Evidence map›Paper›PMID 10595925›Full record

ArticleThe American journal of pathology1999

Human vascular adhesion protein-1 in smooth muscle cells.

K Jaakkola, K Kaunismäki, S Tohka, G Yegutkin, E Vänttinen, T Havia, L J Pelliniemi, M Virolainen, S Jalkanen, M Salmi

Open access · greenAbstract read
In one paragraph

Article in The American journal of pathology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

26 citing papers in PubMed, 85 citations in OpenAlex.

  1. Trial
  2. Review
  3. The role of VAP-1 in cardiovascular disease: a review.Frontiers in cardiovascular medicine · 2025
    Review
  4. Review
  5. Increased atherosclerotic plaque in AOC3 knock-out in ApoEFrontiers in cardiovascular medicine · 2022
    Article
  6. Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Semicarbazide-sensitive amine oxidase in annulo-aortic ectasia disease: relation to elastic lamellae-associated proteins.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2004
    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

10 authors at 3 institutions in 1 country.

K JaakkolaNational Public Health Institute and MediCity Research Laboratory, University of Turku, Finland.
K Kaunismäki
S Tohka
G Yegutkin
E Vänttinen
T Havia
L J Pelliniemi
M Virolainen
S Jalkanen
M Salmi
University of Turku · FITurku University Hospital · FIHelsinki University Hospital · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human vascular adhesion protein-1 (VAP-1) is a dual-function molecule with adhesive and enzymatic properties. In addition to synthesis in endothelial cells, where it mediates lymphocyte binding, VAP-1 is expressed in smooth muscle cells. Here we studied the expression, biochemical structure, and function of VAP-1 in muscle cells and compared it to those in endothelial cells. VAP-1 is expressed on the plasma membrane of all types of smooth muscle cells, but it is completely absent from cardiac and skeletal muscle cells. In tumors, VAP-1 is retained on all leiomyoma cells, whereas it is lost in half of leiomyosarcoma samples. In smooth muscle VAP-1 predominantly exists as a approximately 165-kd homodimeric glycoprotein, but a trimeric (approximately 250 kd) form of VAP-1 is also found. It contains N-linked oligosaccharide side chains and abundant sialic acid decorations. In comparison, in endothelial cells dimeric VAP-1 is larger, no trimeric forms are found, and VAP-1 does not have N-glycanase-sensitive oligosaccharides. Unlike endothelial VAP-1, VAP-1 localized on smooth muscle cells does not support binding of lymphocytes. Instead, it deaminates exogenous and endogenous primary amines. In conclusion, VAP-1 in smooth muscle cells is structurally and functionally distinct from VAP-1 present on endothelial cells.

Indexed as

Amine Oxidase (Copper-Containing)Antibodies, MonoclonalCell Adhesion MoleculesCell LineCell Transformation, NeoplasticDown-RegulationEndotheliumGlycoside HydrolasesHumansImmunoblottingLeiomyosarcomaLymphocytesMicroscopy, ImmunoelectronMonoamine OxidaseMuscle, SmoothMuscle, Smooth, VascularAmine Oxidase (Copper-Containing)Antibodies, MonoclonalAOC3 protein, humanCell Adhesion MoleculesGlycoside HydrolasesMonoamine OxidaseSialoglycoproteins

Identifiers

PMID10595925
PMCPMC1866916
OpenAlexW2157592850

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.