Abstract
Proteases have long been associated with cancer progression because of their ability to degrade extracellular matrices, which facilitates invasion and metastasis. However, recent studies have shown that these enzymes target a diversity of substrates and favour all steps of tumour evolution. Unexpectedly, the post-trial studies have also revealed proteases with tumour-suppressive effects. These effects are associated with more than 30 different enzymes that belong to three distinct protease classes. What are the clinical implications of these findings?
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Review
MeSH terms
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ADAM Proteins / metabolism
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Animals
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Antineoplastic Agents / administration & dosage
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Caspases / metabolism
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Cathepsins / metabolism
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Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / metabolism
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Disease Models, Animal
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Disease Progression
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Drug Delivery Systems / methods
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GPI-Linked Proteins
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Humans
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Kallikreins / metabolism
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Matrix Metalloproteinases / metabolism
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Membrane Proteins / metabolism
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Mice
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Neoplasms / drug therapy
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Neoplasms / enzymology*
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Neprilysin / metabolism
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Peptide Hydrolases / classification
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Peptide Hydrolases / metabolism*
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Serine Endopeptidases / metabolism
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Ubiquitin / metabolism
Substances
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Antineoplastic Agents
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GPI-Linked Proteins
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Membrane Proteins
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Ubiquitin
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Cathepsins
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Peptide Hydrolases
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Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
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Kallikreins
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PRSS21 protein, human
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Serine Endopeptidases
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prostasin
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Caspases
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ADAM Proteins
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Matrix Metalloproteinases
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Neprilysin