Evidence map›Paper›PMID 17635638›Full record

ReviewJournal of cellular and molecular medicine

Mammalian heparanase: what is the message?

Veronique Vreys, Guido David

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of cellular and molecular medicine. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 128 papers.

0numbers the graph read from it
0cells of the map it votes in
128citing papers in PubMed
6.4field-weighted citation impact, top 3% 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

128 citing papers in PubMed, 221 citations in OpenAlex.

  1. Article
  2. The Pathophysiological Functions of Heparanases: From Evolution, Structural and Tissue-Specific Perspectives.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Review
  3. Article
  4. Review
  5. Review
  6. Review
  7. Review
  8. Article
  9. Review
  10. Heparanase Inhibition Prevents Liver Steatosis in EJournal of clinical medicine · 2022
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. The glycocalyx: a central regulator of vascular function.American journal of physiology. Regulatory, integrative and comparative physiology · 2021
    Review
  18. Article
  19. Article
  20. Article

68 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

2 authors at 1 institution in 1 country.

Veronique VreysDepartment of Molecular and Developmental Genetics, VIB, Leuven, Belgium.
Guido David
KU Leuven · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heparan sulphate proteoglycans are ubiquitous macromolecules of cell surfaces and extracellular matrices. Numerous extracellular matrix proteins, growth factors, morphogens, cytokines, chemokines and coagulation factors are bound and regulated by heparan sulphate. Degradation of heparan sulphate thus potentially profoundly affects cell and tissue function. Although there is evidence that several heparan sulphate-degrading endoglucuronidases (heparanases) might exist, so far only one transcript encoding a functional heparanase has been identified: heparanase-1. In the first part of this review, we discuss the current knowledge about heparan sulphate proteoglycans and the functional importance of their versatile interactions. In the second part, we summarize recent findings that have contributed to the characterization of heparanase-1, focusing on the molecular properties, working mechanism, substrate specificity, expression pattern, cellular activation and localization of this enzyme. Additionally, we review data implicating heparanase-1 in several normal and pathological processes, focusing on tumour metastasis and angiogenesis, and on evidence for a potentially direct signalling function of the molecule. In that context, we also briefly discuss heparanase-2, an intriguing close homologue of heparanase-1, for which, so far, no heparan sulphate-degrading activity could be demonstrated.

Indexed as

Amino Acid SequenceAnimalsEnzyme ActivationGlucuronidaseHeparanaseHeparan Sulfate ProteoglycansHumansMammalsMolecular Sequence DataNeoplasmsSubstrate SpecificityGlucuronidaseHeparanaseHeparan Sulfate Proteoglycans

Identifiers

PMID17635638
PMCPMC3922351
OpenAlexW2100864793

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.