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Integrin alpha-11 beta-1 (α11β1) is a heterodimeric transmembrane receptor that serves as a major collagen-binding protein primarily expressed on fibroblasts and mesenchymal stem cells (Popova et al., 2007, PMID: 17635995). It consists of the alpha-11 (ITGA11) and beta-1 (ITGB1) subunits and plays a pivotal role in cell-matrix interactions, specifically mediating fibroblast migration and the differentiation of fibroblasts into contractile myofibroblasts (Zeltz et al., 2014, PMID: 24463607). In pathological conditions, α11β1 is highly upregulated in the stroma of various solid tumors, where it acts as a marker for cancer-associated fibroblasts (CAFs) and contributes to tumor growth and metastasis by remodeling the extracellular matrix (Navab et al., 2016, PMID: 26928460). Additionally, it is a key driver in fibrotic diseases, such as idiopathic pulmonary fibrosis and cardiac fibrosis, where its expression correlates with excessive collagen deposition and tissue stiffening (Bansal et al., 2017, PMID: 28811309). While no drugs targeting α11β1 are currently FDA-approved, research is actively focused on developing monoclonal antibodies and small molecule inhibitors to disrupt its interaction with collagen, thereby targeting the tumor microenvironment and fibrotic progression (Zeltz & Gullberg, 2016, PMID: 27106088).
Antagonism of collagen binding and inhibition of myofibroblast activation and extracellular matrix remodeling (Zeltz & Gullberg, 2016).
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