Evidence map›Paper›PMID 15041670›Full record

ArticleBiophysical journal2004

Myosin regulatory light chain phosphorylation and strain modulate adenosine diphosphate release from smooth muscle Myosin.

Alexander S Khromov, Martin R Webb, Michael A Ferenczi, David R Trentham, Andrew P Somlyo, Avril V Somlyo

Abstract read
In one paragraph

Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
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

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Adenosine diphosphate and strain sensitivity in myosin motors.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004
    Review
  10. Smooth muscle myosin: regulation and properties.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004
    Review
  11. Obituary. Andrew P. Somlyo (1930-2004).Journal of muscle research and cell motility · 2004
    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

6 authors.

Alexander S KhromovMolecular Physiology and Biological Physics, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908, USA.
Martin R Webb
Michael A Ferenczi
David R Trentham
Andrew P Somlyo
Avril V Somlyo

Funding

THE CONTRACTILE SYSTEM OF VASCULAR SMOOTH MUSCLEP01HL019242 · NHLBI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI OWENS, GARY K · 1985 to 2009
$16.9M
NHLBI NIH HHS 5 PO1 HL19242NHLBI NIH HHS P01 HL019242
6 · The paper itself

Abstract

The effects of myosin regulatory light chain (RLC) phosphorylation and strain on adenosine diphosphate (ADP) release from cross-bridges in phasic (rabbit bladder (Rbl)) and tonic (femoral artery (Rfa)) smooth muscle were determined by monitoring fluorescence transients of the novel ADP analog, 3'-deac-eda-ADP (deac-edaADP). Fluorescence transients reporting release of 3'-deac-eda-ADP were significantly faster in phasic (0.57 +/- 0.06 s(-1)) than tonic (0.29 +/- 0.03 s(-1)) smooth muscles. Thiophosphorylation of regulatory light chains increased and strain decreased the release rate approximately twofold. The calculated (k-ADP/k+ADP) dissociation constant, Kd of unstrained, unphosphorylated cross-bridges for ADP was 0.6 microM for rabbit bladder and 0.3 microM for femoral artery. The rates of ADP release from rigor bridges and reported values of Pi release (corresponding to the steady-state adenosine triphosphatase (ATPase) rate of actomyosin (AM)) from cross-bridges during a maintained isometric contraction are similar, indicating that the ADP-release step or an isomerization preceding it may be limiting the adenosine triphosphatase rate. We conclude that the strain- and dephosphorylation-dependent high affinity for and slow ADP release from smooth muscle myosin prolongs the fraction of the duty cycle occupied by strongly bound actomyosin.ADP state(s) and contributes to the high economy of force.

Indexed as

ActomyosinAdenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateAnimalsFluorescent DyesMuscle ContractionMuscle, SkeletalMuscle, SmoothMyosin Light ChainsPhosphorylationRabbitsSmooth Muscle MyosinsUrinary BladderActomyosinAdenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateFluorescent DyesMyosin Light ChainsSmooth Muscle Myosins

Identifiers

PMID15041670
PMCPMC1304081

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.