Evidence map›Paper›PMID 21298062›Full record

ArticlePloS one2011

Comparative proteomic analysis of lung lamellar bodies and lysosome-related organelles.

Ross Ridsdale, Cheng-Lun Na, Yan Xu, Kenneth D Greis, Timothy Weaver

Abstract readComparative Study
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
–field-weighted citation impact
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

35 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Skin lamellar bodies: a unique set of lysosome-related organelles.Frontiers in cell and developmental biology · 2025
    Article
  5. Article
  6. Etiology of lipid-laden macrophages in the lung.International immunopharmacology · 2023
    Review
  7. Article
  8. A dominant negative variant ofProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Review
  10. AP-3-dependent targeting of flippase ATP8A1 to lamellar bodies suppresses activation of YAP in alveolar epithelial type 2 cells.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. The Role of Cholesterol in α-Synuclein and Lewy Body Pathology in GBA1 Parkinson's Disease.Movement disorders : official journal of the Movement Disorder Society · 2021
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Gene-edited MLE-15 Cells as a Model for the Hermansky-Pudlak Syndromes.American journal of respiratory cell and molecular biology · 2018
    Article
  18. A role for P2XThe Journal of general physiology · 2018
    Article
  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

5 authors.

Ross RidsdaleDivision of Pulmonary Biology, Cincinnati Children's Hospital Medical Center, and Department of Pediatrics, University of Cincinnati College of Medicine, Cincinnati, Ohio, United States of America.
Cheng-Lun Na
Yan Xu
Kenneth D Greis
Timothy Weaver

Funding

Structure/Function Analyses Of SP-BR37HL056285 · NHLBI · CINCINNATI CHILDRENS HOSP MED CTR · PI WEAVER, TIMOTHY EDWARD · 2001 to 2010
$5.0M
NHLBI NIH HHS R37 HL056285NHLBI NIH HHS R37HL56285
6 · The paper itself

Abstract

Pulmonary surfactant is a complex mixture of lipids and proteins that is essential for postnatal function. Surfactant is synthesized in alveolar type II cells and stored as multi-bilayer membranes in a specialized secretory lysosome-related organelle (LRO), known as the lamellar body (LB), prior to secretion into the alveolar airspaces. Few LB proteins have been identified and the mechanisms regulating formation and trafficking of this organelle are poorly understood. Lamellar bodies were isolated from rat lungs, separated into limiting membrane and core populations, fractionated by SDS-PAGE and proteins identified by nanoLC-tandem mass spectrometry. In total 562 proteins were identified, significantly extending a previous study that identified 44 proteins in rat lung LB. The lung LB proteome reflects the dynamic interaction of this organelle with the biosynthetic, secretory and endocytic pathways of the type II epithelial cell. Comparison with other LRO proteomes indicated that 60% of LB proteins were detected in one or more of 8 other proteomes, confirming classification of the LB as a LRO. Remarkably the LB shared 37.8% of its proteins with the melanosome but only 9.9% with lamellar bodies from the skin. Of the 229 proteins not detected in other LRO proteomes, a subset of 34 proteins was enriched in lung relative to other tissues. Proteins with lipid-related functions comprised a significant proportion of the LB unique subset, consistent with the major function of this organelle in the organization, storage and secretion of surfactant lipid. The lung LB proteome will facilitate identification of molecular pathways involved in LB biogenesis, surfactant homeostasis and disease pathogenesis.

Indexed as

AnimalsLungLysosomesOrganellesProteinsProteomeProteomicsPulmonary AlveoliPulmonary SurfactantsRatsProteinsProteomePulmonary Surfactants

Identifiers

PMID21298062
PMCPMC3027677

What OpenQuestion holds

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LicenceCC BY
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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.