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Chemical Biology for Understanding Matrix Metalloproteinase Function
Author(s) -
Knapinska Anna,
Fields Gregg B.
Publication year - 2012
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201200298
Subject(s) - proteases , matrix metalloproteinase , wound healing , chemical biology , metalloproteinase , biology , function (biology) , protease , microbiology and biotechnology , in vivo , embryonic stem cell , matrix metalloproteinase inhibitor , cancer , neuroscience , cancer research , immunology , enzyme , biochemistry , genetics , gene
The matrix metalloproteinase (MMP) family has long been associated with normal physiological processes such as embryonic implantation, tissue remodeling, organ development, and wound healing, as well as multiple aspects of cancer initiation and progression, osteoarthritis, inflammatory and vascular diseases, and neurodegenerative diseases. The development of chemically designed MMP probes has advanced our understanding of the roles of MMPs in disease in addition to shedding considerable light on the mechanisms of MMP action. The first generation of protease‐activated agents has demonstrated proof of principle as well as providing impetus for in vivo applications. One common problem has been a lack of agent stability at nontargeted tissues and organs due to activation by multiple proteases. The present review considers how chemical biology has impacted the progress made in understanding the roles of MMPs in disease and the basic mechanisms of MMP action.