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Fibrillar type I and type III collagens are the primary structural proteins of the extracellular matrix, providing tensile strength and structural integrity to connective tissues (UniProt P02452, P02461). Type I collagen is the most abundant protein in the human body, forming thick fibers in tendons and ligaments, while Type III collagen is often found in more elastic tissues and is highly expressed during the early phases of wound healing and fibrotic remodeling (NCBI Gene ID: 1277, 1281). In pathological conditions such as Dupuytren's contracture and Peyronie's disease, an abnormal accumulation of these collagens leads to the formation of dense, inelastic cords or plaques that cause significant physical deformity and loss of function (StatPearls, Dupuytren Contracture). These structures are the direct therapeutic target for Collagenase clostridium histolyticum, a drug composed of two distinct collagenases that enzymatically digest the collagen triple helix (Hurst et al., 2009, NEJM). This localized proteolysis weakens the pathological tissue, allowing for mechanical disruption and restoration of normal anatomy without the need for invasive surgery (FDA, Xiaflex Prescribing Information).
Collagenase clostridium histolyticum (CCH) consists of two collagenases, AUX-I and AUX-II, which work synergistically to cleave the triple-helical structure of type I and type III collagen into smaller fragments, thereby dissolving the pathological cord or plaque (FDA, Xiaflex Label; Hurst et al., 2009, NEJM).
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