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Heparanase processing by lysosomal/endosomal protein preparation.

Esti Cohen¹, Ruth Atzmon, Israel Vlodavsky

¹Cancer and Vascular Biology Research Center, The Bruce Rappaport Faculty of Medicine, Technion, Haifa, Israel.

|April 26, 2005

Summary

Heparanase activation requires specific lysosomal conditions. This enzyme

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Area of Science:

Biochemistry
Cell Biology
Oncology

Background:

Heparanase (HPSE) cleaves heparan sulfate, promoting tumor metastasis and inflammation.
HPSE is synthesized as a latent 65 kDa precursor requiring proteolytic processing for activation.
Previous studies indicated lysosomal proteases and acidic pH are crucial for HPSE processing.

Purpose of the Study:

To investigate the specific cellular compartments and conditions required for heparanase processing and activation.
To elucidate the role of lysosomal fractions in the activation of latent heparanase.

Main Methods:

Cell fractionation to isolate cytoplasmic, lysosomal, and endosomal components.
Incubation of latent heparanase precursor with different cellular fractions.
Analysis of heparanase processing and activation under varying pH conditions.

Main Results:

Incubation of the heparanase precursor with lysosome/endosome fractions, but not cytoplasmic fractions, led to processing and activation.
The water-soluble lysosome/endosome fraction showed no processing activity.
Heparanase processing was detected in the water-insoluble lysosome/endosome membrane fraction and was pH-dependent.

Conclusions:

Heparanase processing and activation are localized to the lysosome/endosome compartment, specifically associated with the membrane fraction.
Acidic pH conditions within the lysosome/endosome are critical for heparanase activation.
These findings provide insights into the mechanism of heparanase activation in the context of cancer metastasis and inflammation.

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