Evidence map›Paper›PMID 2161855›Full record

ArticleThe Journal of cell biology1990

Gelsolin-actin interaction and actin polymerization in human neutrophils.

T Howard, C Chaponnier, H Yin, T Stossel

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

22 citing papers in PubMed, 80 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Regulation of the actin cycle in vivo by actin filament severing.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  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

4 authors at 1 institution in 1 country.

T HowardDepartment of Pediatrics, University of Alabama, Birmingham 35233.
C Chaponnier
H Yin
T Stossel
University of Alabama at Birmingham · US

Funding

PHAGOCYTOSIS--PULMONARY ALVEOLAR MACROPHAGESR01HL019429 · NHLBI · MASSACHUSETTS GENERAL HOSPITAL · PI STOSSEL, THOMAS PETER · 1985 to 2015
$10.1M
NEUTROPHIL MEMBRANEP01AI028465 · NIAID · MASSACHUSETTS GENERAL HOSPITAL · PI ARNAOUT, M. AMIN · 1989 to 1995
–
NEUTROPHIL MOVEMENT--CELLULAR AND MOLECULAR CONTROLR01AI025214 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI HOWARD, THOMAS H · 1988 to 1992
–
PHAGOCYTOSIS: PULMONARY ALVEOLAR MACROPHAGESR37HL019429 · NHLBI · MASSACHUSETTS GENERAL HOSPITAL · PI STOSSEL, THOMAS PETER · 1989 to 1998
–
NHLBI NIH HHS HL19429NIAID NIH HHS AI25214NIAID NIH HHS AI28465
6 · The paper itself

Abstract

The fraction of polymerized actin in human blood neutrophils increases after exposure to formyl-methionyl-leucyl-phenylalanine (fmlp), is maximal 10 s after peptide addition, and decreases after 300 s. Most of the gelsolin (85 +/- 11%) in resting ficoll-hypaque (FH)-purified neutrophils is in an EGTA resistant, 1:1 gelsolin-actin complex, and, within 5 s after 10(-7) M fmlp activation, the amount of gelsolin complexed with actin decreases to 42 +/- 12%. Reversal of gelsolin binding to actin occurs concurrently with an increase in F-actin content, and the appearance of barbed-end nucleating activity. The rate of dissociation of EGTA resistant, 1:1 gelsolin-actin complexes is more rapid in cells exposed to 10(-7) M fmlp than in cells exposed to 10(-9) M fmlp, and the extent of dissociation 10 s after activation depends upon the fmlp concentration. Furthermore, 300 s after fmlp activation when F-actin content is decreasing, gelsolin reassociates with actin as evidenced by an increase in the amount of EGTA resistant, 1:1 gelsolin-actin complex. Since fmlp induces barbed end actin polymerization in neutrophils and since in vitro the gelsolin-actin complex caps the barbed ends of actin filaments and blocks their growth, the data suggests that in FH neutrophils fmlp-induced actin polymerization could be initiated by the reversal of gelsolin binding to actin and the uncapping of actin filaments or nuclei. The data shows that formation and dissociation of gelsolin-actin complexes, together with the effects of other actin regulatory proteins, are important steps in the regulation of actin polymerization in neutrophils. Finally, finding increased amounts of gelsolin-actin complex in basal FH cells and dissociation of the complex in fmlp-activated cells suggests a mechanism by which fmlp can cause actin polymerization without an acute increase in cytosolic Ca++.

Indexed as

ActinsCalcium-Binding ProteinsCell ExtractsDose-Response Relationship, DrugEgtazic AcidGelsolinHumansMicrofilament ProteinsNeutrophilsN-Formylmethionine Leucyl-PhenylalaninePolymersTemperatureTime FactorsActinsCalcium-Binding ProteinsCell ExtractsEgtazic AcidGelsolinMicrofilament ProteinsN-Formylmethionine Leucyl-PhenylalaninePolymers

Identifiers

PMID2161855
PMCPMC2116138
OpenAlexW2039978832

What OpenQuestion holds

Textmetadata
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.