Evidence map›Paper›PMID 19004835›Full record

ArticleThe Journal of biological chemistry2009

Differential interactions of thrombospondin-1, -2, and -4 with CD47 and effects on cGMP signaling and ischemic injury responses.

Jeff S Isenberg, Douglas S Annis, Michael L Pendrak, Malgorzata Ptaszynska, William A Frazier, Deane F Mosher, David D Roberts

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

104 citing papers in PubMed, 146 citations in OpenAlex.

  1. Trial
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  13. Emerging functions of thrombospondin-1 in immunity.Seminars in cell & developmental biology · 2024
    Review
  14. Review
  15. Tolerating CD47.Clinical and translational medicine · 2024
    Review
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

44 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

7 authors at 3 institutions in 1 country.

Jeff S IsenbergLaboratory of Pathology, NCI, National Institutes of Health, Bethesda, Maryland 20892, USA.
Douglas S Annis
Michael L Pendrak
Malgorzata Ptaszynska
William A Frazier
Deane F Mosher
David D Roberts
National Institutes of Health · USUniversity of Wisconsin–Madison · USWashington University in St. Louis · US

Funding

Cellular Interactions with ThrombospondinZIASC009172 · NCI · DIVISION OF CLINICAL SCIENCES - NCI · PI ROBERTS, DAVID D · 2009 to 2024
$17.9M
Integrin Associated Protein in a Thrombospondin ReceptorR01HL054390 · NHLBI · WASHINGTON UNIVERSITY · PI FRAZIER, WILLIAM A · 2002 to 2012
$3.4M
THROMBOSPONDIN &MAMMARY ENDOTHELIAL CELL PROLIFERATIONR01HL054462 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI MOSHER, DEANE FREMONT · 1995 to 2007
$3.1M
Integrin Associated Protein in a Thrombospondin ReceptorR56HL054390 · NHLBI · WASHINGTON UNIVERSITY · PI FRAZIER, WILLIAM A · 2007 to 2007
$380k
Intramural NIH HHSNHLBI NIH HHS HL54390NHLBI NIH HHS HL54462
6 · The paper itself

Abstract

Thrombospondin-1 regulates nitric oxide (NO) signaling in vascular cells via CD47. Because CD47 binding motifs are conserved in the C-terminal signature domains of all five thrombospondins and indirect evidence has implied CD47 interactions with other family members, we compared activities of recombinant signature domains of thrombospondin-1, -2, and -4 to interact with CD47 and modulate cGMP signaling. Signature domains of thrombospondin-2 and -4 were less active than that of thrombospondin-1 for inhibiting binding of radiolabeled signature domain of thrombospondin-1 or SIRPalpha (signal-regulatory protein) to cells expressing CD47. Consistent with this binding selectivity, the signature domain of thrombospondin-1 was more potent than those of thrombospondin-2 or -4 for inhibiting NO-stimulated cGMP synthesis in vascular smooth muscle cells and downstream effects on cell adhesion. In contrast to thrombospondin-1- and CD47-null cells, primary vascular cells from thrombospondin-2-null mice lack enhanced basal and NO-stimulated cGMP signaling. Effects of endogenous thrombospondin-2 on NO/cGMP signaling could be detected only in thrombospondin-1-null cells. Furthermore, tissue survival of ischemic injury and acute recovery of blood flow in thrombospondin-2-nulls resembles that of wild type mice. Therefore, thrombospondin-1 is the dominant regulator of NO/cGMP signaling via CD47, and its limiting role in acute ischemic injury responses is not shared by thrombospondin-2.

Indexed as

Signal TransductionAnimalsCD47 AntigenCells, CulturedCyclic GMPHumansIschemiaMaleMiceMice, Inbred C57BLMice, KnockoutNitric OxideProtein BindingReceptors, ImmunologicThrombospondinsCD47 AntigenCyclic GMPNitric OxideReceptors, ImmunologicSirpa protein, mouseThrombospondins

Identifiers

PMID19004835
PMCPMC2613617
OpenAlexW2087929503

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.