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- W2079678424 abstract "Ca2+ dependent inactivation (CDI) has been documented for the great majority of voltage dependent Ca2+ channels (Cav) but whether native Cav1.1 of adult skeletal muscle exhibits this feature remains controversial. When explored in heterologous (i.e., HEK cells) or homologous expression (i.e., myotubes), systems that lack or display immature E-C coupling, respectively, several groups have demonstrated both the absence and presence of Cav1.1 CDI. In a recent report using homologous expression system where CDI was documented, Cav1.1 channels displayed the classical features of CDI: 1) dependence on extracellular Ca2+, 2) elimination by replacing Ca2+ with Ba2+ or by using high affinity and fast kinetics Ca2+ buffer BAPTA, and 3) calmodulin modulation. Here we use whole-cell voltage clamp Ca2+ current recordings obtained from adult skeletal muscle fibers to address whether Cav1.1 exhibits CDI in its native environment. Surprisingly, Ca2+ current inactivation was insensitive to Ca2+ substitution by Ba2+, suggesting that 1) CDI is not present or 2) that Ca2+ flowing through the channels is not the Ca2+ source for current inactivation. We tested the hypothesis that Ca2+ release from SR via ortograde Cav1.1-RyR signaling may be the source for CDI. To test this hypothesis we use dantrolene (a membrane permeable RyR Ca2+ release channel antagonist). When 40 μM dantrolene (a concentration that suppress action potential evoked-Ca2+ transient by ∼30%) was added to the external solution Cav1.1 CDI was partially suppressed. These observations suggest the provocative idea that Cav1.1 CDI is regulated by Ca2+ release via adjacent sarcoplasmic reticulum RyR1 channels. Supported by NIH-NIAMS (R01-AR055099)." @default.
- W2079678424 created "2016-06-24" @default.
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- W2079678424 date "2012-01-01" @default.
- W2079678424 modified "2023-10-16" @default.
- W2079678424 title "Calcium Dependent Inactivation of CaV1.1 Channels in Adult Skeletal Muscle: A Possible Role of RyR1 Channels" @default.
- W2079678424 doi "https://doi.org/10.1016/j.bpj.2011.11.697" @default.
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