Evidence map›Paper›PMID 25446551›Full record

ArticleMatrix biology : journal of the International Society for Matrix Biology2015

Osteopontin binding to the alpha 4 integrin requires highest affinity integrin conformation, but is independent of post-translational modifications of osteopontin.

Tommy Hui, Esben S Sørensen, Susan R Rittling

Open access · goldAbstract readComparative Study
PubMed Full text at PMC Publisher
In one paragraph

Article in Matrix biology : journal of the International Society for Matrix Biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Potential Targeting Mechanisms for Bone-Directed Therapies.International journal of molecular sciences · 2024
    Review
  6. Methods to Investigate Thrombin Cleavage of Osteopontin (OPN).Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Prostate cancer sheds the αvβ3 integrin in vivo through exosomes.Matrix biology : journal of the International Society for Matrix Biology · 2019
    Article
  12. Article
  13. Exosomal αvβ6 integrin is required for monocyte M2 polarization in prostate cancer.Matrix biology : journal of the International Society for Matrix Biology · 2018
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Osteopontin in Immune-mediated Diseases.Journal of dental research · 2015
    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

3 authors at 2 institutions in 2 countries.

Tommy HuiDepartment of Immunology and Infectious Disease, The Forsyth Institute, Cambridge, MA, USA.
Esben S SørensenDepartment of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark.
Susan R RittlingDepartment of Immunology and Infectious Disease, The Forsyth Institute, Cambridge, MA, USA; Department of Developmental Biology, Harvard School of Dental Medicine, Boston, MA, USA. Electronic address: srittling@forsyth.org.
Aarhus University · DKHarvard University · US

Funding

Osteopontin and Integrins in Innate Immune Responses to Polymicrobial InfectionR01DE022380 · NIDCR · ADA FORSYTH INSTITUTE, INC. · PI RITTLING, SUSAN R · 2012 to 2016
$2.4M
NIDCR NIH HHS R01 DE022380NIDCR NIH HHS R01DE022380
6 · The paper itself

Abstract

Osteopontin (OPN) is a ligand for the α4ß1 integrin, but the physiological importance of this binding is not well understood. Here, we have assessed the effect of post-translational modifications on OPN binding to the α4 integrin on cultured human leukocyte cell lines and compared OPN interaction with α4 integrin to that of VCAM and fibronectin. Jurkat cells, whose α4 integrins are inherently activated, adhered to different preparations of OPN in the presence of Mn(2+): the EC50 of adhesion was not affected by phosphorylation or glycosylation status. Thrombin cleavage of OPN at the C-terminus of the α4 integrin-binding site also did not affect binding affinity. THP-1 cells express a low-affinity conformation of the integrin and adhered to OPN only in the presence of Mn(2+) plus PMA or an activating antibody. This was in contrast to VCAM and fibronectin: THP-1 cells adhered to these ligands without integrin activation. Studies with ligand-induced binding site antibodies demonstrated that the SVVYGLR peptide of OPN bound to the α4 integrin with a similar affinity as the LDV peptide of fibronectin, suggesting that a high off-rate is responsible for the reduced binding of OPN to the low-affinity forms of this integrin. Together, the results suggest OPN has very low affinity for the α4 integrin on human leukocytes under physiological conditions.

Indexed as

Binding SitesCell Line, TumorHumansIntegrin alpha4Integrin alpha5beta1Jurkat CellsLeukocytesOsteopontinPhosphorylationProtein ConformationProtein Processing, Post-TranslationalThrombinVascular Cell Adhesion Molecule-1Integrin alpha4Integrin alpha5beta1OsteopontinSPP1 protein, humanThrombinVascular Cell Adhesion Molecule-1AdhesionIntegrin Alpha4OsteopontinPhosphorylationVCAMVLA-4

Identifiers

PMID25446551
PMCPMC4912046
OpenAlexW1981810203

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.