Evidence map›Paper›PMID 8793726›Full record

ArticleJournal of muscle research and cell motility1996

Immunocytochemical localization of caldesmon and calponin in chicken gizzard smooth muscle.

K Mabuchi, Y Li, T Tao, C L Wang

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of muscle research and cell motility, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

18 citing papers in PubMed, 77 citations in OpenAlex.

  1. Calponin 1 contributes to myofibroblast differentiation of human pleural mesothelial cells.American journal of physiology. Lung cellular and molecular physiology · 2022
    Article
  2. Article
  3. Article
  4. Review
  5. Caldesmon and the regulation of cytoskeletal functions.Advances in experimental medicine and biology · 2008
    Review
  6. Direct interaction between caldesmon and cortactin.Archives of biochemistry and biophysics · 2006
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Actin and the smooth muscle regulatory proteins: a structural perspective.Journal of muscle research and cell motility · 2000
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Slow cycling of unphosphorylated myosin is inhibited by calponin, thus keeping smooth muscle relaxed.Proceedings of the National Academy of Sciences of the United States of America · 1997
    Article
  18. 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

4 authors at 1 institution in 1 country.

K MabuchiMuscle Research Group, Boston Biomedical Research Institute, MA 02114, USA.
Y Li
T Tao
C L Wang
Boston Biomedical Research Institute · US

Funding

X-ray Crystallographic Investigation of Smooth Muscle RegulationP01AR041637 · NIAMS · BOSTON BIOMEDICAL RESEARCH INSTITUTE · PI TAO, TERENCE · 1992 to 2007
$15.1M
NIAMS NIH HHS P01-AR41637
6 · The paper itself

Abstract

The distribution of caldesmon and calponin in chicken gizzard smooth muscle was investigated with immunofluorescence and immunogold electron microscopy. Immunofluorescence microscopy showed that in verapamil treated (relaxed) muscles the distributions of caldesmon and myosin appeared to be uniform throughout the cytoplasm, but clearly more textured than that of actin filaments as revealed by the distribution of tropomyosin. In shortened muscles both caldesmon and myosin became segregated, in contrast to the distribution of actin, which remained uniform. The distribution of calponin was even more textured, with no similarity to those of caldesmon or myosin. Instead, considerable overlap was observed between calponin and the cytoskeletal protein desmin and, to a lesser extent, beta-actin. By immunogold electron microscopy caldesmon appeared mostly near and around myosin filaments in both relaxed and shortened muscle. Calponin, on the other hand, was found primarily at the periphery of cytoskeletal structures in the same general region as desmin, and very often adjacent to beta-actin, which is mainly in the core. These observations indicated that caldesmon and calponin are associated with different subsets of actin filaments, caldesmon with contractile actin, while calponin with cytoskeletal actin. Thus the in situ localization of caldesmon is consistent with its proposed regulatory function. Calponin, on the other hand, is unlikely to directly regulate actomyosin interactions in these cells; instead, it may function as a bridging protein between the actin and the intermediate filament networks.

Indexed as

AnimalsAntibodiesBlotting, WesternCalcium-Binding ProteinsCalmodulin-Binding ProteinsCalponinsChickensCross ReactionsCytoplasmFluorescent Antibody TechniqueGizzard, AvianImmunohistochemistryMicrofilament ProteinsMicroscopy, ImmunoelectronMuscle ProteinsMuscle, SmoothAntibodiesCalcium-Binding ProteinsCalmodulin-Binding ProteinsCalponinsMicrofilament ProteinsMuscle ProteinsMyosinsTropomyosin

Identifiers

PMID8793726
OpenAlexW1969184507

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.