Evidence map›Paper›PMID 23192608›Full record

ArticleJournal of cellular biochemistry2013

Osteopontin mediates macrophage chemotaxis via α4 and α9 integrins and survival via the α4 integrin.

Susan Amanda Lund, Carole L Wilson, Elaine W Raines, Jingjing Tang, Cecilia M Giachelli, Marta Scatena

Open access · greenAbstract read
In one paragraph

Article in Journal of cellular biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
3.9field-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

61 citing papers in PubMed, 103 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Review
  5. Article
  6. The emerging role of integrin signaling in pulmonary vascular disease.American journal of physiology. Lung cellular and molecular physiology · 2026
    Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. The injury effect of osteopontin in sepsis-associated lung injury.Journal of inflammation (London, England) · 2025
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Review

1 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 1 institution in 1 country.

Susan Amanda LundDepartment of Bioengineering, University of Washington, Seattle, WA 98109, USA.
Carole L Wilson
Elaine W Raines
Jingjing Tang
Cecilia M Giachelli
Marta Scatena
University of Washington · US

Funding

VLA-4 and VCAM-1 in Advanced AtherosclerosisP01HL018645 · NHLBI · UNIVERSITY OF WASHINGTON · PI CHAIT, ALAN · 1985 to 2010
$23.9M
NHLBI NIH HHS HL-018645NHLBI NIH HHS P01 HL018645
6 · The paper itself

Abstract

Osteopontin (OPN) is highly expressed by macrophages and plays a key role in the pathology of several chronic inflammatory diseases including atherosclerosis and the foreign body reaction. However, the molecular mechanism behind OPN regulation of macrophage functions is not well understood. OPN is a secreted molecule and interacts with several integrins via two domains: the RGD sequence binding to α(v) -containing integrins, and the SLAYGLR sequence binding to α(4) β(1), α(4) β(7), and α(9) β(1) integrins. Here we determined the role of OPN in macrophage survival, chemotaxis, and activation state. For survival studies, OPN treated-bone marrow derived macrophages (BMDMs) were challenged with growth factor withdrawal and neutralizing integrin antibodies. We found that survival in BMDMs is mediated primarily through the α(4) integrin. In chemotaxis studies, we observed that migration to OPN was blocked by neutralizing α(4) and α(9) integrin antibodies. Further, OPN did not affect macrophage activation as measured by IL-12 production. Finally, the relative contributions of the RGD and the SLAYGLR functional domains of OPN to leukocyte recruitment were evaluated in an in vivo model. We generated chimeric mice expressing mutated forms of OPN in myeloid-derived leukocytes, and found that the SLAYGLR functional domain of OPN, but not the RGD, mediates macrophage accumulation in response to thioglycollate-elicited peritonitis. Collectively, these data indicate that α(4) and α(9) integrins interacting with OPN via the SLAYGLR domain play a key role in macrophage biology by regulating migration, survival, and accumulation.

Indexed as

ChemotaxisAmino Acid SequenceAnimalsBone Marrow CellsCell SurvivalCytokinesInflammation MediatorsIntegrin alpha4Integrin alpha ChainsMacrophagesMiceMice, Inbred C57BLMolecular Sequence DataOsteopontinPeritonitisPhenotypeCytokinesInflammation MediatorsIntegrin alpha4integrin alpha9Integrin alpha ChainsOsteopontinThioglycolates

Identifiers

PMID23192608
PMCPMC12462639
OpenAlexW2035744669

What OpenQuestion holds

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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.