Evidence map›Paper›PMID 16333357›Full record

ReviewCanadian journal of physiology and pharmacology2005

The latch-bridge hypothesis of smooth muscle contraction.

Richard A Murphy, Christopher M Rembold

Abstract readReview
In one paragraph

Review in Canadian journal of physiology and pharmacology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
1.4field-weighted citation impact, top 17% 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

39 citing papers in PubMed, 75 citations in OpenAlex.

  1. Review
  2. Coronary Spasm Due to Pulsed Field Ablation: A State-of-the-Art Review.Pacing and clinical electrophysiology : PACE · 2026
    Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. A multiscale sliding filament model of lymphatic muscle pumping.Biomechanics and modeling in mechanobiology · 2021
    Article
  11. Article
  12. Article
  13. Dynamic cytosolic CaAmerican journal of physiology. Lung cellular and molecular physiology · 2021
    Article
  14. Effects of TNFα on Dynamic Cytosolic CaFrontiers in physiology · 2021
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

2 authors at 1 institution in 1 country.

Richard A MurphyDepartment of Molecular Physiology and Biological Physics, University of Virginia Health Sciences Center, Charlottesville, VA 22908, USA. ram4s@virginia.edu
Christopher M Rembold
University of Virginia · US

Funding

NO-CGMP INHIBITION OF UROGENITAL SMOOTH MUSCLER01DK056034 · NIDDK · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI REMBOLD, CHRISTOPHER M · 2001 to 2004
$1.4M
P20-Mediated Suppression of Vascular ForceR01HL071191 · NHLBI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI REMBOLD, CHRISTOPHER M · 2002 to 2004
$999k
NHLBI NIH HHS HL71191NHLBI NIH HHS R01 HL071191NIDDK NIH HHS DK56034NIDDK NIH HHS R01 DK056034
6 · The paper itself

Abstract

In contrast to striated muscle, both normalized force and shortening velocities are regulated functions of cross-bridge phosphorylation in smooth muscle. Physiologically this is manifested as relatively fast rates of contraction associated with transiently high levels of cross-bridge phosphorylation. In sustained contractions, Ca2+, cross-bridge phosphorylation, and ATP consumption rates fall, a phenomenon termed "latch". This review focuses on the Hai and Murphy (1988a) model that predicted the highly non-linear dependence of force on phosphorylation and a directly proportional dependence of shortening velocity on phosphorylation. This model hypothesized that (i) cross-bridge phosphorylation was obligatory for cross-bridge attachment, but also that (ii) dephosphorylation of an attached cross-bridge reduced its detachment rate. The resulting variety of cross-bridge cycles as predicted by the model could explain the observed dependencies of force and velocity on cross-bridge phosphorylation. New evidence supports modifications for more general applicability. First, myosin light chain phosphatase activity is regulated. Activation of myosin phosphatase is best demonstrated with inhibitory regulatory mechanisms acting via nitric oxide. The second modification of the model incorporates cooperativity in cross-bridge attachment to predict improved data on the dependence of force on phosphorylation. The molecular basis for cooperativity is unknown, but may involve thin filament proteins absent in striated muscle.

Indexed as

Models, BiologicalAnimalsCalciumCyclic AMPMuscle ContractionMuscle, SkeletalMuscle, SmoothMyosin-Light-Chain PhosphataseNitric OxidePhosphorylationCalciumCyclic AMPMyosin-Light-Chain PhosphataseNitric Oxide

Identifiers

PMID16333357
PMCPMC2278007
OpenAlexW2118471443

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.