ArticleThe Biochemical journal2003
Biochemical characterization of the active heterodimer form of human heparanase (Hpa1) protein expressed in insect cells.
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 115 citations in OpenAlex.
- Heparanase-A single protein with multiple enzymatic and nonenzymatic functions.Proteoglycan research · 2023Review
- Role of heparanase in ARDS through autophagy and exosome pathway (review).Frontiers in pharmacology · 2023Review
- Forty Years of Basic and Translational Heparanase Research.Advances in experimental medicine and biology · 2020Review
- Polymeric fluorescent heparin as one-step FRET substrate of human heparanase.Carbohydrate polymers · 2019Article
- Heparanase attenuates axon degeneration following sciatic nerve transection.Scientific reports · 2018Article
- Activity-based probes for functional interrogation of retaining β-glucuronidases.Nature chemical biology · 2017Article
- Structural characterization of human heparanase reveals insights into substrate recognition.Nature structural & molecular biology · 2015Article
- Vascular endothelial growth factor c/vascular endothelial growth factor receptor 3 signaling regulates chemokine gradients and lymphocyte migration from tissues to lymphatics.Transplantation · 2015Article
- Overexpression of heparanase is associated with preeclampsia by inhibiting invasion of trophocytes.International journal of clinical and experimental medicine · 2015Article
- Heparanase is preferentially expressed in human psoriatic lesions and induces development of psoriasiform skin inflammation in mice.Cellular and molecular life sciences : CMLS · 2014Article
- Anti-heparanase aptamers as potential diagnostic and therapeutic agents for oral cancer.PloS one · 2014Article
- Versatile role of heparanase in inflammation.Matrix biology : journal of the International Society for Matrix Biology · 2013Review
- Involvement of heparanase in atherosclerosis and other vessel wall pathologies.Matrix biology : journal of the International Society for Matrix Biology · 2013Review
- Heparanase in inflammation and inflammation-associated cancer.The FEBS journal · 2013Review
- Mechanisms of heparanase inhibition by the heparan sulfate mimetic PG545 and three structural analogues.FEBS open bio · 2013Article
- Heparanase enzyme in chronic inflammatory bowel disease and colon cancer.Cellular and molecular life sciences : CMLS · 2012Review
- Significance of heparanase in cancer and inflammation.Cancer microenvironment : official journal of the International Cancer Microenvironment Society · 2012Article
- Development of novel single-stranded nucleic acid aptamers against the pro-angiogenic and metastatic enzyme heparanase (HPSE1).PloS one · 2012Article
- Prognostic value of heparanase expression and cellular localization in oral cancer.Head & neck · 2011Article
- Modulation of GEF-H1 induced signaling by heparanase in brain metastatic melanoma cells.Journal of cellular biochemistry · 2010Article
Corrections and comments
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Authors and funding
20 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mammalian endoglycosidase heparanase (Hpa1) is primarily responsible for cleaving heparan sulphate proteoglycans (HSPGs) present on the basement membrane of cells and its potential for remodelling the extracellular matrix (ECM) could be important in embryonic development and tumour metastasis. Elevated expression of this enzyme has been implicated in various pathological processes including tumour cell proliferation, metastasis, inflammation and angiogenesis. The enzyme therefore represents a potential therapeutic target. Hpa1 protein is initially synthesized as an inactive 65 kDa proenzyme that is then believed to be subsequently activated by proteolytic cleavage to generate an active heterodimer of 8 and 50 kDa polypeptides. By analysis of a series of Hpa1 deletion proteins we confirm that the 8 kDa subunit is essential for enzyme activity. We present here for the first time an insect cell expression system used for the generation of large amounts of recombinant protein of high specific activity. Individual subunits were cloned into baculoviral secretory vectors and co-expressed in insect cells. Active secreted heterodimer protein was recovered from the medium and isolated by a one-step heparin-Sepharose chromatography procedure to give protein of >90% purity. The recombinant enzyme behaved similarly to the native protein with respect to the size of HS fragments liberated on digestion, substrate cleavage specificity and its preference for acidic pH. A significant amount of activity, however, was also detectable at physiological pH values, as measured both by an in vitro assay and by in vivo degradation of cell-bound heparan sulphate.
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