Native fibrillar collagen

Native fibrillar collagen is the primary structural component of the extracellular matrix (ECM), consisting of triple-helical proteins (Types I, II, III, V, and XI) that assemble into supramolecular fibrils to provide tensile strength and tissue architecture (Source: PubMed, PMID: 21432111). It plays a dual role as both a physical scaffold and a biochemical signaling ligand, interacting with receptors like integrins and discoidin domain receptors (DDRs) to influence cell survival, migration, and differentiation (Source: UniProt). In pathological conditions such as organ fibrosis and cancer, the excessive accumulation and cross-linking of these collagens lead to increased tissue stiffness, which impairs organ function and facilitates tumor progression (Source: NIH). Therapeutic interventions target this molecule through enzymatic degradation using collagenases, inhibition of synthesis via TGF-beta pathway modulation, or prevention of cross-linking by targeting enzymes like lysyl oxidase (Source: StatPearls).

Other names

Fibrillar collagenType I collagenType II collagenType III collagenType V collagenType XI collagenInterstitial collagen

The therapeutic targeting of native fibrillar collagen involves several distinct mechanisms: direct enzymatic degradation of the collagen triple helix by collagenases, inhibition of collagen biosynthesis through the modulation of pro-fibrotic growth factors like TGF-beta, and the prevention of fibril stabilization by inhibiting cross-linking enzymes such as lysyl oxidase (LOX) and lysyl oxidase-like 2 (LOXL2) (Source: PubMed, PMID: 30215616; StatPearls).