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Heparanase: A Challenging Cancer Drug Target.

Deirdre R Coombe1, Neha S Gandhi2

  • 1School of Pharmacy and Biomedical Sciences, Curtin Health Innovation Research Institute, Faculty of Health Sciences, Curtin University, Perth, WA, Australia.

Frontiers in Oncology
|December 19, 2019
PubMed
Summary

Heparanase is a promising cancer target, but its complex functions and challenging drug development hinder clinical success. Further research is needed to overcome these obstacles for effective anti-heparanse therapies.

Keywords:
cancerdrug discoveryheparan sulfateheparanaseheparanase-2heparintumor progression

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Research

Background:

  • Heparanase is highly expressed in many cancers, correlating with poor prognosis.
  • Despite being a target for two decades, no anti-heparanase therapy has reached clinical trials.
  • Heparanase possesses diverse enzymatic and non-enzymatic functions both intracellularly and extracellularly.

Purpose of the Study:

  • To re-examine heparanase functions in light of structural data.
  • To discuss the roles of heparanase variants and related proteins in drug efficacy.
  • To evaluate current anti-heparanase drug development strategies.

Main Methods:

  • Review of existing literature and structural data of heparanase.
  • Analysis of heparanase structure-function relationships.
  • Discussion of enzymatic versus non-enzymatic roles in cancer progression.

Main Results:

  • Crystal structure knowledge aids in understanding heparanase functions and designing inhibitors.
  • Heparanase-related proteins (e.g., T5, heparanase-2) influence anti-heparanase drug efficacy.
  • Current drugs primarily target enzymatic activity, which may not be sufficient.

Conclusions:

  • Heparanase is a valid but challenging cancer drug target.
  • The multifaceted nature of heparanase necessitates a broader therapeutic approach.
  • Further investigation into non-enzymatic functions and novel drug strategies is crucial.