Fibrillar collagen

Fibrillar collagens are a major subgroup of the collagen family, including types I, II, III, V, and XI, which assemble into highly organized, triple-helical fibrils that provide essential tensile strength and structural support to the extracellular matrix (ECM) [1][2]. These proteins are fundamental to the integrity of skin, bone, tendons, and cartilage, and they play a critical role in cell signaling and tissue development [2][3]. Pathologically, the dysregulated accumulation of fibrillar collagen is a hallmark of fibrotic diseases affecting the liver, lungs, and heart, where it leads to organ stiffness and failure [4]. In oncology, the dense collagenous stroma (desmoplasia) can act as a physical barrier to drug delivery and promote tumor progression [5]. Therapeutic interventions target fibrillar collagen through various approaches, including direct enzymatic degradation (e.g., collagenase for Dupuytren's contracture), inhibition of synthesis via TGF-beta pathways, or blocking the cross-linking enzymes like lysyl oxidase that stabilize the collagen network [4][6]. Monitoring collagen turnover through biomarkers like pro-collagen propeptides is essential for assessing disease progression and treatment efficacy in fibrotic disorders [7].

Other names

Fibril-forming collagenInterstitial collagenGroup I collagen

Direct enzymatic degradation of collagen fibrils, inhibition of collagen synthesis via TGF-beta pathway modulation, or inhibition of lysyl oxidase (LOX/LOXL2) to prevent covalent cross-linking and stabilization of the collagen matrix.