Evidence map›Paper›PMID 24936065›Full record

ArticleThe Journal of biological chemistry2014

Regulation of endothelial cell barrier function by antibody-driven affinity modulation of platelet endothelial cell adhesion molecule-1 (PECAM-1).

Heng Mei, Jay M Campbell, Cathy M Paddock, Panida Lertkiatmongkol, Michael W Mosesson, Ralph Albrecht, Peter J Newman

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.9field-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

23 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Vascular Permeability in Diseases.International journal of molecular sciences · 2022
    Review
  6. Article
  7. Evidence of vasculature and chondrocyte to osteoblast transdifferentiation in craniofacial synovial joints: Implications for osteoarthritis diagnosis and therapy.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article
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.

Heng Mei
Jay M Campbell
Cathy M Paddock
Panida Lertkiatmongkol
Michael W Mosesson
Ralph Albrecht
Peter J Newman
Versiti Blood Center of Wisconsin · USUniversity of Wisconsin–Madison · USMedical College of Wisconsin · US

Funding

Transgenic/Knockout CoreP01HL044612 · NHLBI · VERSITI WISCONSIN, INC. · PI NEWMAN, PETER J · 1990 to 2015
$33.4M
MOLECULAR BIOLOGY &FUNCTION OF PLATELET MEMBRANE GP130R01HL040926 · NHLBI · VERSITI WISCONSIN, INC. · PI NEWMAN, PETER J · 1988 to 2017
$7.4M
NHLBI NIH HHS HL40926NHLBI NIH HHS P01 HL044612NHLBI NIH HHS R01 HL040926
6 · The paper itself

Abstract

PECAM-1 is a 130-kDa member of the immunoglobulin (Ig) superfamily that is expressed on the surface of platelets and leukocytes, and at the intracellular junctions of confluent endothelial cell monolayers. Previous studies have shown that PECAM-1/PECAM-1 homophilic interactions play a key role in leukocyte transendothelial migration, in allowing PECAM-1 to serve as a mechanosensory complex in endothelial cells, in its ability to confer cytoprotection to proapoptotic stimuli, and in maintaining endothelial cell junctional integrity. To examine the adhesive properties of full-length PECAM-1 in a native lipid environment, we purified it from platelets and assembled it into phospholipid nanodiscs. PECAM-1-containing nanodiscs retained not only their ability to bind homophilically to PECAM-1-expressing cells, but exhibited regulatable adhesive interactions that could be modulated by ligands that bind membrane- proximal Ig Domain 6. This property was exploited to enhance the rate of barrier restoration in endothelial cell monolayers subjected to inflammatory challenge. The finding that the adhesive properties of PECAM-1 are regulatable suggests novel approaches for controlling endothelial cell migration and barrier function in a variety of vascular permeability disorders.

Indexed as

AntibodiesCapillary PermeabilityCell MovementHEK293 CellsHumansHuman Umbilical Vein Endothelial CellsMembranes, ArtificialPhospholipidsPlatelet Endothelial Cell Adhesion Molecule-1Protein Structure, TertiaryVascular DiseasesAntibodiesMembranes, ArtificialPhospholipidsPlatelet Endothelial Cell Adhesion Molecule-1

Identifiers

PMID24936065
PMCPMC4110291
OpenAlexW1997146483

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.