Evidence map›Paper›PMID 8531200›Full record

ArticleThe Journal of membrane biology1995

Cytoplasmic Ca2+ inhibits the ryanodine receptor from cardiac muscle.

D R Laver, L D Roden, G P Ahern, K R Eager, P R Junankar, A F Dulhunty

Abstract read
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In one paragraph

Article in The Journal of membrane biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
3.5field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

93 citing papers in PubMed, 171 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Molecular pharmacology · 2024
    Article
  5. Article
  6. EuBiophysical journal · 2023
    Article
  7. Article
  8. FKBP12 binds to the cardiac ryanodine receptor with negative cooperativity: implications for heart muscle physiology in health and disease.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Article
  9. Article
  10. Article
  11. CaeLife · 2022
    Article
  12. Review
  13. Regulatory mechanisms of ryanodine receptor/CaJournal of muscle research and cell motility · 2021
    Review
  14. Article
  15. Article
  16. Molecular basis for allosteric regulation of the type 2 ryanodine receptor channel gating by key modulators.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  17. Article
  18. Review
  19. Dysregulated ZnThe Journal of biological chemistry · 2017
    Article
  20. Review

33 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

D R LaverDivision of Neuroscience, John Curtin School of Medical Research, Australian National University, Canberra, Australia.
L D Roden
G P Ahern
K R Eager
P R Junankar
A F Dulhunty
Australian National University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ca(2+)-dependent inhibition of native and isolated ryanodine receptor (RyR) calcium release channels from sheep heart and rabbit skeletal muscle was investigated using the lipid bilayer technique. We found that cytoplasmic Ca2+ inhibited cardiac RyRs with an average Km = 15 mM, skeletal RyRs with Km = 0.7 mM and with Hill coefficients of 2 in both isoforms. This is consistent with measurements of Ca2+ release from the sarcoplasmic reticulum (SR) in skinned fibers and with [3H]-ryanodine binding to SR vesicles, but is contrary to previous bilayer studies which were unable to demonstrate Ca(2+)-inhibition in cardiac RyRs (Chu, Fill, Stefani & Entman (1993) J. Membrane Biol. 135, 49-59). Ryanodine prevented Ca2+ from inhibiting either cardiac or skeletal RyRs. Ca(2+)-inhibition in cardiac RyRs appeared to be the most fragile characteristic of channel function, being irreversibly disrupted by 500 mM Cs+, but not by 500 mM K+, in the cis bath or by solublization with the detergent CHAPS. These treatments had no effect on channel regulation by AMP-PNP, caffeine, ryanodine, ruthenium red, or Ca(2+)-activation. Ca(2+)-inhibition in skeletal RyRs was retained in the presence of 500 mM Cs+. Our results provide an explanation for previous findings in which cardiac RyRs in bilayers with 250 mM Cs+ in the solutions fail to demonstrate Ca(2+)-inhibition, while Ca(2+)-inhibition of Ca2+ release is observed in vesicle studies where K+ is the major cation. A comparison of open and closed probability distributions from individual RyRs suggested that the same gating mechanism mediates Ca(2+)-inhibition in skeletal RyRs and cardiac RyRs, with different Ca2+ affinities for inhibition. We conclude that differences in the Ca(2+)-inhibition in cardiac and skeletal channels depends on their Ca2+ binding properties.

Indexed as

AnimalsCalciumCalcium ChannelsCytoplasmFemaleIn Vitro TechniquesIon Channel GatingLipid BilayersMembrane PotentialsModels, BiologicalMuscle ProteinsMuscle, SkeletalMyocardiumRabbitsRyanodine Receptor Calcium Release ChannelSarcoplasmic ReticulumCalciumCalcium ChannelsLipid BilayersMuscle ProteinsRyanodine Receptor Calcium Release Channel

Identifiers

PMID8531200
OpenAlexW2037138364

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.