Phosphorylation of Anchoring Protein by Calmodulin Protein Kinase Associated to the Sarcoplasmic Reticulum of Rabbit Fast-Twitch Muscle

Damiani, Ernesto; Sacchetto, Roberta; Margreth, Alfredo

doi:10.1006/bbrc.2000.3845

Cited by 12 publications

(21 citation statements)

References 31 publications

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“…In fast-twitch fibers, CaMKII targets proteins involved in SR Ca 2ϩ release, i.e., RyR, DHPR, and some of their associated proteins (97,109). In slow-twitch fibers, CaMKII also acts on the SR Ca 2ϩ -ATPase and phospholamban (110,387).…”

Section: Factors Counteracting Fatiguementioning

confidence: 99%

Skeletal Muscle Fatigue: Cellular Mechanisms

Allen¹,

Lamb²,

Westerblad³

2008

Physiological Reviews

1,867

1,876

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Repeated, intense use of muscles leads to a decline in performance known as muscle fatigue. Many muscle properties change during fatigue including the action potential, extracellular and intracellular ions, and many intracellular metabolites. A range of mechanisms have been identified that contribute to the decline of performance. The traditional explanation, accumulation of intracellular lactate and hydrogen ions causing impaired function of the contractile proteins, is probably of limited importance in mammals. Alternative explanations that will be considered are the effects of ionic changes on the action potential, failure of SR Ca2+ release by various mechanisms, and the effects of reactive oxygen species. Many different activities lead to fatigue, and an important challenge is to identify the various mechanisms that contribute under different circumstances. Most of the mechanistic studies of fatigue are on isolated animal tissues, and another major challenge is to use the knowledge generated in these studies to identify the mechanisms of fatigue in intact animals and particularly in human diseases.

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Section: Factors Counteracting Fatiguementioning

confidence: 99%

Skeletal Muscle Fatigue: Cellular Mechanisms

Allen¹,

Lamb²,

Westerblad³

2008

Physiological Reviews

1,867

1,876

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show abstract

“…The myosin regulatory light chain (RLC) is considered to have a central role in this potentiation because there is a correlation between the extent of myosin RLC phosphorylation and force increase (for review, see Ref. 112) and skinned fiber experiments have shown that myosin RLC phosphorylation increases force at submaximal, but not saturating, Ca 2ϩ concentrations (93,113 (33,39). In slow-twitch fibers, CaMKII also acts on the SR Ca 2ϩ ATPase and phospholamban (40,102).…”

Section: Modification Of Sr Calcium Releasementioning

confidence: 99%

Impaired calcium release during fatigue

Allen

Lamb²,

Westerblad³

2008

Journal of Applied Physiology

185

143

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“…TC vesicles from the sucrose-density gradient were extracted with 2% Triton X-100, using experimental conditions identical to those reported by Lee et al (12). Triton extracts (about 5 mg of protein) were incubated with 1 mM CaCl 2, and then centrifuged to equilibrium on a linear 5-30% sucrose gradient, as described (18), except that the gradient contained 1 mM CaCl 2 . Gradient fractions (0.5 ml) were collected from the top of the tube, and protein samples (5-30 l) were analyzed by SDS-PAGE and immunoblotting.…”

Section: Generation and Purification Of 6ϫ His-hrc Fusion Proteinmentioning

confidence: 99%

“…Basal assay conditions for phosphorylation of TC protein, were identical to those previously reported for CaM K II (18,19). The concentration of [␥-32 P]ATP (specific radioactivity 0.10 Ci/mmol), was 400 M. The reaction was stopped by adding SDSsolubilizing buffer to samples.…”

Section: Generation and Purification Of 6ϫ His-hrc Fusion Proteinmentioning

confidence: 99%