ArticleThe Journal of physiology2001
Effects of ADP on sarcoplasmic reticulum function in mechanically skinned skeletal muscle fibres of the rat.
Article in The Journal of physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 72 citations in OpenAlex.
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- Juxtaposition of the changes in intracellular calcium and force during staircase potentiation at 30 and 37°C.The Journal of general physiology · 2014Article
- Sarcoplasmic reticulum Ca2+ uptake and leak properties, and SERCA isoform expression, in type I and type II fibres of human skeletal muscle.The Journal of physiology · 2014Article
- Endogenous and maximal sarcoplasmic reticulum calcium content and calsequestrin expression in type I and type II human skeletal muscle fibres.The Journal of physiology · 2013Article
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- Modulation of contractile apparatus Ca2+ sensitivity and disruption of excitation-contraction coupling by S-nitrosoglutathione in rat muscle fibres.The Journal of physiology · 2011Article
- PERK activation at low glucose concentration is mediated by SERCA pump inhibition and confers preemptive cytoprotection to pancreatic β-cells.Molecular endocrinology (Baltimore, Md.) · 2011Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
1. The sarcoplasmic reticulum (SR) Ca(2+) content (expressed in terms of endogenous SR Ca(2+) content under physiologically resting conditions and measured from caffeine-induced force responses) and the effective rates of the SR Ca(2+) pump and SR Ca(2+) leak (measured from the temporal changes in SR Ca(2+) content) were determined in mechanically skinned skeletal muscle fibres of the rat at different [ADP] (< 0.10 microM to 1.04 mM). 2. The estimated SR Ca(2+) pump rate at 200 nM Ca(2+) did not change when [ADP] increased from below 0.10 microM to 10 microM but decreased by about 30 % when [ADP] increased from 10 microM to 1.04 mM. 3. The rate constant of SR Ca(2+) leak increased markedly with rising [ADP] when [Ca(2+)] in solution was 200 nM (apparent dissociation constant Kd(ADP) = 64 +/- 27 microM). Decreasing the [Ca(2+)] in solution from 200 nM to < 10 nM significantly increased the leak rate constant at all [ADP]. The SR Ca(2+) leak rate constant could be significantly reduced by blocking the SR Ca(2+) pump with 2,5-di(tert-butyl)-1,4-hydroquinone (TBQ). 4. The decrease in the SR Ca(2+) pump rate and the increase in the rate constant of SR Ca(2+) leak when the [ADP] increased from < 0.10 microM to 1.04 mM caused a 4.4-fold decrease in SR Ca(2+) loading ability at 200 nM Ca(2+). 5. The results can be fully explained by a mechanism whereby the presence of ADP causes a marked increase in the ADP-sensitive fraction of the phosphorylated pump protein, which can act as a Ca(2+)-Ca(2+) exchanger and demonstrates that ADP is an important modulator of SR function in skeletal muscle.
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