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Calpain Inhibitors Exhibit Matrix metalloproteinase-2 Inhibitory Activity

Calpain Inhibitors Exhibit Matrix metalloproteinase-2 Inhibitory Activity

Mohammad A M Ali, Alesandra Stepanko, Xiaohu Fan, Andrew Holt, Richard Schulz

Biochem Biophys Res Commun. 2012 Jun 22;423(1):1-5.

PMID: 22575511

Abstract:

Matrix metalloproteinase (MMP)-2 is a zinc-dependent endopeptidase which, alongside its known extracellular actions, plays fundamental roles in oxidative stress-induced injury to the heart. Intracellular cleavage targets of MMP-2 selectively mediating this injury include the sarcomeric proteins troponin I, myosin light chain-1 and titin; some of these are also targeted by calpains. In myocardial ischemia and reperfusion injury, inhibitors of MMP-2 and some calpain inhibitors were shown to improve the recovery of contractile function. We hypothesized that the protective effects of calpain inhibitors may be due in part to their ability to inhibit MMP-2. Four calpain inhibitors (calpain inhibitor III, ALLM, ALLN, and PD-150606) were tested for their ability to inhibit MMP-2 in comparison to the selective MMP inhibitor ONO-4817. At 100 μM, all calpain inhibitors, except ALLM, showed significant inhibition of MMP-2 gelatinolytic activity. When assessed by the troponin I proteolysis assay, both ALLN and PD-150606, but neither ALLM nor calpain inhibitor III (at 20 μM), significantly inhibited MMP-2 activity. Using a fluorogenic MMP substrate peptide OmniMMP in a kinetic assay the rank order of IC(50) values against MMP-2 were: PD-150606

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP179528451	PD 150606		179528-45-1	Price
IAR42416010	MMP Substrate III, Fluorogenic			Price

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