ArticleThe Journal of biological chemistry2014
A liquid chromatography-mass spectrometry-based approach to characterize the substrate specificity of mammalian heparanase.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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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.
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.
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Who cites it
19 citing papers in PubMed, 33 citations in OpenAlex.
- Glycomics Meets Oncology: The Role of Mass Spectrometry in Cancer Research.Advances in experimental medicine and biology · 2026Review
- A Novel Chimeric Molecule of Heparanase and Ig-Fc Enables Histochemical and Cytochemical Detection ofInternational journal of molecular sciences · 2025Article
- Heparan sulfate chains in hepatocellular carcinoma.Gastroenterology report · 2025Review
- Endoglycosidase assay using enzymatically synthesized fluorophore-labeled glycans as substrates to uncover enzyme substrate specificities.Communications biology · 2022Article
- Implications of Heparanase on Heparin Synthesis and Metabolism in Mast Cells.International journal of molecular sciences · 2022Article
- Specific Non-Reducing Ends in Heparins from Different Animal Origins: Building Blocks Analysis Using Reductive Amination Tagging by Sulfanilic Acid.Molecules (Basel, Switzerland) · 2020Article
- Ultrasensitive small molecule fluorogenic probe for human heparanase.Chemical science · 2020Article
- Inhibition of heparanase protects against pancreatic beta cell death in streptozotocin-induced diabetic mice via reducing intra-islet inflammatory cell infiltration.British journal of pharmacology · 2020Article
- Non-Anticoagulant Heparins as Heparanase Inhibitors.Advances in experimental medicine and biology · 2020Review
- Heparanase as an Additional Tool for Detecting Structural Peculiarities of Heparin Oligosaccharides.Molecules (Basel, Switzerland) · 2019Article
- Sequencing Heparan Sulfate Using HILIC LC-NETD-MS/MS.Analytical chemistry · 2019Article
- Targeting Heparanase in Cancer: Inhibition by Synthetic, Chemically Modified, and Natural Compounds.iScience · 2019Review
- The Development of Assays for Heparanase Enzymatic Activity: Towards a Gold Standard.Molecules (Basel, Switzerland) · 2018Review
- The exostosin family of glycosyltransferases: mRNA expression profiles and heparan sulphate structure in human breast carcinoma cell lines.Bioscience reports · 2018Article
- Imaging specific cellular glycan structures using glycosyltransferases via click chemistry.Glycobiology · 2018Article
- Emerging Roles of Heparanase in Viral Pathogenesis.Pathogens (Basel, Switzerland) · 2017Review
- Mast cell glycosaminoglycans.Glycoconjugate journal · 2017Review
- Non-reducing end labeling of heparan sulfate via click chemistry and a high throughput ELISA assay for heparanase.Glycobiology · 2017Article
- Kinetic analysis and molecular modeling of the inhibition mechanism of roneparstat (SST0001) on human heparanase.Glycobiology · 2016Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Extracellular heparanase activity releases growth factors and angiogenic factors from heparan sulfate (HS) storage sites and alters the integrity of the extracellular matrix. These activities lead to a loss of normal cell matrix adherent junctions and correlate with invasive cellular phenotypes. Elevated expression of heparanase is associated with several human cancers and with vascular remodeling. Heparanase cleaves only a limited fraction of glucuronidic linkages in HS. There have been few investigations of the functional consequences of heparanase activity, largely due to the heterogeneity and complexity of HS. Here, we report a liquid chromatography-mass spectrometry (LC-MS)-based approach to profile the terminal structures created by heparanase digestion and reconstruct the heparanase cleavage sites from the products. Using this method, we demonstrate that heparanase cleaves at the non-reducing side of highly sulfated HS domains, exposing cryptic growth factor binding sites. This cleavage pattern is observed in HS from several tissue sources, regardless of overall sulfation degree, indicating a common recognition pattern. We further demonstrate that heparanase cleavage of HS chains leads to increased ability to support FGF2-dependent cell proliferation. These results suggest a new mechanism to explain how heparanase might potentiate the uncontrolled cell proliferation associated with cancer through its ability to activate nascent growth factor-promoting domains within HS.
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Registered trials
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.