Evidence map›Paper›PMID 35036899›Full record

ArticleMatrix biology plus2022

Heparanase as active player in endothelial glycocalyx remodeling.

Valentina Masola, Nicola Greco, Giovanni Gambaro, Marco Franchi, Maurizio Onisto

Open access · goldAbstract read
In one paragraph

Article in Matrix biology plus, 2022. 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
2.8field-weighted citation impact, top 9% 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, 37 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. Heparan Sulfate Proteoglycans in Immunity.Proteoglycan research · 2026
    Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Endothelial Surface Glycocalyx in Vascular Functions and Diseases.Advances in experimental medicine and biology · 2026
    Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Understanding Viral-Glycocalyx Interactions Using Brush-Linked to Cross-Linked Models.Langmuir : the ACS journal of surfaces and colloids · 2025
    Article
  17. Review
  18. Review
  19. Review
  20. 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

5 authors at 3 institutions in 1 country.

Valentina MasolaRenal Unit, Dept. of Medicine, University Hospital of Verona, Verona, Italy.
Nicola GrecoDept. of Biomedical Sciences, University of Padova, Padua, Italy.
Giovanni GambaroRenal Unit, Dept. of Medicine, University Hospital of Verona, Verona, Italy.
Marco FranchiDept. of Life Quality Sciences, University of Bologna, Rimini, Italy.
Maurizio OnistoDept. of Biomedical Sciences, University of Padova, Padua, Italy.
University of Padua · ITUniversity of Verona · ITUniversity of Bologna · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The surface of all animal cells is coated with a layer of carbohydrates linked in various ways to the outer side of the plasma membrane. These carbohydrates are mainly bound to proteins in the form of glycoproteins and proteoglycans and together with the glycolipids constitute the so-called glycocalyx. In particular, the endothelial glycocalyx that covers the luminal layer of the endothelium is composed of glycosaminoglycans (heparan sulphate -HS and hyaluronic acid -HA), proteoglycans (syndecans and glypicans) and adsorbed plasma proteins. Thanks to its ability to absorb water, this structure contributes to making the surface of the vessels slippery but at the same time acts by modulating the mechano-transduction of the vessels, the vascular permeability and the adhesion of leukocytes in thus regulating several physiological and pathological events. Among the various enzymes involved in the degradation of the glycocalyx, heparanase (HPSE) has been shown to be particularly involved. This enzyme is responsible for the cutting of heparan sulfate (HS) chains at the level of the proteoglycans of the endothelial glycocalyx whose dysfunction appears to have a role in organ fibrosis, sepsis and viral infection. In this mini-review, we describe the mechanisms by which HPSE contributes to glycocalyx remodeling and then examine the role of glycocalyx degradation in the development of pathological conditions and pharmacological strategies to preserve glycocalyx during disease pathogenesis.

Indexed as

EndotheliumGlycocalyxHeparanase

Identifiers

PMID35036899
PMCPMC8749438
OpenAlexW4200154949

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.