Matrix metalloproteinase inhibition. From the Jurassic to the third millennium.
A brief historical introduction to the matrix metalloproteinase (MMP) field, which began in 1962, is followed by an overview of the inhibition of these proteases by natural inhibitors such as alpha 2 macroglobulin and the TIMPs (tissue inhibitors of metalloproteinases) and by synthetic inhibitors, which are largely chelating agents. The latter include thiol, alkylcarbonyl, phosponamidate and hydroxamate compounds, as well as the tetracyclines. A review of the most recent progress concludes with prognostications as to where the field may be going next.
Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, Florida 33101, USA. fwoessne@mednet.med.miami.edu
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JF
Woessner
D000818:Animals; D002614:Chelating Agents / Q000494:pharmacology; D006801:Humans; D008666:Metalloendopeptidases / Q000037:antagonists & inhibitors*; D011480:Protease Inhibitors / Q000138:chemical synthesis / Q000494:pharmacology*; D019714:Tissue Inhibitor of Metalloproteinases / Q000378:metabolism* / Q000494:pharmacology; D014407:Tumor Cells, Cultured
D002614:Chelating Agents; D011480:Protease Inhibitors; D019714:Tissue Inhibitor of Metalloproteinases; D008666:Metalloendopeptidases