Evidence map›Paper›PMID 21575570›Full record

ArticleBiophysical journal2011

Effects of conformational peptide probe DP4 on bidirectional signaling between DHPR and RyR1 calcium channels in voltage-clamped skeletal muscle fibers.

Rotimi O Olojo, Erick O Hernández-Ochoa, Noriaki Ikemoto, Martin F Schneider

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

9 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Article
  3. Review of RyR1 pathway and associated pathomechanisms.Acta neuropathologica communications · 2016
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
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

4 authors at 2 institutions in 1 country.

Rotimi O OlojoDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, Maryland, USA.
Erick O Hernández-Ochoa
Noriaki Ikemoto
Martin F Schneider
University of Maryland, Baltimore · USBoston Biomedical Research Institute · US

Funding

Interdisciplinary Training Program Muscle BiologyT32AR007592 · NIAMS · UNIVERSITY OF MARYLAND BALTIMORE · PI Aikaterini Kontrogianni-Konstantopoulos · 1996 to 2026
$11.7M
Roles of voltage sensor, S100A1 and calmodulin in skeletal muscle Ca2+ signalingR37AR055099 · NIAMS · UNIVERSITY OF MARYLAND BALTIMORE · PI SCHNEIDER, MARTIN F · 2012 to 2021
$3.5M
Control of Calcium Release in Skeletal Muscle FibersR01AR055099 · NIAMS · UNIVERSITY OF MARYLAND BALTIMORE · PI SCHNEIDER, MARTIN F · 2007 to 2011
$1.7M
NIAMS NIH HHS R01 AR055099NIAMS NIH HHS R37 AR055099NIAMS NIH HHS T32 AR007592
6 · The paper itself

Abstract

In skeletal muscle, excitation-contraction coupling involves the activation of dihydropyridine receptors (DHPR) and type-1 ryanodine receptors (RyR1) to produce depolarization-dependent sarcoplasmic reticulum Ca²⁺ release via orthograde signaling. Another form of DHPR-RyR1 communication is retrograde signaling, in which RyRs modulate the gating of DHPR. DP4 (domain peptide 4), is a peptide corresponding to residues Leu²⁴⁴²-Pro²⁴⁷⁷ of the central domain of the RyR1 that produces RyR1 channel destabilization. Here we explore the effects of DP4 on orthograde excitation-contraction coupling and retrograde RyR1-DHPR signaling in isolated murine muscle fibers. Intracellular dialysis of DP4 increased the peak amplitude of Ca²⁺ release during step depolarizations by 64% without affecting its voltage-dependence or kinetics, and also caused a similar increase in Ca²⁺ release during an action potential waveform. DP4 did not modify either the amplitude or the voltage-dependence of the intramembrane charge movement. However, DP4 augmented DHPR Ca²⁺ current density without affecting its voltage-dependence. Our results demonstrate that the conformational changes induced by DP4 regulate both orthograde E-C coupling and retrograde RyR1-DHPR signaling.

Indexed as

Action PotentialsAniline CompoundsAnimalsCalciumCalcium Channels, L-TypeDialysisFluorescenceIntracellular SpaceIn Vitro TechniquesIon Channel GatingMiceMuscle Fibers, SkeletalNonlinear DynamicsPatch-Clamp TechniquesPeptidesProtein ConformationAniline CompoundsCalciumCalcium Channels, L-TypeFluo 4PeptidesRyanodine Receptor Calcium Release ChannelXanthenes

Identifiers

PMID21575570
PMCPMC3093551
OpenAlexW1973788054

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.