1 +/- 0.4).
Population
Skeletal myotubes derived from RyR1-knockout (dyspedic) mice
Comparison
Expression of RyR1 mutations that disrupt FKBP12… vs Expression of wild-type RyR1
Design
Preclinical
Authors
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Supports FKBP12 enhancing skeletal muscle EC coupling gain; leaves open human disease relevance or therapeutic potential.
Absolute Event Rate: 1.6% vs 3.1%
FKBP12 binding to RyR1 enhances the gain of skeletal muscle excitation-contraction coupling.
Ávila et al. (2003) studied this question. Mutations in RyR1 disrupting FKBP12 binding (V2461G and V2461I) vs. Wild-type RyR1 was evaluated on Maximal voltage-gated Ca2+ release. Mutations in RyR1 that disrupt FKBP12 binding reduced maximal voltage-gated Ca2+ release by approximately 50% compared with wild-type RyR1 (deltaF/Fmax = 1.6 +/- 0.2 vs 3.1 +/- 0.4).
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