Evidence map›Paper›PMID 35912991›Full record

ReviewAmerican journal of physiology. Cell physiology2022

The matricellular protein thrombospondin-1 in lung inflammation and injury.

Mohammadreza Tabary, Atish Gheware, Hernán F Peñaloza, Janet S Lee

Open access · greenAbstract readReview
In one paragraph

Review in American journal of physiology. Cell physiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. The emerging role of integrin signaling in pulmonary vascular disease.American journal of physiology. Lung cellular and molecular physiology · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Diagnostic and prognostic utility of plasma thrombospondin-1 levels in traumatic brain injury.European journal of trauma and emergency surgery : official publication of the European Trauma Society · 2024
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Proteoglycans: a common portal for SARS-CoV-2 and extracellular vesicle uptake.American journal of physiology. Cell physiology · 2023
    Review
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 2 institutions in 2 countries.

Mohammadreza TabaryDivision of Pulmonary, Allergy, and Critical Care Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania.
Atish GhewareDivision of Pulmonary, Allergy, and Critical Care Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania.
Hernán F PeñalozaDivision of Pulmonary, Allergy, and Critical Care Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania.
Janet S LeeDivision of Pulmonary, Allergy, and Critical Care Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania.ORCID 0000-0002-6812-6043
University of Pittsburgh · USPontificia Universidad Católica de Chile · CL

Funding

Regulation of Cardiolin Byosynthesis in Epithelial InjuryP01HL114453 · NHLBI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI MALLAMPALLI, RAMA K · 2014 to 2023
$21.3M
Mechanisms of host protection against pathogen-secreted proteases in acute lung injuryR01HL136143 · NHLBI · WASHINGTON UNIVERSITY · PI LEE, JANET SOJUNG · 2017 to 2024
$4.4M
The role of ACOD1 in immunomodulation in intrapulmonary Klebsiella pneumoniae infectionR01HL142084 · NHLBI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI CHEN, KONG · 2018 to 2021
$2.4M
Patient-Oriented Research in Acute Lung Injury and Host Defense in the ICUK24HL143285 · NHLBI · WASHINGTON UNIVERSITY · PI LEE, JANET SOJUNG · 2019 to 2023
$579k
HHS | NIH | National Heart, Lung, and Blood Institute (NHLBI) R01 HL136143,P01HL114453,R01 HL142084,K24 HL143285NHLBI NIH HHS K24 HL143285NHLBI NIH HHS P01 HL114453NHLBI NIH HHS R01 HL136143NHLBI NIH HHS R01 HL142084
6 · The paper itself

Abstract

Matricellular proteins comprise a diverse group of molecular entities secreted into the extracellular space. They interact with the extracellular matrix (ECM), integrins, and other cell-surface receptors, and can alter matrix strength, cell attachment to the matrix, and cell-cell adhesion. A founding member of this group is thrombospondin-1 (TSP-1), a high molecular-mass homotrimeric glycoprotein. Given the importance of the matrix and ECM remodeling in the lung following injury, TSP-1 has been implicated in a number of lung pathologies. This review examines the role of TSP-1 as a damage controller in the context of lung inflammation, injury resolution, and repair in noninfectious and infectious models. This review also discusses the potential role of TSP-1 in human diseases as it relates to lung inflammation and injury.

Indexed as

PneumoniaThrombospondin 1Cell AdhesionExtracellular MatrixExtracellular Matrix ProteinsHumansThrombospondinsExtracellular Matrix ProteinsThrombospondin 1Thrombospondinslung inflammationlung injurymatricellular proteinthrombospondin-1

Identifiers

PMID35912991
PMCPMC9467471
OpenAlexW4289225623

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.