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Heparanase expression upregulates platelet adhesion activity and thrombogenicity
Hao Cui1, Ying-Xia Tan1,2, Cecilia Österholm3,4
1Department of Medical Biochemistry and Microbiology, SciLifeLab Uppsala, The Biomedical Center, University of Uppsala, Husargatan, Uppsala, Sweden.
Oncotarget
|April 30, 2016
Summary
Platelet heparanase, an enzyme that breaks down heparan sulfate, enhances platelet adhesion and thrombosis. This suggests a role for platelet heparanase in the hyper-thrombotic conditions associated with metastatic cancer.
Area of Science:
- Biochemistry
- Hematology
- Oncology
Background:
- Heparanase is an enzyme that cleaves heparan sulfate (HS) and heparin.
- It is normally expressed at low levels but upregulated in pathological conditions like cancer and inflammation.
- Human platelets have high levels of heparanase, but its function in platelets is unknown.
Purpose of the Study:
- To investigate the functional roles of heparanase in platelets.
- To compare the properties of platelets with high (Hpa-tg) versus low (Ctr) heparanase levels.
Main Methods:
- Comparison of platelet properties between Hpa-tg and Ctr mice.
- Assessment of platelet adhesion and thrombotic activity using a carotid thrombosis model.
- Analysis of heparanase and CD62P (P-selectin) expression upon platelet activation.
Main Results:
- Hpa-tg platelets showed significantly stronger adhesion compared to Ctr platelets.
- Hpa-tg platelets exhibited higher thrombotic activity in vivo.
- Platelet activation led to upregulated expression of both heparanase and CD62P in mouse and human platelets.
Conclusions:
- Platelet heparanase enhances platelet adhesion and thrombotic activity.
- The findings suggest a contribution of platelet heparanase to hyper-thrombotic conditions in metastatic cancer.
- Heparanase may play a role in the link between platelets and tumor metastasis.
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