Evidence map›Paper›PMID 24213916›Full record

ArticleAmerican journal of physiology. Lung cellular and molecular physiology2014

F-actin scaffold stabilizes lamellar bodies during surfactant secretion.

Mohammad N Islam, Galina A Gusarova, Eiji Monma, Shonit R Das, Jahar Bhattacharya

Open access · greenAbstract read
In one paragraph

Article in American journal of physiology. Lung cellular and molecular physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.7field-weighted citation impact, top 25% 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

16 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. A role for TMEM63 in the lung.The Journal of clinical investigation · 2024
    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

5 authors at 1 institution in 1 country.

Mohammad N Islam630 West 168th St., BB 8-812, New York, NY 10032. jb39@columbia.edu.
Galina A Gusarova
Eiji Monma
Shonit R Das
Jahar Bhattacharya
Columbia University · US

Funding

MICROPUNCTURE STUDIES OF LUNG, WATER AND SOLUTE EXCHANGER01HL036024 · NHLBI · ST. LUKE'S-ROOSEVELT INST FOR HLTH SCIS · PI BHATTACHARYA, JAHAR · 1985 to 2025
$7.0M
MICROSCOPIC IMAGING OF ALVEOLAR FUNCTIONR01HL064896 · NHLBI · ST. LUKE'S-ROOSEVELT INST FOR HLTH SCIS · PI BHATTACHARYA, JAHAR · 2000 to 2011
$4.0M
OPTICAL IMAGING OF LUNG CAPILLARIES IN VIVOR01HL078645 · NHLBI · ST. LUKE'S-ROOSEVELT INST FOR HLTH SCIS · PI BHATTACHARYA, JAHAR · 2004 to 2014
$3.1M
MICROPUNCTURE STUDIES OF LUNG WATER SOLUTE EXCHANGER37HL036024 · NHLBI · ST. LUKE'S-ROOSEVELT INST FOR HLTH SCIS · PI BHATTACHARYA, JAHAR · 1998 to 2007
$3.0M
NHLBI NIH HHS HL-36024NHLBI NIH HHS HL-64896NHLBI NIH HHS HL-78645
6 · The paper itself

Abstract

Alveolar type 2 (AT2) cells secrete surfactant that forms a protective layer on the lung's alveolar epithelium. Vesicles called lamellar bodies (LBs) store surfactant. Failure of surfactant secretion, which causes severe lung disease, relates to the manner in which LBs undergo exocytosis during the secretion. However, the dynamics of LBs during the secretion process are not known in intact alveoli. Here, we addressed this question through real-time confocal microscopy of single AT2 cells in live alveoli of mouse lungs. Using a combination of phospholipid and aqueous fluorophores that localize to LBs, we induced surfactant secretion by transiently hyperinflating the lung, and we quantified the secretion in terms of loss of bulk LB fluorescence. In addition, we quantified inter-LB phospholipid flow through determinations of fluorescence recovery after photobleaching. Furthermore, we determined the role of F-actin in surfactant secretion through expression of the fluorescent F-actin probe Lifeact. Our findings indicate that, in AT2 cells in situ, LBs are held in an F-actin scaffold. Although F-actin transiently decreases during surfactant secretion, the LBs remain stationary, forming a chain of vesicles connected by intervesicular channels that convey surfactant to the secretion site on the plasma membrane. This is the first instance of a secretory process in which the secretory vesicles are immobile, but form a conduit for the secretory material.

Indexed as

Actin CytoskeletonActinsAlveolar Epithelial CellsAnimalsMiceProtein MultimerizationPulmonary Surfactant-Associated Protein BRatsRats, Sprague-DawleySecretory PathwaySecretory VesiclesTissue Culture TechniquesActinsPulmonary Surfactant-Associated Protein Balveolar type 2 cellsfluorescence microscopylung injury

Identifiers

PMID24213916
PMCPMC3920216
OpenAlexW2042903540

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.