Evidence map›Paper›PMID 10388765›Full record

ArticleBiophysical journal1999

The ADP release step of the smooth muscle cross-bridge cycle is not directly associated with force generation.

J A Dantzig, R J Barsotti, S Manz, H L Sweeney, Y E Goldman

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

19 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Myosin IC generates power over a range of loads via a new tension-sensing mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  8. Article
  9. Article
  10. Smooth muscle myosin: regulation and properties.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004
    Review
  11. Article
  12. Review
  13. Myosin isoforms show unique conformations in the actin-bound state.Proceedings of the National Academy of Sciences of the United States of America · 2003
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
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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

5 authors at 1 institution in 1 country.

J A DantzigDepartment of Physiology and Pennsylvania Muscle Institute, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6083, USA.
R J Barsotti
S Manz
H L Sweeney
Y E Goldman
University of Pennsylvania · US

Funding

VASCULAR SMOOTH MUSCLEP01HL015835 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI GOLDMAN, YALE E · 1985 to 2002
$5.5M
MECHANISM OF CARDIAC MUSCLE CONTRACTIONR01HL040953 · NHLBI · THOMAS JEFFERSON UNIVERSITY · PI BARSOTTI, ROBERT J · 1995 to 1999
–
MECHANISM OF CARDIAC MUSCLE CONTRACTIONR29HL040953 · NHLBI · GRADUATE HOSPITAL (PHILADELPHIA) · PI BARSOTTI, ROBERT J · 1988 to 1992
–
NHLBI NIH HHS HL 15835NHLBI NIH HHS HL 40953
6 · The paper itself

Abstract

When smooth muscle myosin subfragment 1 (S1) is bound to actin filaments in vitro, the light chain domain tilts upon release of MgADP, producing a approximately 3.5-nm axial motion of the head-rod junction (Whittaker et al., 1995. Nature. 378:748-751). If this motion contributes significantly to the power stroke, rigor tension of smooth muscle should decrease substantially in response to cross-bridge binding of MgADP. To test this prediction, we monitored mechanical properties of permeabilized strips of chicken gizzard muscle in rigor and in the presence of MgADP. For comparison, we also tested psoas and soleus muscle fibers. Any residual bound ADP was minimized by incubation in Mg2+-free rigor solution containing 15 mM EDTA. The addition of 2 mM MgADP, while keeping ionic strength and free Mg2+ concentration constant, resulted in a slight increase in rigor tension in both gizzard and soleus muscles, but a decrease in psoas muscle. In-phase stiffness monitored during small (<0.1%) 500-Hz sinusoidal length oscillations decreased in all three muscle types when MgADP was added. The changes in force and stiffness with the addition of MgADP were similar at ionic strengths from 50 to 200 mM and were reversible. The results with gizzard muscle were similar after thiophosphorylation of the regulatory light chain of myosin. These results suggest that the axial motion of smooth muscle S1 bound to actin, upon dissociation of MgADP, is not associated with force generation. The difference between the present mechanical data and previous structural studies of smooth S1 may be explained if geometrical constraints of the intact contractile filament array alter the motions of the myosin heads.

Indexed as

Muscle ContractionActinsAdenosine DiphosphateAnimalsChickensMuscle, SkeletalMuscle, SmoothMyosin SubfragmentsOsmolar ConcentrationPhosphorylationProtein BindingRabbitsActinsAdenosine DiphosphateMyosin Subfragments

Identifiers

PMID10388765
PMCPMC1300337
OpenAlexW1974271806

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.