Evidence map›Paper›PMID 2960683›Full record

ArticleThe Journal of cell biology1987

The calpactin light chain is tightly linked to the cytoskeletal form of calpactin I: studies using monoclonal antibodies to calpactin subunits.

L Zokas, J R Glenney

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
2.7field-weighted citation impact, top 8% 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

50 citing papers in PubMed, 170 citations in OpenAlex.

  1. Revisiting the role of Annexins in membrane trafficking.Cellular and molecular life sciences : CMLS · 2025
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  7. Annexin A2 heterotetramer: structure and function.International journal of molecular sciences · 2013
    Article
  8. Annexin A2: the importance of being redox sensitive.International journal of molecular sciences · 2013
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
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  15. S100A10/p11: family, friends and functions.Pflugers Archiv : European journal of physiology · 2008
    Review
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  17. Review
  18. Article
  19. Article
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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.

L ZokasMolecular Biology and Virology Laboratory, Salk Institute for Biological Studies, San Diego, California 92138.
J R Glenney
Salk Institute for Biological Studies · US

Funding

MEMBRANE-MICROFILAMENT CONNECTIONSR01GM032866 · NIGMS · UNIVERSITY OF KENTUCKY · PI GLENNEY, JOHN R · 1985 to 1991
–
NIGMS NIH HHS GM32866
6 · The paper itself

Abstract

Calpactins are a family of related Ca++-regulated cytoskeletal proteins. To analyze the expression and cytoskeletal association of calpactins we raised monoclonal antibodies with specificity for the heavy or light chains of calpactin I or to calpactin II. Comparison of the tissue distribution of calpactin I heavy and light chains by Western blots revealed that these subunits are coordinately expressed. Both soluble and cytoskeletal forms of the heavy chain of calpactin I were detected in human fibroblasts whereas only a soluble pool of calpactin II was found. These two forms of the calpactin I heavy chain differed both in their state of association with the light chain and in their rate of turnover. Both the soluble pool of the calpactin I heavy chain and calpactin II turned over three to four times faster than the cytoskeletal pool of heavy and light chains. Immunofluorescence microscopy revealed that the calpactin I light chain was present exclusively in the cytoskeleton whereas the calpactin I heavy chain distribution was more diffuse. No difference in the amount of light chain or the cytoskeletal attachment of phosphorylated calpactin I heavy chain was found in Rous sarcoma virus-transformed chick embryo fibroblasts compared with their normal counterpart. The antibody to the light chain of calpactin I was microinjected into cultured fibroblasts and kidney epithelial cells. In many cases antibody clustering was observed with the concomitant aggregation of the associated calpactin I heavy chain. The distribution of fodrin and calpactin II in injected cells remained unchanged. These results are consistent with the existence of two functionally distinct pools of calpactin I which differ in their association with the cytoskeleton.

Indexed as

AnimalsAnnexinsAntibodies, MonoclonalAntigen-Antibody ComplexCalcium-Binding ProteinsCattleCytoskeletonFibroblastsFluorescent Antibody TechniqueHumansKineticsLungMacromolecular SubstancesAnnexinsAntibodies, MonoclonalAntigen-Antibody ComplexCalcium-Binding ProteinsMacromolecular Substances

Identifiers

PMID2960683
PMCPMC2114835
OpenAlexW2143064177

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LicenceCC BY-NC-SA
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.