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J Biol Chem, Vol. 273, Issue 30, 18770-18777, July 24, 1998
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From the Heparan sulfate proteoglycans, attached to cell
surfaces or in the extracellular matrix, interact with a multitude of
proteins via their heparan sulfate side chains. Degradation of these
chains by limited (endoglycosidic) heparanase cleavage is believed to affect a variety of biological processes. Although the occurrence of
heparanase activity in mammalian tissues has been recognized for many
years, the molecular characteristics and substrate recognition properties of the enzyme(s) have remained elusive.
In the present study, the substrate specificity and cleavage site of
heparanase from human hepatoma and platelets were investigated. Both
enzyme preparations were found to cleave the single
Department of Medical Biochemistry and
Microbiology, Uppsala University, The Biomedical Center, Box 575, S-751
23 Uppsala, Sweden and the ¶ Department of Oncology, Hadassah
University Hospital, P.O. Box 12000, Jerusalem 91120, Israel
-D-glucuronidic linkage of a heparin
octasaccharide. A capsular polysaccharide from Escherichia
coli K5, with the same (-GlcUA1,4-GlcNAc
1,4-)n structure as the unmodified backbone of heparan sulfate, resisted heparanase degradation in its native state as well as after chemical N-deacetylation/N-sulfation or partial
enzymatic C-5 epimerization of -D-GlcUA to
-L-IdceA. By contrast, a chemically
O-sulfated (but still N-acetylated) K5
derivative was susceptible to heparanase cleavage.
O-Sulfate groups, but not N-sulfate or IdceA
residues, thus are essential for substrate recognition by the
heparanase(s). In particular, selective O-desulfation of
the heparin octasaccharide implicated a 2-O-sulfate group
on a hexuronic acid residue located two monosaccharide units from the
cleavage site, toward the reducing end.
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