Evidence map›Paper›PMID 20181948›Full record

ArticleThe Journal of biological chemistry2010

Unraveling the specificity of heparanase utilizing synthetic substrates.

Sherket B Peterson, Jian Liu

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

39 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
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  6. Synthetic Heparanase Inhibitors Can Prevent Herpes Simplex Viral Spread.Angewandte Chemie (International ed. in English) · 2023
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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.

Sherket B PetersonDivision of Medicinal Chemistry and Natural Products, Eshelman School of Pharmacy, University of North Carolina, Chapel Hill, North Carolina 27599, USA.
Jian Liu
University of North Carolina at Chapel Hill · US

Funding

In vitro synthesis of recombinant heparan sulfateR01HL094463 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI LIU, JIAN, PAWLINSKI, RAFAL L · 2009 to 2021
$5.2M
Structural Specificity of Heparan Sulfate for Herpes InfectionsR01AI050050 · NIAID · UNIV OF NORTH CAROLINA CHAPEL HILL · PI LIU, JIAN · 2001 to 2010
$2.6M
Glycomics of Heparan Sulfate in Bacterial PathogenesisR21AI074775 · NIAID · UNIV OF NORTH CAROLINA CHAPEL HILL · PI LIU, JIAN, PARK, PYONG WOO · 2009 to 2010
$448k
Enzyme-based approach to probe the specificity of heparanase and its inhibitorF31GM090647 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI PETERSON, SHERKET BRESHON · 2010 to 2012
$89k
NHLBI NIH HHS R01 HL094463NHLBI NIH HHS R01HL094463NIAID NIH HHS R01 AI050050NIAID NIH HHS R01AI050050NIAID NIH HHS R21 AI074775NIAID NIH HHS R21AI074775NIGMS NIH HHS 1F31GM090647-01NIGMS NIH HHS F31 GM090647
6 · The paper itself

Abstract

Heparanase is a promising anticancer target because of its involvement in cancer invasion and metastasis. Heparanase cleaves heparan sulfate (HS), a sulfated polysaccharide, and activates a series of HS-mediated cell proliferation and angiogenesis processes. Understanding the substrate specificity of heparanase will aid the discovery of heparanase inhibitors. Here, we sought to determine the specificity of heparanase using synthetic polysaccharide substrates. The substrates were prepared using purified HS biosynthetic enzymes. Using these substrates, we were able to dissect the structural moieties required for heparanase. Our data suggest that heparanase cleaves the linkage between a GlcA unit and an N-sulfo glucosamine unit carrying either a 3-O-sulfo or a 6-O-sulfo group. In addition, heparanase cleaves the linkage of a GlcA unit and N-sulfo glucosamine unit with a 2-O-sulfated GlcA residue, not a 2-O-sulfated IdoA residue, in proximity. We also discovered that the polysaccharide with repeating disaccharide units of IdoA2S-GlcNS inhibits the activity of heparanase. Our findings advance the understanding of the substrate specificity of heparanase and identify a lead compound for developing polysaccharide-based heparanase inhibitors.

Indexed as

AnimalsCHO CellsCricetinaeCricetulusGlucosamineGlucuronidaseHeparanaseHeparan SulfatePolysaccharidesRecombinant Fusion ProteinsSubstrate SpecificityGlucosamineGlucuronidaseHeparanaseHeparan SulfatePolysaccharidesRecombinant Fusion Proteins

Identifiers

PMID20181948
PMCPMC2863188
OpenAlexW2073968538

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.