proMMP8

proMMP-8, also called the neutrophil collagenase zymogen, is the latent form of matrix metalloproteinase-8 (MMP-8). MMP-8 is a zinc-dependent endopeptidase produced mainly by neutrophils and stored in azurophil granules, released during inflammation. As a proenzyme, it contains a prodomain that keeps the enzyme inactive by blocking the catalytic site; proteolytic removal of the prodomain activates the enzyme.

Activated MMP-8 degrades extracellular matrix components, especially type I, II, and III collagen, and participates in tissue remodeling, wound healing, and inflammatory tissue destruction. Activation can be mediated by other proteases or autocatalysis under inflammatory conditions. The enzyme's activity is tightly regulated by tissue inhibitors of metalloproteinases (TIMPs). It is zinc- and calcium-dependent for catalysis.

In humans, proMMP-8 is encoded by the MMP8 gene. It is expressed by neutrophils and detectable in body fluids such as saliva and gingival crevicular fluid, with increased levels in inflamed tissues.

Because of its role in collagen degradation during inflammation, proMMP-8 and its active form are studied as biomarkers of periodontal disease and other inflammatory conditions. Measurement of proMMP-8 in saliva or oral fluids can aid assessment of disease activity and response to treatment.