Collagen type I heparin-binding site

Collagen type I is the primary structural component of the extracellular matrix in connective tissues, including skin, bone, and tendons (Ricard-Blum, 2011). The heparin/heparan sulfate proteoglycan (HSPG) binding motif is a specialized region within the collagen triple helix that facilitates the docking of sulfated glycosaminoglycans (San Antonio et al., 1994). This interaction is essential for the proper assembly of collagen fibrils and the regulation of cell-matrix interactions (Sweeney et al., 1998). It also plays a crucial role in the sequestration and presentation of heparin-binding growth factors, such as fibroblast growth factor (FGF) and vascular endothelial growth factor (VEGF), to their respective receptors (UniProt P02452). In pathological conditions like systemic fibrosis and various cancers, the interaction between collagen I and HSPGs is often dysregulated, promoting excessive tissue scarring and tumor cell invasion (Ricard-Blum, 2011). Consequently, this motif is considered a therapeutic target for modulating ECM remodeling and inhibiting pathological signaling pathways. Therapeutic strategies include the use of heparin mimetics, such as Regenerating Agents (RGTAs), or competitive peptides designed to disrupt or mimic these interactions (OTR3, 2023). These interventions aim to restore tissue homeostasis in chronic wounds or prevent the progression of fibrotic diseases.

Other names

Collagen I heparin/HSPG-binding motifHeparin-binding domain of type I collagenCOL1-HBS

Competitive inhibition of the interaction between Collagen I and cell-surface or matrix-associated heparan sulfate proteoglycans, leading to modulated fibrillogenesis and growth factor signaling.