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Matrix metallopeptidase 8 (neutrophil collagenase), also known as MMP8, is a part of the MMP family which are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the enzyme encoded by MMP8 is stored in secondary granules within neutrophils and is activated by autolytic cleavage. MMP8 is a neutral metalloproteinase of the fibrillar collagenase family that also includes MMP-1 and MMP-13. In contrast to the other collagenases, MMP-8 has a very limited tissue distribution, thought to be restricted to neutrophils and chondrocytes.1 Its function is degradation of type I, II and III collagens. MMP-8 is the predominant collagenase present in normal healing wounds and suggests that overexpression and activation of this collagenase may be involved in the pathogenesis of nonhealing chronic ulcers.2 MMP-8 might also be useful in monitoring periodontal disease in diabetes.3