Evidence map›Paper›PMID 11731586›Full record

ArticleThe Journal of physiology2001

Calponin is required for agonist-induced signal transduction--evidence from an antisense approach in ferret smooth muscle.

H D Je, S S Gangopadhyay, T D Ashworth, K G Morgan

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

28 citing papers in PubMed, 56 citations in OpenAlex.

  1. The machinery of healthy vasoconstriction: an overview.Pflugers Archiv : European journal of physiology · 2025
    Review
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  10. Molluscan smooth catch muscle contains calponin but not caldesmon.Journal of muscle research and cell motility · 2013
    Article
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  15. Scaffolding proteins and non-proliferative functions of ERK1/2.Communicative & integrative biology · 2010
    Article
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  20. Interleukin-10 attenuates vascular responses to endothelin-1 via effects on ERK1/2-dependent pathway.American journal of physiology. Heart and circulatory physiology · 2009
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

H D JeBoston Biomedical Research Institute, Watertown, MA 02472, USA.
S S Gangopadhyay
T D Ashworth
K G Morgan
Boston Biomedical Research Institute · USHarvard University · US

Funding

REGULATION OF CONTRACTION OF BLOOD VESSELSR01HL031704 · NHLBI · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI MORGAN, KATHLEEN G · 1985 to 2009
$3.7M
CONTRACTION OF VASCULAR SMOOTH MUSCLE CELLSR01HL042293 · NHLBI · BOSTON BIOMEDICAL RESEARCH INSTITUTE · PI MORGAN, KATHLEEN G · 1989 to 2004
$1.2M
NHLBI NIH HHS HL31704NHLBI NIH HHS HL42293NHLBI NIH HHS R01 HL031704NHLBI NIH HHS R01 HL042293
6 · The paper itself

Abstract

1. The present study was undertaken to determine whether calponin (CaP) participates in the regulation of vascular smooth muscle contraction and, if so, to investigate the mechanism. 2. By PCR homology cloning, the cDNA sequence of ferret basic (h1) CaP was determined and phosphorothioate antisense and random oligonucleotides were synthesized and introduced into strips of ferret aorta by a chemical loading procedure. 3. Treatment of ferret aorta with CaP antisense oligonucleotides resulted in a decrease in protein levels of CaP to 54% of that in random sequence-loaded muscles, but no change in the protein levels of caldesmon (CaD), actin, desmin or extracellular regulated protein kinase (ERK). 4. Contraction in response to phenylephrine or a phorbol ester was significantly decreased in antisense-treated muscles compared to random sequence-loaded controls. Neither basal intrinsic tone nor the contraction in response to 51 mM KCl was significantly affected by antisense treatment. 5. During phenylephrine contractions, phospho-ERK levels increased, as did myosin light chain (LC20) phosphorylation. Phenylephrine-induced ERK phosphorylation and CaD phosphorylation at an ERK site were significantly decreased by CaP antisense. Increases in myosin light chain phosphorylation were unaffected. 6. The data indicate that CaP plays a significant role in the regulation of contraction and suggest that in a tonically active smooth muscle CaP may function as a signalling protein to facilitate ERK-dependent signalling, but not as a direct regulator of actomyosin interactions at the myofilament level.

Indexed as

Adrenergic alpha-AgonistsAmino Acid SequenceAnimalsAortaBase SequenceCalcium-Binding ProteinsCalponinsDNA, ComplementaryFerretsMicrofilament ProteinsMitogen-Activated Protein KinasesMolecular Sequence DataMuscle, Smooth, VascularMyosin Light ChainsOligonucleotides, AntisenseOrgan Culture TechniquesAdrenergic alpha-AgonistsCalcium-Binding ProteinsCalponinsDNA, ComplementaryMicrofilament ProteinsMitogen-Activated Protein KinasesMyosin Light ChainsOligonucleotides, AntisensePhenylephrineVasoconstrictor Agents

Identifiers

PMID11731586
PMCPMC2278950
OpenAlexW2061481722

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.