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Matrix metalloproteinases (MMPs) are zinc-dependent endopeptidases that are specialised to degrade extracellular protein assemblies which provide cells with much of the structural and biochemical apparatus. The members of this structure-related family of proteases, comprising more than 25 members, differ from each other, particularly in their location in the cell and the specificity of substrate proteolysis. The gelatinases, referred to as MMP-2 and MMP-9, are the main contributors to many cardiovascular diseases.1 For example, by degrading extracellular proteins such as collagen and elastin, MMP-2 triggers proliferation and migration of many cell types, thus favouring conditions ranging from angiogenesis and embryogenesis to hypertension, aortic aneurysm, inflammation and cancer.2
To protect MMPs from abnormal autoproteolysis or uncontrolled tissue degradation, MMPs are synthesised with an autoinhibitory propeptide which binds its cysteine thiol to the zinc ion in the catalytic domain. As soon as MMPs are secreted from cells the cysteine–zinc bond is disrupted by other proteases or by oxidising compounds, setting free the catalytic domain.1 Tissue inhibitors of MMPs (TIMPs) are the main inhibitors of MMP activity and bind to the catalytic site of MMPs non-covalently in a 1:1 stoichiometric ratio. Among four TIMPs, TIMP-2 binds preferentially to …
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