Glycome Atlas
protein
Also known as HPSE, HPA1, endo-beta-glucuronidase
Plain-language answer
Heparanase is an enzyme that cuts the heparan sulfate sugar chains, the most abundant sugar chains in the glycocalyx. It works like molecular scissors, snipping these long chains into shorter pieces.12
When heparanase becomes active during inflammation or infection, it strips heparan sulfate off the vessel lining. This is a key step in shedding the glycocalyx, which makes vessels leakier and more prone to clotting. It also releases fragments and anchor proteins into the blood that can be measured as signs of vessel damage.1
Technical detail
Heparanase (HPSE) is the mammalian endo-beta-glucuronidase that hydrolyzes heparan sulfate side chains at a limited number of internal sites, releasing biologically active fragments and, in the vasculature, driving degradation and shedding of the heparan sulfate rich endothelial glycocalyx.12
Heparanase is an endoglycosidase that cleaves the beta-1,4 glycosidic bond between glucuronic acid and N-sulfoglucosamine within heparan sulfate chains, acting at a limited number of internal sites rather than fully depolymerizing the chain. This releases heparan sulfate fragments that can carry bound growth factors and other proteins, so cleavage both remodels the matrix and mobilizes signaling molecules.2
In the vessel wall heparanase is one of the principal enzymes, alongside hyaluronidase and matrix metalloproteinases, that degrade the endothelial glycocalyx. By removing heparan sulfate it thins the protective layer, unmasks adhesion molecules, and releases fragments and cleaved core proteins such as syndecan-1 into plasma, a sequence described in sepsis, ischemia-reperfusion, and other inflammatory states.1
Human relevance
Heparanase-mediated cleavage of heparan sulfate is a recognized mechanism of glycocalyx degradation that increases vascular permeability and promotes a pro-inflammatory, pro-coagulant endothelial surface in inflammatory and critical illness states.1
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