Evidence map›Paper›PMID 2537317›Full record

ArticleThe Journal of cell biology1989

Association of gelsolin with actin filaments and cell membranes of macrophages and platelets.

J H Hartwig, K A Chambers, T P Stossel

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
20.1field-weighted citation impact, top 1% 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

41 citing papers in PubMed, 149 citations in OpenAlex.

  1. Article
  2. Regulation of Mitochondrial Function by the Actin Cytoskeleton.Frontiers in cell and developmental biology · 2021
    Review
  3. Low Admission Plasma Gelsolin Concentrations Identify Community-acquired Pneumonia Patients at High Risk for Severe Outcomes.Clinical infectious diseases : an official publication of the Infectious Diseases Society of America · 2019
    Article
  4. Review
  5. Article
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  12. Article
  13. CapZ-lipid membrane interactions: a computer analysis.Theoretical biology & medical modelling · 2006
    Article
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  15. 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

3 authors at 1 institution in 1 country.

J H HartwigHematology-Oncology Unit, Massachusetts General Hospital, Boston 02114.
K A Chambers
T P Stossel
Harvard University · US

Funding

PHAGOCYTOSIS--PULMONARY ALVEOLAR MACROPHAGESR01HL019429 · NHLBI · MASSACHUSETTS GENERAL HOSPITAL · PI STOSSEL, THOMAS PETER · 1985 to 2015
$10.1M
MECHANISM OF F ACTIN CROSSLINKING BY ABPR01GM036507 · NIGMS · MASSACHUSETTS GENERAL HOSPITAL · PI HARTWIG, JOHN H · 1987 to 1989
–
PHAGOCYTOSIS: PULMONARY ALVEOLAR MACROPHAGESR37HL019429 · NHLBI · MASSACHUSETTS GENERAL HOSPITAL · PI STOSSEL, THOMAS PETER · 1989 to 1998
–
NHLBI NIH HHS HL 19429NIGMS NIH HHS GM36507
6 · The paper itself

Abstract

Recent evidence that polyphosphoinositides regulate the function of the actin-modulating protein gelsolin in vitro raises the possibility that gelsolin interacts with cell membranes. This paper reports ultrastructural immunohistochemical data revealing that gelsolin molecules localize with plasma and intracellular membranes, including rough endoplasmic reticulum, cortical vesicles and mitochondria of macrophages, and blood platelets. Anti-gelsolin gold also labeled the surface and interior of secondary lysosomes presumably representing plasma gelsolin ingested by these cells from the lung surface by endocytosis. Gelsolin molecules, visualized with colloidal gold in replicas of the cytoplasmic side of the substrate-adherent plasma membrane of mechanically unroofed and rapidly frozen and freeze-dried macrophages, associated with the ends of short actin filaments sitting on the cytoplasmic membrane surface. A generalized distribution of gelsolin molecules in thin sections of resting platelets rapidly became peripheral, and plasmalemma association increased following thrombin stimulation. At later times the distribution reverted to the cytoplasmic distribution of resting cells. These findings provide the first evidence for gelsolin binding to actin filament ends in cells and indicate that gelsolin functions in both cytoplasmic and membrane domains.

Indexed as

ActinsBlood PlateletsCalcium-Binding ProteinsCell MembraneCytoplasmEndocytosisEndoplasmic ReticulumGelsolinGoldHumansImmunohistochemistryIntracellular MembranesLysosomesMacrophagesMicrofilament ProteinsMicroscopy, ElectronActinsCalcium-Binding ProteinsGelsolinGoldMicrofilament ProteinsThrombin

Identifiers

PMID2537317
PMCPMC2115434
OpenAlexW2024901711

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.