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Processing of macromolecular heparin by heparanase
Feng Gong1, Per Jemth, Martha L Escobar Galvis
1Department of Medical Biochemistry and Microbiology, University of Uppsala, The Biomedical Center, Box 582, SE-751 23 Uppsala, Sweden.
The Journal of Biological Chemistry
|July 3, 2003
Summary
Heparanase, an enzyme that degrades heparan sulfate, also processes serglycin heparin proteoglycans in mouse mast cells. Commercial heparin inhibits this enzyme, suggesting therapeutic potential.
Area of Science:
- Biochemistry
- Cell Biology
- Enzymology
Background:
- Heparanase is an endo-glucuronidase that cleaves heparan sulfate.
- Heparan sulfate proteoglycans are crucial in various biological processes.
Purpose of the Study:
- To investigate the role of heparanase in the processing of serglycin heparin proteoglycan in mouse mast cells.
- To determine if heparanase activity affects the antithrombin-binding sequence in heparin fragments.
Main Methods:
- Incubation of rat skin heparin with recombinant human heparanase.
- Analysis of heparin fragments generated by heparanase.
- Testing commercial heparin as an inhibitor of heparanase.
Main Results:
- Heparanase degrades newly synthesized heparin chains into smaller fragments.
- A fraction of these fragments retains the antithrombin-binding pentasaccharide sequence.
- Commercial heparin effectively inhibits heparanase activity.
Conclusions:
- Heparanase catalyzes the intracellular processing of heparin proteoglycan chains.
- Heparanase cleaves structures distinct from the antithrombin-binding sequence.
- Commercial heparin's inhibitory effect suggests its potential in modulating heparanase activity.