Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases
Top Cited Papers
- 1 June 2007
- journal article
- review article
- Published by Springer Nature in Nature Reviews Drug Discovery
- Vol. 6 (6) , 480-498
- https://doi.org/10.1038/nrd2308
Abstract
Matrix metalloproteinases (MMPs) have outgrown the field of extracellular-matrix biology and have progressed towards being important regulatory molecules in cancer and inflammation. This rise in status was accompanied by the development of various classes of inhibitors. Although clinical trials with synthetic inhibitors for the treatment of cancer were disappointing, recent data indicate that the use of selective inhibitors might lead to new therapies for acute and chronic inflammatory and vascular diseases. In this Review, we compare the major classes of MMP inhibitors and advocate that future drug discovery should be based on crucial insights into the differential roles of specific MMPs in pathophysiology obtained with animal models, including knockout studies.Keywords
This publication has 215 references indexed in Scilit:
- Novel functions of TIMPs in cell signalingCancer and Metastasis Reviews, 2006
- Validating matrix metalloproteinases as drug targets and anti-targets for cancer therapyNature Reviews Cancer, 2006
- Impaired alveolization in mice deficient in membrane-type matrix metalloproteinase 1 (MT1-MMP)Medical Molecular Morphology, 2005
- Membrane‐type 1 matrix metalloproteinase is required for normal alveolar developmentDevelopmental Dynamics, 2005
- Matrix metalloproteinases as modulators of inflammation and innate immunityNature Reviews Immunology, 2004
- The Pathophysiology and Treatment of SepsisNew England Journal of Medicine, 2003
- Inflammation and cancerNature, 2002
- New functions for the matrix metalloproteinases in cancer progressionNature Reviews Cancer, 2002
- Gelatinase B Is Required for Alveolar Bronchiolization after Intratracheal BleomycinThe American Journal of Pathology, 2000
- Selection of a histidine-containing inhibitor of gelatinases through deconvolution of combinatorial tetrapeptide librariesMolecular Diversity, 1997