Colagenasa

Colagenasa, or collagenase, is a family of proteolytic enzymes that catalyze the hydrolysis of collagen, the major structural protein of connective tissue. Collagenases participate in normal tissue remodeling, wound healing, and inflammatory processes, and are produced by both humans (as part of the matrix metalloproteinase system) and various microorganisms.

Endogenous collagenases belong to the matrix metalloproteinase (MMP) family, notably MMP-1, MMP-8, and MMP-13. They are secreted as inactive proenzymes and activated in the extracellular space. These mammalian collagenases can cleave native collagen types I, II, and III, contributing to matrix turnover and cell migration during development and repair.

Bacterial collagenases are secreted enzymes produced by organisms such as Clostridium histolyticum and other bacteria. Clinically relevant preparations derived from these enzymes are used for enzymatic debridement of necrotic tissue in chronic wounds. In some medical contexts, collagenase clostridium histolyticum is used as an injectable enzyme to disrupt pathological collagen bundles, such as in Dupuytren's contracture and Peyronie's disease, under controlled conditions.

Mechanistically, the active site of collagenases coordinates a catalytic zinc ion and uses a defined set of histidine residues to hydrolyze peptide bonds within the collagen triple helix or within collagenous domains. Bacterial collagenases often act on native triple-helix collagen, whereas mammalian MMPs can target denatured collagen as well.

Safety and regulation: collagenase-based therapies are used under medical supervision, with caution to avoid damage to healthy tissue and to manage infection risk. Adverse effects can include tissue injury, bleeding, or allergic reactions.