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Integrin alpha 1 beta 1 (VLA-1) is a heterodimeric cell surface receptor composed of the alpha 1 (ITGA1) and beta 1 (ITGB1) subunits, which functions as a primary receptor for collagens, including Type I and Type IV, and laminin. It is expressed on various cell types, including mesenchymal cells, vascular smooth muscle cells, and activated T cells, where it mediates cell-matrix adhesion and regulates biological processes such as cell proliferation, migration, and the immune response. In the context of disease, the interaction between Type I collagen and integrin alpha 1 beta 1 is implicated in the pathogenesis of chronic inflammatory conditions like rheumatoid arthritis, as well as in fibrosis and tumor angiogenesis. Therapeutic strategies targeting this receptor, such as the monoclonal antibody SAN-300, aim to disrupt its binding to collagen to reduce leukocyte recruitment and tissue inflammation. However, because integrin alpha 1 beta 1 also acts as a negative regulator of the epidermal growth factor receptor (EGFR), its inhibition may potentially enhance EGFR signaling, presenting a theoretical risk for promoting tumor growth in certain environments.
Inhibition of the interaction between the integrin alpha 1 subunit and collagen ligands, thereby blocking downstream signaling pathways such as FAK and MAPK and preventing leukocyte recruitment and tissue retention.
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