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Related Experiment Video

Updated: Jun 20, 2026

Using a GFP-tagged TMEM184A Construct for Confirmation of Heparin Receptor Identity

Using a GFP-tagged TMEM184A Construct for Confirmation of Heparin Receptor Identity

Published on: February 17, 2017

Heparanase: busy at the cell surface.

Liat Fux¹, Neta Ilan, Ralph D Sanderson

¹Cancer and Vascular Biology Research Center, Bruce Rappaport Faculty of Medicine, Technion, P. O. Box 9649, Haifa 31096, Israel.

Trends in Biochemical Sciences

|September 8, 2009

Summary

This summary is machine-generated.

Heparanase promotes tumor progression by remodeling the extracellular matrix and augmenting signaling pathways. Inhibiting heparanase activity with modified heparin shows promise for anti-cancer therapies.

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Using a GFP-tagged TMEM184A Construct for Confirmation of Heparin Receptor Identity

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In vivo Liver Endocytosis Followed by Purification of Liver Cells by Liver Perfusion

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Published on: November 10, 2011

Area of Science:

Biochemistry
Oncology
Molecular Biology

Background:

Heparanase plays a key role in extracellular matrix remodeling, facilitating tumor cell invasion.
Heparanase activity is linked to signaling cascades that enhance tumor progression and gene transcription.
Heparanase regulates syndecan clustering, shedding, and mitogen binding, expanding its functional role.

Purpose of the Study:

To investigate the multifaceted roles of heparanase in tumor progression.
To explore the potential of inhibiting heparanase activity for cancer therapy.

Main Methods:

Analysis of heparanase's enzymatic and non-enzymatic functions.
Evaluation of modified glycol-split heparin as a heparanase inhibitor.
Assessment of tumor xenograft progression in response to anti-heparanase therapy.

Main Results:

Heparanase activity contributes to extracellular matrix structural changes and tumor cell invasion.
A novel protein domain at the heparanase C-terminus mediates functions independent of enzyme activity.
Modified glycol-split heparin significantly inhibited the progression of myeloma and carcinoma tumor xenografts.

Conclusions:

Heparanase is a critical mediator of aggressive tumor progression through diverse mechanisms.
Targeting heparanase activity with inhibitors like modified heparin represents a viable therapeutic strategy for cancer treatment.