Heparanase (HPSE) cleaves heparan sulfate from its proteoglycan (lysosome)

Stable Identifier
R-HSA-1667005
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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Heparanase (HPSE) is an endoglycosidase that cleaves heparan sulfate (HS) from its HS proteoglycan (HSPG) (Toyoshima & Nakajima 1999). The formation of a heterodimer of 8kDa and 50kDa subunits cleaved from the 65kDa form is required for enzyme activity (Levy-Adam et al. 2003) and this proteolytic cleavage occurs in the lysosome (Goldshmidt et al. 2002). Acidic conditions within the lysosome optimises HPSE activity.

Literature References
PubMed ID Title Journal Year
12927802 Heterodimer formation is essential for heparanase enzymatic activity

Levy-Adam, F, Miao, HQ, Heinrikson, RL, Vlodavsky, I, Ilan, N

Biochem Biophys Res Commun 2003
12441129 Human heparanase is localized within lysosomes in a stable form

Goldshmidt, O, Nadav, L, Aingorn, H, Irit, C, Feinstein, N, Ilan, N, Zamir, E, Geiger, B, Vlodavsky, I, Katz, BZ

Exp Cell Res 2002
10446189 Human heparanase. Purification, characterization, cloning, and expression

Toyoshima, M, Nakajima, M

J Biol Chem 1999
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
heparanase activity of HPSE dimer [lysosomal lumen]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created