Secreted phosphoprotein 1 (Osteopontin) SVVYGLR neo-epitope (OPN SVVYGLR)

Osteopontin (OPN), also known as Secreted phosphoprotein 1 (SPP1), is a multifunctional matricellular glycoprotein that undergoes proteolytic processing by thrombin to reveal cryptic functional domains. The SVVYGLR neo-epitope is specifically exposed following cleavage at the Arg168-Ser169 peptide bond, a process that occurs during inflammation and tissue injury (Yamamoto et al., 2003, J Clin Invest). This exposed sequence acts as a potent ligand for integrins, particularly alpha-9-beta-1 and alpha-4-beta-1, which are not recognized by the full-length, uncleaved protein (Yokosaki et al., 1999, J Biol Chem). This interaction triggers significant biological responses, including enhanced cell adhesion, migration, and the production of pro-inflammatory cytokines. Pathologically, the SVVYGLR neo-epitope is strongly associated with chronic inflammatory conditions, such as rheumatoid arthritis and liver fibrosis, where it promotes tissue remodeling and disease progression (Uede, 2011, Clin Exp Nephrol). Therapeutic strategies focusing on this target involve the development of monoclonal antibodies, such as M5, that specifically mask the SVVYGLR sequence to block its interaction with integrin receptors without affecting the other physiological functions of full-length osteopontin (Kon et al., 2008, J Biol Chem).

Other names

Thrombin-cleaved osteopontinOPN-NhalfSVVYGLR-exposed osteopontinSecreted phosphoprotein 1 neo-epitopeSPP1 neo-epitope

Monoclonal antibodies bind to the exposed SVVYGLR sequence, preventing its interaction with integrins alpha-9-beta-1 and alpha-4-beta-1, thereby inhibiting pro-inflammatory and pro-fibrotic signaling pathways.