Evidence map›Paper›PMID 21193412›Full record

ArticleThe Journal of biological chemistry2011

Pregnancy-specific glycoprotein 1 induces endothelial tubulogenesis through interaction with cell surface proteoglycans.

Felipe A Lisboa, James Warren, Gisela Sulkowski, Marta Aparicio, Guido David, Enrique Zudaire, Gabriela S Dveksler

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

33 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. Biliary atresia-related liver fibrosis.Frontiers in cell and developmental biology · 2026
    Review
  3. Article
  4. Review
  5. Genetic background and biliary atresia.World journal of pediatric surgery · 2025
    Review
  6. Pregnancy and Gastric Cancer: A Narrative Review.Diagnostics (Basel, Switzerland) · 2023
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Role of the pregnancy-specific glycoprotein in regulation of the cytokine and chemokine profiles of intact mononuclear cells.Doklady biological sciences : proceedings of the Academy of Sciences of the USSR, Biological sciences sections · 2017
    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 4 institutions in 2 countries.

Felipe A LisboaDepartment of Pathology, Uniformed Services University of the Health Sciences, Bethesda, Maryland 20814, USA.
James Warren
Gisela Sulkowski
Marta Aparicio
Guido David
Enrique Zudaire
Gabriela S Dveksler
Uniformed Services University of the Health Sciences · USKU Leuven · BENational Cancer Institute · USNational Institutes of Health · US

Funding

FUNCTIONS OF PREGNANCY SPECIFIC GLYCOPROTEINSR01HD035832 · NICHD · HENRY M. JACKSON FDN FOR THE ADV MIL/MED · PI DVEKSLER, GABRIELA S · 2006 to 2010
$1.5M
NICHD NIH HHS R01 HD035832NICHD NIH HHS R01HD035832
6 · The paper itself

Abstract

Pregnancy-specific β1 glycoproteins (PSGs) are the most abundant fetal proteins in the maternal bloodstream in late pregnancy. They are secreted by the syncytiotrophoblast and are detected around day 14 postfertilization. There are 11 human PSG genes, which encode a family of proteins exhibiting significant conservation at the amino acid level. We and others have proposed that PSGs have an immune modulatory function. In addition, we recently postulated that they are proangiogenic due to their ability to induce the secretion of VEGF-A and the formation of tubes by endothelial cells. The cellular receptor(s) for human PSGs remain unknown. Therefore, we conducted these studies to identify the receptor for PSG1, the highest expressed member of the family. We show that removal of cell surface glycosaminoglycans (GAGs) by enzymatic or chemical treatment of cells or competition with heparin completely inhibited binding of PSG1. In addition, PSG1 did not bind to cells lacking heparan or chondroitin sulfate on their surface, and binding was restored upon transfection with all four syndecans and glypican-1. Importantly, the presence of GAGs on the surface of endothelial cells was required for the ability of PSG1 to induce tube formation. This finding indicates that the PSG1-GAG interaction mediates at least some of the PSG1 proposed functions.

Indexed as

AnimalsCHO CellsChondroitin SulfatesCricetinaeCricetulusEndothelial CellsFemaleHeLa CellsHeparan SulfateHeparinHumansJurkat CellsMiceNeovascularization, PhysiologicNIH 3T3 CellsPregnancyChondroitin SulfatesHeparan SulfateHeparinPregnancy-Specific beta 1-GlycoproteinsReceptors, Cell SurfaceSyndecans

Identifiers

PMID21193412
PMCPMC3045012
OpenAlexW2020722973

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.