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• W2155079019 abstract "Although an elevation in myoplasmic Ca2+ can activate the skeletal muscle ryanodine receptor (RyR1), the function of this Ca2+ activation is unclear because extracellular Ca2+ influx is unnecessary for skeletal-type EC coupling. To determine whether Ca2+ activation of RyR1 is necessary for the initiation of skeletal-type EC coupling, we examined the behavior of RyR1 with glutamate 4032 mutated to alanine (E4032A-RyR1) because this mutation had been shown to dramatically reduce activation by Ca2+. Proc. Natl. Acad. Sci. USA. 98:2865–2870). Analysis after reconstitution into planar lipid bilayers revealed that E4032A-RyR1 was negligibly activated by 100 μM Ca2+ (Po too low to be measured). Even in the presence of both 2 mM caffeine and 2 mM ATP, Po remained low for E4032A-RyR1 (ranging from <0.0001 in 100 μM free Ca2+ to 0.005 in 2 mM free Ca2+). Thus, the E4032A mutation caused a nearly complete suppression of activation of RyR1 by Ca2+. Depolarization of E4032A-RyR1-expressing myotubes elicited L-type Ca2+ currents of approximately normal size and myoplasmic Ca2+ transients that were skeletal-type, but about fivefold smaller than those for wild-type RyR1. The reduced amplitude of the Ca2+ transient is consistent either with the possibility that Ca2+ activation amplifies Ca2+ release during EC coupling, or that the E4032A mutation generally inhibits activation of RyR1. In either case, Ca2+ activation of RyR1 does not appear to be necessary for the initiation of Ca2+ release during EC coupling in skeletal muscle." @default.
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• W2155079019 date "2002-05-01" @default.
• W2155079019 modified "2023-10-18" @default.
• W2155079019 title "Ca2+ Activation of RyR1 Is Not Necessary for the Initiation of Skeletal-Type Excitation-Contraction Coupling" @default.
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• W2155079019 doi "https://doi.org/10.1016/s0006-3495(02)75586-0" @default.
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