Evidence map›Paper›PMID 11118508›Full record

ArticleThe Journal of physiology2000

Contractile properties and proteins of smooth muscles of a calponin knockout mouse.

J D Matthew, A S Khromov, M J McDuffie, A V Somlyo, A P Somlyo, S Taniguchi, K Takahashi

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

35 citing papers in PubMed, 93 citations in OpenAlex.

  1. Review
  2. Evolution and function of calponin and transgelin.Frontiers in cell and developmental biology · 2023
    Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
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  11. Article
  12. Review
  13. Article
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  19. Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 2 countries.

J D MatthewDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22906-0011, USA.
A S Khromov
M J McDuffie
A V Somlyo
A P Somlyo
S Taniguchi
K Takahashi
University of Virginia · USOsaka Medical Center for Cancer and Cardiovascular Diseases · JPShinshu University · JP

Funding

THE CONTRACTILE SYSTEM OF VASCULAR SMOOTH MUSCLEP01HL019242 · NHLBI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI OWENS, GARY K · 1985 to 2009
$16.9M
THREE DIMENSIONAL DISTRIBUTION OF ION TRANSPORTING MEMBRANE CHANNELS/ORGANELLESP01HL048807 · NHLBI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI SOMLYO, AVRIL V. · 1992 to 2008
$14.0M
NHLBI NIH HHS P01 HL019242NHLBI NIH HHS P01 HL048807NHLBI NIH HHS P01-HL 19242NHLBI NIH HHS P01-HL 48807
6 · The paper itself

Abstract

The role of h1-calponin in regulating the contractile properties of smooth muscle was investigated in bladder and vas deferens of mice carrying a targeted mutation in both alleles designed to inactivate the basic calponin gene. These calponin knockout (KO) mice displayed no detectable h1-calponin in their smooth muscles. The amplitudes of Ca2+ sensitization, force and Ca2+ sensitivity were not significantly different in permeabilized smooth muscle of KO compared with wild-type (WT) mice, nor were the delays in onset and half-times of Ca2+ sensitization, initiated by flash photolysis of caged GTPgammaS, different. The unloaded shortening velocity (Vus) of thiophosphorylated fibres was significantly (P<0.05) faster in the smooth muscle of KO than WT animals, but could be slowed by exogenous calponin to approximate WT levels; the concentration dependence of exogenous calponin slowing of Vus was proportional to its actomyosin binding in situ. Actin expression was reduced by 25-50%, relative to that of myosin heavy chain, in smooth muscle of KO mice, without any change in the relative distribution of the actin isoforms. We conclude that the faster Vus of smooth muscle of the KO mouse is consistent with, but does not prove without further study, physiological regulation of the crossbridge cycle by calponin. Our results show no detectable role of calponin in the signal transduction of the Ca2+-sensitization pathways in smooth muscle.

Indexed as

AnimalsCalciumCalcium-Binding ProteinsCalponinsContractile ProteinsMaleMesenteric VeinsMiceMice, KnockoutMicrofilament ProteinsMuscle ContractionMuscle ProteinsMuscle RelaxationMuscle, SmoothReference ValuesTime FactorsCalciumCalcium-Binding ProteinsCalponinsContractile ProteinsMicrofilament ProteinsMuscle Proteins

Identifiers

PMID11118508
PMCPMC2270213
OpenAlexW2054029925

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.