Proteases in cancer drug delivery

Vandooren, Jennifer, Opdenakker, Ghislain, Loadman, Paul M. and Edwards, Dylan R ORCID: https://orcid.org/0000-0002-3292-2064 (2016) Proteases in cancer drug delivery. Advanced Drug Delivery Reviews, 97. pp. 144-155. ISSN 0169-409X

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Abstract

Whereas protease inhibitors have been developed successfully against hypertension and viral infections, they have failed thus far as cancer drugs. With advances in cancer profiling we now better understand that the tumor "degradome" (i.e. the repertoire of proteases and their natural inhibitors and interaction partners) forms a complex network in which specific nodes determine the global outcome of manipulation of the protease web. However, knowing which proteases are active in the tumor micro-environment, we may tackle cancers with the use of Protease-Activated Prodrugs (PAPs). Here we exemplify this concept for metallo-, cysteine and serine proteases. PAPs not only exist as small molecular adducts, containing a cleavable substrate sequence and a latent prodrug, they are presently also manufactured as various types of nanoparticles. Although the emphasis of this review is on PAPs for treatment, it is clear that protease activatable probes and nanoparticles are also powerful tools for imaging purposes, including tumor diagnosis and staging, as well as visualization of tumor imaging during microsurgical resections.

Item Type:	Article
Additional Information:	Copyright © 2016. Published by Elsevier B.V.
Uncontrolled Keywords:	prodrug,metalloproteinase,urokinase,legumain,cathepsin,nanoparticles,sdg 3 - good health and well-being ,/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_being
Faculty \ School:	Faculty of Science > School of Biological Sciences
UEA Research Groups:	Faculty of Science > Research Groups > Cells and Tissues Faculty of Medicine and Health Sciences > Research Groups > Cancer Studies
Depositing User:	Pure Connector
Date Deposited:	02 Mar 2016 17:00
Last Modified:	19 Apr 2023 23:49
URI:	https://ueaeprints.uea.ac.uk/id/eprint/57362
DOI:	10.1016/j.addr.2015.12.020

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