Inhibition of MMPs and ADAM/ADAMTS

Binding and inhibition of protease enzymes, including MMPs, by a superabsorbent dressing in vitro.

OBJECTIVE To demonstrate the binding and inactivation action of a superabsorbent dressing on proteolytic enzymes MMP-2, MMP-9 and collagenase using an established methodology. METHOD An in vitro assay of MMP binding and collagenase inactivation has been conducted using the superabsorbent wound dressing (Eclypse; Advancis Medical UK). Dressings in this category, and other absorbents, have been...

MMPs and ADAMTSs: functional studies.

Members of the MMP (matrix metalloproteinase) and ADAMTS (a disintegrin and metalloproteinase with thrombospondin type I motifs) families of enzymes are capable of cleaving a diverse array of cellular, extracellular and extracellular matrix substrates, including collagens and procollagens, proteoglycans, cytokines and cytokine ligands, chemokines, elastin and von Willebrand factor, thereby modu...

Substrate Specificity of MMPs

TIMPs, MMPs and cardiovascular disease.

The matrix metalloproteinases (MMPs) are a family of proteolytic enzymes that cleave the extracellular matrix and have been shown to be regulated by a class of proteins called the tissue inhibitors of metalloproteinases (TIMPs). Several studies have shown that extracellular matrix degradation by MMPs, specifically MMP-9, is involved in the pathogenesis of a wide spectrum of cardiovascular disor...

2 Substrate Specificity of MMPs