Interstitial collagen

Interstitial collagens, primarily types I, II, and III, are the most abundant proteins in the human body and form the structural backbone of the extracellular matrix (ECM) in connective tissues (Ricard-Blum, 2011, Cold Spring Harb Perspect Biol). The "native" form refers to the intact, highly ordered triple-helical structure composed of three polypeptide alpha chains, which provides exceptional tensile strength and resistance to most proteases (Shoulders & Raines, 2009, Annu Rev Biochem). In pathological states such as fibrosis, excessive deposition of these collagens leads to organ scarring and dysfunction, while in conditions like Dupuytren's contracture, localized collagen accumulation causes physical impairment (Karsdal et al., 2017, Adv Drug Deliv Rev). Therapeutic strategies targeting the native triple helix include the use of specialized enzymes like collagenase clostridium histolyticum (Xiaflex), which specifically cleaves the triple helix under physiological conditions to break down excessive fibrous tissue (FDA, Xiaflex Prescribing Information). Additionally, the native collagen structure serves as a critical scaffold for cell signaling via receptors like integrins and discoidin domain receptors (DDRs), making its regulation a key focus in regenerative medicine and oncology (Leitinger, 2011, Int Rev Cell Mol Biol).

Other names

Native interstitial collagen triple helixFibrillar collagenType I collagenType II collagenType III collagenCollagen triple helixNative collagen

Proteolytic degradation of the native triple-helical structure of interstitial collagens (primarily Types I, II, and III) to reduce pathological collagen accumulation or facilitate tissue remodeling; inhibition of synthesis or cross-linking to prevent matrix expansion.