Evidence map›Paper›PMID 8280082›Full record

ArticleThe Biochemical journal1993

Calponin phosphorylation in vitro and in intact muscle.

S J Winder, B G Allen, E D Fraser, H M Kang, G J Kargacin, M P Walsh

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
6.7field-weighted citation impact, top 3% 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

31 citing papers in PubMed, 92 citations in OpenAlex.

  1. Review
  2. Article
  3. A rapid degradation of calponin 2 is required for cytokinesis.American journal of physiology. Cell physiology · 2021
    Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Maturation and the role of PKC-mediated contractility in ovine cerebral arteries.American journal of physiology. Heart and circulatory physiology · 2009
    Article
  15. Review
  16. Smooth muscle signalling pathways in health and disease.Journal of cellular and molecular medicine · 2008
    Review
  17. Article
  18. Review
  19. Article
  20. 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

6 authors at 1 institution in 1 country.

S J WinderMRC Group in Signal Transduction, University of Calgary, Alberta, Canada.
B G Allen
E D Fraser
H M Kang
G J Kargacin
M P Walsh
University of Calgary · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Calponin, a thin-filament-associated protein implicated in the regulation of smooth-muscle contraction, is phosphorylated in vitro by protein kinase C and Ca2+/calmodulin-dependent protein kinase II [Winder and Walsh (1990) J. Biol. Chem. 265, 10148-10155] and dephosphorylated by a type 2A protein phosphatase [Winder, Pato and Walsh (1992) Biochem. J. 286, 197-203]. Unphosphorylated calponin binds to actin and inhibits the actin-activated myosin MgATPase; these properties are lost on phosphorylation. Although both serine and threonine residues in calponin are phosphorylated, the major site of phosphorylation by either kinase is Ser-175. Calponin also undergoes phosphorylation when bound to actin in synthetic thin filaments, in a reconstituted actomyosin system, in washed myofibrils and in tissue extracts; this results in dissociation of calponin from actin. Tryptic phosphopeptide mapping indicates that the same sites are phosphorylated in the bound as in the isolated protein. Toad stomach calponin exists in at least three isoforms which differ in charge but exhibit the same molecular mass on SDS/PAGE. In a toad stomach extract, all three isoforms are phosphorylated by protein kinase C or Ca2+/calmodulin-dependent protein kinase II as shown by two-dimensional gel electrophoresis (non-equilibrium pH-gradient gel electrophoresis and SDS/PAGE). Calponin phosphorylation also occurs in intact toad stomach smooth-muscle strips metabolically labelled with 32Pi and stimulated to contract with carbachol. These results support the hypothesis that calponin may be regulated in vivo by phosphorylation-dephosphorylation.

Indexed as

Amino Acid SequenceAnimalsAnuraCalcium-Binding ProteinsCalcium-Calmodulin-Dependent Protein KinasesCalponinsIn Vitro TechniquesMicrofilament ProteinsMolecular Sequence DataMuscle ContractionMuscle ProteinsMuscle, SmoothPeptide FragmentsPhosphorylationCalcium-Binding ProteinsCalcium-Calmodulin-Dependent Protein KinasesCalponinsMicrofilament ProteinsMuscle ProteinsPeptide Fragments

Identifiers

PMID8280082
PMCPMC1137769
OpenAlexW2135424171

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.