Domains 12 to 16 of tropoelastin promote cell attachment and spreading through interactions with glycosaminoglycan and integrins alphaV and alpha5beta1

Elastin is an extracellular matrix component with key structural and biological roles in elastic tissues. Interactions between resident cells tropoelastin, the monomer of elastin, underpin elastin's regulation cellular processes. However, nature tropoelastin–cell interactions contributions individual tropoelastin domains to these are only partly elucidated. In this study, we identified characterized novel cell-adhesive sites N-terminal region 12 16. We found that interacts αV α5β1 integrin receptors, which mediate cell attachment spreading. A peptide sequence from within region, spanning 14 mid-domain 16, binds heparan sulfate through electrostatic lysine residues induces conformational ordering peptide. propose 14–16 direct initial cell-surface glycosaminoglycans, followed by integrin-promoted spreading on 12–16 tropoelastin. These findings advance our mechanistic understanding elastin biology, potential enhance tissue regenerative outcomes elastin-based materials.