1988
DOI: 10.1016/0005-2736(88)90124-1
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Inhibition of calcium release from skeletal muscle sarcoplasmic reticulum by calmodulin

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Cited by 30 publications
(13 citation statements)
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“…It has been reported that calmodulin (CaM) inhibits Ca 2ϩ -, caffeine-, and AMP-induced Ca 2ϩ release from cardiac and skeletal muscle SR (11,21,22,35). Plank et al (35) found that the caffeine-induced Ca 2ϩ release from actively loaded SR vesicles is reduced to 51% of the respective control value by 1 M exogenous CaM.…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…It has been reported that calmodulin (CaM) inhibits Ca 2ϩ -, caffeine-, and AMP-induced Ca 2ϩ release from cardiac and skeletal muscle SR (11,21,22,35). Plank et al (35) found that the caffeine-induced Ca 2ϩ release from actively loaded SR vesicles is reduced to 51% of the respective control value by 1 M exogenous CaM.…”
Section: Discussionmentioning
confidence: 99%
“…It has been reported that calmodulin (CaM) inhibits Ca 2ϩ -, caffeine-, and AMP-induced Ca 2ϩ release from cardiac and skeletal muscle SR (11,21,22,35). Plank et al (35) found that the caffeine-induced Ca 2ϩ release from actively loaded SR vesicles is reduced to 51% of the respective control value by 1 M exogenous CaM. Furthermore, it was reported that a synthetic peptide containing residues 3,614 to 3,643 of the RyR1 was found to be capable of binding with high affinity either apo-CaM or Ca 2ϩ /CaM (23,40), suggesting that CaM could participate as a negative module in R9 RyR1 .…”
Section: Discussionmentioning
confidence: 99%
“…Channel inhibition was reversible and an only partial (twoto sixfold) rather than complete inhibition by CaM was observed. Calmodulin inhibited SR Ca2+ release and single-channel activities in the absence of ATP, which suggested a direct inhibitory action of CaM (Meissner, 1986;Meissner and Henderson, 1987;Plank et al, 1988;Fuentes et al, 1994).…”
Section: Introductionmentioning
confidence: 95%
“…Importantly, suramin and the related agonist NF307 bind to the calmodulin‐binding site of the RyR1 but mimic only the stimulatory effect of calmodulin ( Klinger et al ., 1999 ; Papineni et al ., 2002 ). Apocalmodulin acts as an activator, whereas Ca 2+ bound to the COOH‐terminal end of calmodulin switches the protein to an inhibitor ( Plank et al ., 1988 ; Smith et al ., 1989 ; Buratti et al ., 1995 ; Tripathy et al ., 1995 ; Rodney et al ., 2001 ). The calmodulin‐binding site was mapped to a peptide stretched from RyR1 amino acids 3609–3643 ( Moore et al ., 1999 ; Rodney et al ., 2000 ; 2001 ).…”
Section: Discussionmentioning
confidence: 99%
“…Out of these, calmodulin exerts a dualistic influence on the RyR1 depending on the free Ca 2+ concentration ( Tripathy et al ., 1995 ; Rodney et al ., 2000 ). In its Ca 2+ ‐free form, calmodulin (apocalmodulin) activates the RyR1, but Ca 2+ ‐liganded calmodulin is an inhibitor of the channel ( Plank et al ., 1988 ; Smith et al ., 1989 ; Buratti et al ., 1995 ; Tripathy et al ., 1995 ).…”
Section: Introductionmentioning
confidence: 99%