pubmed-article:21289290 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:21289290 | lifeskim:mentions | umls-concept:C0242692 | lld:lifeskim |
pubmed-article:21289290 | lifeskim:mentions | umls-concept:C0036226 | lld:lifeskim |
pubmed-article:21289290 | lifeskim:mentions | umls-concept:C0006772 | lld:lifeskim |
pubmed-article:21289290 | lifeskim:mentions | umls-concept:C0054493 | lld:lifeskim |
pubmed-article:21289290 | lifeskim:mentions | umls-concept:C0221099 | lld:lifeskim |
pubmed-article:21289290 | lifeskim:mentions | umls-concept:C1419781 | lld:lifeskim |
pubmed-article:21289290 | lifeskim:mentions | umls-concept:C0030685 | lld:lifeskim |
pubmed-article:21289290 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
pubmed-article:21289290 | lifeskim:mentions | umls-concept:C1709059 | lld:lifeskim |
pubmed-article:21289290 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:21289290 | lifeskim:mentions | umls-concept:C0680255 | lld:lifeskim |
pubmed-article:21289290 | lifeskim:mentions | umls-concept:C0391871 | lld:lifeskim |
pubmed-article:21289290 | lifeskim:mentions | umls-concept:C1283071 | lld:lifeskim |
pubmed-article:21289290 | lifeskim:mentions | umls-concept:C1963578 | lld:lifeskim |
pubmed-article:21289290 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:21289290 | pubmed:dateCreated | 2011-4-27 | lld:pubmed |
pubmed-article:21289290 | pubmed:abstractText | In vitro, calmodulin (CaM) and S100A1 activate the skeletal muscle ryanodine receptor ion channel (RyR1) at submicromolar Ca(2+) concentrations, whereas at micromolar Ca(2+) concentrations, CaM inhibits RyR1. One amino acid substitution (RyR1-L3625D) has previously been demonstrated to impair CaM binding and regulation of RyR1. Here we show that the RyR1-L3625D substitution also abolishes S100A1 binding. To determine the physiological relevance of these findings, mutant mice were generated with the RyR1-L3625D substitution in exon 74, which encodes the CaM and S100A1 binding domain of RyR1. Homozygous mutant mice (Ryr1(D/D)) were viable and appeared normal. However, single RyR1 channel recordings from Ryr1(D/D) mice exhibited impaired activation by CaM and S100A1 and impaired CaCaM inhibition. Isolated flexor digitorum brevis muscle fibers from Ryr1(D/D) mice had depressed Ca(2+) transients when stimulated by a single action potential. However, during repetitive stimulation, the mutant fibers demonstrated greater relative summation of the Ca(2+) transients. Consistently, in vivo stimulation of tibialis anterior muscles in Ryr1(D/D) mice demonstrated reduced twitch force in response to a single action potential, but greater summation of force during high-frequency stimulation. During repetitive stimulation, Ryr1(D/D) fibers exhibited slowed inactivation of sarcoplasmic reticulum Ca(2+) release flux, consistent with increased summation of the Ca(2+) transient and contractile force. Peak Ca(2+) release flux was suppressed at all voltages in voltage-clamped Ryr1(D/D) fibers. The results suggest that the RyR1-L3625D mutation removes both an early activating effect of S100A1 and CaM and delayed suppressing effect of CaCaM on RyR1 Ca(2+) release, providing new insights into CaM and S100A1 regulation of skeletal muscle excitation-contraction coupling. | lld:pubmed |
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pubmed-article:21289290 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:21289290 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21289290 | pubmed:language | eng | lld:pubmed |
pubmed-article:21289290 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21289290 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:21289290 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:21289290 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:21289290 | pubmed:month | May | lld:pubmed |
pubmed-article:21289290 | pubmed:issn | 1522-1563 | lld:pubmed |
pubmed-article:21289290 | pubmed:author | pubmed-author:LinN GNG | lld:pubmed |
pubmed-article:21289290 | pubmed:author | pubmed-author:SchneiderMart... | lld:pubmed |
pubmed-article:21289290 | pubmed:author | pubmed-author:WeberDavidD | lld:pubmed |
pubmed-article:21289290 | pubmed:author | pubmed-author:EuJerry PJP | lld:pubmed |
pubmed-article:21289290 | pubmed:author | pubmed-author:MeissnerGerha... | lld:pubmed |
pubmed-article:21289290 | pubmed:author | pubmed-author:YamaguchiNaoh... | lld:pubmed |
pubmed-article:21289290 | pubmed:author | pubmed-author:MelzerWernerW | lld:pubmed |
pubmed-article:21289290 | pubmed:author | pubmed-author:PasekDaniel... | lld:pubmed |
pubmed-article:21289290 | pubmed:author | pubmed-author:GhassemiFarsh... | lld:pubmed |
pubmed-article:21289290 | pubmed:author | pubmed-author:LoveringRicha... | lld:pubmed |
pubmed-article:21289290 | pubmed:author | pubmed-author:WilderPaul... | lld:pubmed |
pubmed-article:21289290 | pubmed:author | pubmed-author:Hernández-Och... | lld:pubmed |
pubmed-article:21289290 | pubmed:author | pubmed-author:ProsserBenjam... | lld:pubmed |
pubmed-article:21289290 | pubmed:author | pubmed-author:CannonBrian... | lld:pubmed |
pubmed-article:21289290 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:21289290 | pubmed:volume | 300 | lld:pubmed |
pubmed-article:21289290 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:21289290 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:21289290 | pubmed:pagination | C998-C1012 | lld:pubmed |
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pubmed-article:21289290 | pubmed:year | 2011 | lld:pubmed |
pubmed-article:21289290 | pubmed:articleTitle | Modulation of sarcoplasmic reticulum Ca2+ release in skeletal muscle expressing ryanodine receptor impaired in regulation by calmodulin and S100A1. | lld:pubmed |
pubmed-article:21289290 | pubmed:affiliation | Dept. of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599-7260, USA. | lld:pubmed |
pubmed-article:21289290 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:21289290 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:21289290 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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