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Review
. 2001 Aug;108(3):341-7.
doi: 10.1172/JCI13662.

Molecular properties and involvement of heparanase in cancer metastasis and angiogenesis

I Vlodavsky  1 , Y Friedmann
Affiliations
Review

Molecular properties and involvement of heparanase in cancer metastasis and angiogenesis

I Vlodavsky et al. J Clin Invest. 2001 Aug.
No abstract available

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Figures

Figure 1
Figure 1
Heparanase-mediated release of bioactive molecules sequestered in the ECM. Heparanase cleaves HSPGs (arrows) and releases a variety of physiologically and pathologically important molecules. Inset shows the cleavage site within the antithrombin-binding heparin 3H-octasaccharide. The actual antithrombin-binding sequence corresponds to sugar units 2–6 (within brackets). X in sugar unit 4 represents hydrogen or SO–3. Adapted from Pikas et al. (17).
Figure 2
Figure 2
Heparanase-mediated extravasation of blood-borne cells. Heparanase expressed by tumor cells (left) and neutrophils (right) promotes cell invasion between adjacent vascular ECs and through their underlying basal lamina (BL) into the ECM. Platelets may facilitate extravasation of blood-borne cells through binding to the invading cells, and activation and release of their own heparanase enzyme. Left: Scanning electron micrographs showing invasion of T-lymphoma cells, in the absence (top) or presence (bottom) of platelets, through a monolayer of cultured vascular ECs.
Figure 3
Figure 3
Proposed involvement of heparanase in angiogenesis. Heparanase promotes: EC migration and degradation of the subendothelial basal lamina (BL) and ECM; release of active HS-bound bFGF and VEGF; and release of HS degradation fragments that promote FGF-receptor (FGFR) binding, dimerization, and signaling (arrows), inducing EC migration and proliferation.
See this image and copyright information in PMC

References

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