Integrin subunit beta 7 (ITGB7) (ITGB7)

Integrin subunit beta 7 (ITGB7) is a critical cell-surface protein that pairs with either alpha 4 or alpha E subunits to form the alpha-4-beta-7 and alpha-E-beta-7 integrin heterodimers, respectively (UniProt P26010). The alpha-4-beta-7 complex is the primary 'gut-homing' receptor, mediating the migration of lymphocytes to the intestinal mucosa by binding to mucosal vascular addressin cell adhesion molecule 1 (MAdCAM-1) (Gorfu et al., 2009, PubMed). The alpha-E-beta-7 complex, also known as CD103, facilitates the retention of intraepithelial lymphocytes within the intestinal mucosa through its interaction with E-cadherin (Ley et al., 2016, PubMed). The 'activated conformation' refers to the high-affinity, extended-open state of the integrin that is triggered during inflammatory signaling, allowing for stable cell adhesion and subsequent transmigration into tissues (Sun et al., 2014, PubMed). Dysregulation of ITGB7-mediated trafficking is a central driver of inflammatory bowel diseases (IBD), such as ulcerative colitis and Crohn's disease (Lamb et al., 2018, PubMed). Therapeutic agents like vedolizumab and etrolizumab target these pathways to selectively inhibit gut-specific inflammation while minimizing systemic immunosuppression (Wyant et al., 2016, PubMed).

Other names

Integrin beta-7ITGB7Gut-homing receptor beta subunitLy-69Integrin beta-P

Selective antagonism of the integrin beta 7 subunit or its heterodimers (alpha-4-beta-7 and alpha-E-beta-7), which prevents the binding of leukocytes to ligands like MAdCAM-1 and E-cadherin, thereby inhibiting lymphocyte recruitment and retention in the gastrointestinal tract (DrugBank DB09033; Ley et al., 2016, PubMed).