Evidence map›Paper›PMID 10982388›Full record

ArticleMolecular biology of the cell2000

Cell contact-dependent activation of alpha3beta1 integrin modulates endothelial cell responses to thrombospondin-1.

L Chandrasekaran, C Z He, H Al-Barazi, H C Krutzsch, M L Iruela-Arispe, D D Roberts

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

63 citing papers in PubMed, 154 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. The Role of Thrombospondin-2 in Myocardial Fibrosis.Drug design, development and therapy · 2026
    Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Functions of Thrombospondin-1 in the Tumor Microenvironment.International journal of molecular sciences · 2021
    Review
  15. Review
  16. Review
  17. Article
  18. A mechanistic evaluation of the angiogenic properties of a dehydrated amnion chorion membrane in vitro and in vivo.Wound repair and regeneration : official publication of the Wound Healing Society [and] the European Tissue Repair Society · 2019
    Article
  19. Article
  20. Article

3 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

6 authors at 2 institutions in 1 country.

L ChandrasekaranLaboratory of Pathology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
C Z He
H Al-Barazi
H C Krutzsch
M L Iruela-Arispe
D D Roberts
National Institutes of Health · USUniversity of California, Los Angeles · US

Funding

CELLULAR INTERACTIONS WITH THROMBOSPONDINZ01SC009172 · SC · DIVISION OF CLINICAL SCIENCES - NCI · PI ROBERTS, DAVID D · 1996 to 2008
$1.7M
NCI NIH HHS CA63356-01
6 · The paper itself

Abstract

Thrombospondin-1 (TSP1) can inhibit angiogenesis by interacting with endothelial cell CD36 or proteoglycan receptors. We have now identified alpha3beta1 integrin as an additional receptor for TSP1 that modulates angiogenesis and the in vitro behavior of endothelial cells. Recognition of TSP1 and an alpha3beta1 integrin-binding peptide from TSP1 by normal endothelial cells is induced after loss of cell-cell contact or ligation of CD98. Although confluent endothelial cells do not spread on a TSP1 substrate, alpha3beta1 integrin mediates efficient spreading on TSP1 substrates of endothelial cells deprived of cell-cell contact or vascular endothelial cadherin signaling. Activation of this integrin is independent of proliferation, but ligation of the alpha3beta1 integrin modulates endothelial cell proliferation. In solution, both intact TSP1 and the alpha3beta1 integrin-binding peptide from TSP1 inhibit proliferation of sparse endothelial cell cultures independent of their CD36 expression. However, TSP1 or the same peptide immobilized on the substratum promotes their proliferation. The TSP1 peptide, when added in solution, specifically inhibits endothelial cell migration and inhibits angiogenesis in the chick chorioallantoic membrane, whereas a fragment of TSP1 containing this sequence stimulates angiogenesis. Therefore, recognition of immobilized TSP1 by alpha3beta1 integrin may stimulate endothelial cell proliferation and angiogenesis. Peptides that inhibit this interaction are a novel class of angiogenesis inhibitors.

Indexed as

AllantoisAnimalsAortaCadherinsCattleCD36 AntigensCell CommunicationCell DivisionCells, CulturedChick EmbryoChorionEndothelium, VascularFibronectinsIntegrin alpha3beta1IntegrinsNeovascularization, PhysiologicCadherinsCD36 AntigensFibronectinsIntegrin alpha3beta1IntegrinsThrombospondin 1

Identifiers

PMID10982388
PMCPMC14963
OpenAlexW2106706809

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.