Evidence map›Paper›PMID 24440155›Full record

ReviewBiochimica et biophysica acta2014

Thrombospondin-2 and extracellular matrix assembly.

Nicole E Calabro, Nina J Kristofik, Themis R Kyriakides

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

84 citing papers in PubMed, 140 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Article
  5. Article
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  9. Article
  10. The Role of Thrombospondin-2 in Myocardial Fibrosis.Drug design, development and therapy · 2026
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Clinical Insights from Proteomics in Heart Failure.Current heart failure reports · 2025
    Review
  17. Article
  18. Article
  19. Article
  20. Targeting hypoxia and thrombospondin-2 in diabetic wound healing.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Article

24 more citing papers are in PubMed but not listed here.

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.

Nicole E CalabroInterdepartmental Program in Vascular Biology and Therapeutics, Yale University School of Medicine, New Haven, CT 06520, USA; Department of Pathology, Yale University School of Medicine, New Haven, CT 06520, USA.
Nina J KristofikInterdepartmental Program in Vascular Biology and Therapeutics, Yale University School of Medicine, New Haven, CT 06520, USA; Department of Biomedical Engineering, Yale University School of Medicine, New Haven, CT 06520, USA.
Themis R KyriakidesInterdepartmental Program in Vascular Biology and Therapeutics, Yale University School of Medicine, New Haven, CT 06520, USA; Department of Pathology, Yale University School of Medicine, New Haven, CT 06520, USA; Department of Biomedical Engineering, Yale University School of Medicine, New Haven, CT 06520, USA. Electronic address: themis.kyriakides@yale.edu.
Yale University · US

Funding

Surgery / Physiology CoreP01HL107205 · NHLBI · YALE UNIVERSITY · PI SIMONS, MICHAEL · 2012 to 2022
$18.8M
NHLBI NIH HHS HL107205NHLBI NIH HHS P01 HL107205
6 · The paper itself

Abstract

backgroundNumerous proteins and small leucine-rich proteoglycans (SLRPs) make up the composition of the extracellular matrix (ECM). Assembly of individual fibrillar components in the ECM, such as collagen, elastin, and fibronectin, is understood at the molecular level. In contrast, the incorporation of non-fibrillar components and their functions in the ECM are not fully understood. SCOPE OF REVIEW: This review will focus on the role of the matricellular protein thrombospondin (TSP) 2 in ECM assembly. Based on findings in TSP2-null mice and in vitro studies, we describe the participation of TSP2 in ECM assembly, cell-ECM interactions, and modulation of the levels of matrix metalloproteinases (MMPs). MAJOR

conclusionsEvidence summarized in this review suggests that TSP2 can influence collagen fibrillogenesis without being an integral component of fibrils. Altered ECM assembly and excessive breakdown of ECM can have both positive and negative consequences including increased angiogenesis during tissue repair and compromised cardiac tissue integrity, respectively. GENERAL SIGNIFICANCE: Proper ECM assembly is critical for maintaining cell functions and providing structural support. Lack of TSP2 is associated with increased angiogenesis, in part, due to altered endothelial cell-ECM interactions. Therefore, minor changes in ECM composition can have profound effects on cell and tissue function. This article is part of a Special Issue entitled Matrix-mediated cell behaviour and properties.

Indexed as

AnimalsCollagenDisease Models, AnimalExtracellular MatrixHumansPhenotypeThrombospondin 2ThrombospondinsTissue EngineeringCollagenThrombospondin 2ThrombospondinsAngiogenesisCollagenDecellularizationExtracellular matrixThrombospondin

Identifiers

PMID24440155
PMCPMC4074560
OpenAlexW2092401955

What OpenQuestion holds

Textmetadata
LicenceTDM
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.