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Author Spotlight: High-Sensitivity Tissue Factor Activity Assay for Plasma Diagnosis
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Tissue factor-heparanase complex: intracellular nonhemostatic effects.

Shorook Ghanem1, Anat Keren-Politansky2, Victoria Kaplan1

  • 1Thrombosis and Hemostasis Unit, The Rappaport Faculty of Medicine, Rambam Health Care Campus, Technion, Haifa, Israel.

Research and Practice in Thrombosis and Haemostasis
|September 28, 2023
PubMed
Summary
This summary is machine-generated.

The heparanase procoagulant domain promotes cancer progression by interacting with tissue factor (TF), influencing cell proliferation and heparanase release. This interaction highlights a link between hemostasis and cancer.

Keywords:
heparanaseneoplastic processesreceptortissue factortissue factor pathway inhibitor

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • Heparanase is implicated in angiogenesis, cancer progression, and inflammation.
  • Heparanase forms a complex with tissue factor (TF) via its procoagulant domain, enhancing the hemostatic system.

Purpose of the Study:

  • To investigate the nonhemostatic roles of the heparanase procoagulant domain.
  • To explore the interaction between heparanase and tissue factor in cellular processes.

Main Methods:

  • Utilized peptides derived from the heparanase procoagulant domain (peptides 16 and 16AC).
  • Employed XTT proliferation assays, western blot analysis, and immunostaining in vitro.
  • Investigated effects in human tumor cell lines (U87, T47D, MCF-7) and endothelial cells.
  • Used a mouse wound-healing model to assess in vivo effects.
  • Examined cells overexpressing full-length TF or TF devoid of its cytoplasmic domain.

Main Results:

  • Procoagulant peptides increased proliferation and heparanase release.
  • Upregulation of heparanase, TF, tissue factor pathway inhibitor (TFPI), and TFPI-2 was observed.
  • A TFPI-2-derived peptide inhibited the heparanase procoagulant domain-TF complex, reversing effects.
  • Thrombin mimicked some effects, with heparanase procoagulant domain mediating proliferation.
  • In vivo, procoagulant peptides increased heparanase, TF, TFPI, and TFPI-2 levels in healing skin wounds.
  • Intracellular signaling via TF was mediated by its procoagulant domain.

Conclusions:

  • The heparanase procoagulant domain induces nonhemostatic effects through TF.
  • TF acts as a receptor for heparanase, underscoring the connection between hemostasis and cancer progression.