collagenase

Collagenase is an enzyme that catalyzes the hydrolysis of collagen, the main structural protein of the extracellular matrix. It belongs to the matrix metalloproteinase (MMP) family and functions as a zinc-dependent endopeptidase. Collagenases preferentially cleave native fibrillar collagens (types I, II, and III) within the triple helix, producing partially degraded fragments that can be further degraded by other proteases. Through controlled degradation of collagen, collagenases participate in normal tissue remodeling, wound healing, and in various pathological processes such as inflammation, fibrosis, and cancer invasion. Their activity is balanced by tissue inhibitors of metalloproteinases (TIMPs) and tight regulation within tissues.

Natural sources include endogenous human collagenases produced by cells in connective tissue (for example MMP-1, MMP-8, and MMP-13) and bacterial collagenases, notably from Clostridium histolyticum. Bacterial forms are often used clinically and in research; they are zinc-dependent metalloproteases that degrade collagen in intact fibrils and can be employed as therapeutic enzymes under controlled conditions. In humans, collagenases contribute to normal matrix remodeling but can contribute to tissue destruction when overactive, as seen in arthritic joints, invasive tumors, and fibrotic diseases.

Clinical applications include topical collagenase preparations for enzymatic debridement of necrotic tissue in wounds, and collagenase clostridium histolyticum (CCH), approved for Dupuytren's contracture and Peyronie's disease, where it enzymatically dissolves pathogenic collagen cords. In research, collagenases are used to dissociate tissues for cell isolation and to study extracellular matrix biology. Potential risks include local tissue damage, inflammation, allergic reactions, and immune responses; treatment requires careful dosing and supervision.