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Cell surface collagen receptors are a heterogeneous group of transmembrane proteins that facilitate communication between cells and the collagenous extracellular matrix (ECM). This group primarily includes the collagen-binding integrins (alpha-1 beta-1, alpha-2 beta-1, alpha-10 beta-1, and alpha-11 beta-1), the discoidin domain receptors (DDR1 and DDR2), and the platelet-specific glycoprotein VI (GPVI) (Leitinger, 2011; Borza & Pozzi, 2014). These receptors are vital for regulating cell adhesion, migration, survival, and differentiation by converting mechanical and chemical signals from the ECM into intracellular responses (Zutter & Edelson, 2007). In pathological states, their dysregulation contributes significantly to cancer progression, particularly through the promotion of epithelial-mesenchymal transition and metastasis, as well as to the development of organ fibrosis and inflammatory conditions like rheumatoid arthritis (Vogel et al., 2006). Pharmacological targeting of these receptors is an active area of research, with strategies ranging from small-molecule kinase inhibitors for DDRs to monoclonal antibodies and soluble decoy receptors for GPVI to prevent thrombosis without significantly increasing bleeding risk (Nieswandt & Watson, 2003).
Inhibition of collagen-induced signal transduction through competitive binding or kinase domain blockade.
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