Evidence map›Paper›PMID 32623935›Full record

ReviewThe journal of histochemistry and cytochemistry : official journal of the Histochemistry Society2020

Heparanase-enhanced Shedding of Syndecan-1 and Its Role in Driving Disease Pathogenesis and Progression.

Sunil Rangarajan, Jillian R Richter, Robert P Richter, Shyam K Bandari, Kaushlendra Tripathi, Israel Vlodavsky, Ralph D Sanderson

Open access · bronzeAbstract readReview
In one paragraph

Review in The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

52 citing papers in PubMed, 75 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Article
  5. SSTNSignal transduction and targeted therapy · 2026
    Article
  6. Article
  7. Heparan Sulfate Proteoglycans in Immunity.Proteoglycan research · 2026
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Exosomes are specialized vehicles to induce fibronectin assembly.bioRxiv : the preprint server for biology · 2025
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Observational
  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

7 authors at 2 institutions in 2 countries.

Sunil RangarajanDepartment of Pathology, O'Neal Comprehensive Cancer Center.
Jillian R RichterDepartment of Surgery.
Robert P RichterDepartment of Pediatrics.
Shyam K BandariDepartment of Pathology, O'Neal Comprehensive Cancer Center.
Kaushlendra TripathiDepartment of Pathology, O'Neal Comprehensive Cancer Center.
Israel VlodavskyThe University of Alabama at Birmingham, Birmingham, Alabama, and Technion Integrated Cancer Center, Rappaport Faculty of Medicine, Technion - Israel Institute of Technology, Haifa, Israel.
Ralph D SandersonDepartment of Pathology, O'Neal Comprehensive Cancer Center.
O'Neal Comprehensive Cancer CenterUniversity of Alabama at Birmingham · US

Funding

Heparanase Regulation of Myeloma Metastasis: Mechanism and TherapyR01CA138340 · NCI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI SANDERSON, RALPH D · 2009 to 2018
$3.3M
Heparanase in Tumor Progression, Metastasis and ChemoresistanceR01CA211752 · NCI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI SANDERSON, RALPH D · 2017 to 2021
$1.7M
NCI NIH HHS R01 CA138340NCI NIH HHS R01 CA211752
6 · The paper itself

Abstract

Both heparanase and syndecan-1 are known to be present and active in disease pathobiology. An important feature of syndecan-1 related to its role in pathologies is that it can be shed from the surface of cells as an intact ectodomain composed of the extracellular core protein and attached heparan sulfate and chondroitin sulfate chains. Shed syndecan-1 remains functional and impacts cell behavior both locally and distally from its cell of origin. Shedding of syndecan-1 is initiated by a variety of stimuli and accomplished predominantly by the action of matrix metalloproteinases. The accessibility of these proteases to the core protein of syndecan-1 is enhanced, and shedding facilitated, when the heparan sulfate chains of syndecan-1 have been shortened by the enzymatic activity of heparanase. Interestingly, heparanase also enhances shedding by upregulating the expression of matrix metalloproteinases. Recent studies have revealed that heparanase-induced syndecan-1 shedding contributes to the pathogenesis and progression of cancer and viral infection, as well as other septic and non-septic inflammatory states. This review discusses the heparanase/shed syndecan-1 axis in disease pathogenesis and progression, the potential of targeting this axis therapeutically, and the possibility that this axis is widespread and of influence in many diseases.

Indexed as

Disease ProgressionGlucuronidaseHeparanaseHumansNeoplasmsSyndecan-1Virus DiseasesGlucuronidaseHeparanaseSDC1 protein, humanSyndecan-1cancerglycocalyxheparanaseinflammationorgan failuresepsisshocksyndecan-1therapeuticstraumavirus

Identifiers

PMID32623935
PMCPMC7711244
OpenAlexW3039837059

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.