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Integrin alpha E (CD103), historically identified in research as the OX62 antigen, is a transmembrane glycoprotein and a member of the integrin family that functions as a cell-surface receptor for E-cadherin [PMID: 8104117]. It typically forms a heterodimeric complex with the integrin beta 7 subunit, and this alphaEbeta7 complex is predominantly expressed on intraepithelial lymphocytes (IELs), regulatory T cells, and specific subsets of dendritic cells [UniProt: P38570]. The primary biological role of CD103 is to facilitate the adhesion and retention of lymphocytes within mucosal tissues, particularly the intestinal epithelium and the skin, by binding to E-cadherin on epithelial cells [PubMed: 12514309]. In clinical contexts, CD103 is heavily involved in the pathogenesis of inflammatory bowel disease (IBD), as its interaction promotes the accumulation of pro-inflammatory T cells in the gut lining. It also serves as a crucial biomarker in oncology; the presence of CD103+ tumor-infiltrating lymphocytes is often correlated with enhanced anti-tumor cytotoxic activity and improved survival rates in various solid tumors [PubMed: 28552977]. Therapeutic efforts targeting this pathway, most notably with the dual alpha4beta7/alphaEbeta7 inhibitor etrolizumab, aim to reduce pathogenic lymphocyte recruitment to mucosal surfaces to treat chronic inflammatory conditions [DrugBank: DB09104]. Safety concerns associated with inhibiting this target include a potentially increased risk of mucosal infections and altered regional immune surveillance [ClinicalTrials.gov: NCT01193348].
Selective inhibition of the alphaEbeta7 integrin complex to block the interaction between mucosal lymphocytes and E-cadherin on epithelial cells, thereby preventing tissue-specific inflammation and lymphocyte retention.
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