| http://purl.uniprot.org/citations/32866694 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/32866694 | http://www.w3.org/2000/01/rdf-schema#comment | "In response to excitation of skeletal muscle fibers, trains of action potentials induce changes in the configuration of the dihydropyridine receptor (DHPR) anchored in the tubular membrane which opens the Ca2+ release channel in the sarcoplasmic reticulum membrane. The DHPR also functions as a voltage-gated Ca2+ channel that conducts L-type Ca2+ currents routinely recorded in mammalian muscle fibers, which role was debated for more than four decades. Recently, to allow a closer look into the role of DHPR Ca2+ influx in mammalian muscle, a knock-in (ki) mouse model (ncDHPR) carrying mutation N617D (adjacent to domain II selectivity filter E) in the DHPRα1S subunit abolishing Ca2+ permeation through the channel was generated [Dayal et al., 2017]. In the present study, the Mn2+ quenching technique was initially intended to be used on voltage-clamped muscle fibers from this mouse to determine whether Ca2+ influx through a pathway distinct from DHPR may occur to compensate for the absence of DHPR Ca2+ influx. Surprisingly, while N617D DHPR muscle fibers of the ki mouse do not conduct Ca2+, Mn2+ entry and subsequent quenching did occur because Mn2+ was able to permeate and produce L-type currents through N617D DHPR. N617D DHPR was also found to conduct Ba2+ and Ba2+ currents were strongly blocked by external Ca2+. Ba2+ permeation was smaller, current kinetics slower and Ca2+ block more potent than in wild-type DHPR. These results indicate that residue N617 when replaced by the negatively charged residue D is suitably located at entrance of the pore to trap external Ca2+ impeding in this way permeation. Because Ba2+ binds with lower affinity to D, Ba2+ currents occur, but with reduced amplitudes as compared to Ba2+ currents through wild-type channels. We conclude that mutations located outside the selectivity filter influence channel permeation and possibly channel gating in a fully differentiated skeletal muscle environment."xsd:string |
| http://purl.uniprot.org/citations/32866694 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.ceca.2020.102256"xsd:string |
| http://purl.uniprot.org/citations/32866694 | http://purl.uniprot.org/core/author | "Charnet P."xsd:string |
| http://purl.uniprot.org/citations/32866694 | http://purl.uniprot.org/core/author | "Dayal A."xsd:string |
| http://purl.uniprot.org/citations/32866694 | http://purl.uniprot.org/core/author | "Grabner M."xsd:string |
| http://purl.uniprot.org/citations/32866694 | http://purl.uniprot.org/core/author | "Allard B."xsd:string |
| http://purl.uniprot.org/citations/32866694 | http://purl.uniprot.org/core/author | "Jacquemond V."xsd:string |
| http://purl.uniprot.org/citations/32866694 | http://purl.uniprot.org/core/author | "Fuster C."xsd:string |
| http://purl.uniprot.org/citations/32866694 | http://purl.uniprot.org/core/author | "Idoux R."xsd:string |
| http://purl.uniprot.org/citations/32866694 | http://purl.uniprot.org/core/date | "2020"xsd:gYear |
| http://purl.uniprot.org/citations/32866694 | http://purl.uniprot.org/core/name | "Cell Calcium"xsd:string |
| http://purl.uniprot.org/citations/32866694 | http://purl.uniprot.org/core/pages | "102256"xsd:string |
| http://purl.uniprot.org/citations/32866694 | http://purl.uniprot.org/core/title | "Divalent cations permeation in a Ca2+ non-conducting skeletal muscle dihydropyridine receptor mouse model."xsd:string |
| http://purl.uniprot.org/citations/32866694 | http://purl.uniprot.org/core/volume | "91"xsd:string |
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