ITGA11

Integrin alpha-11 (ITGA11), also known as CD51, pairs with integrin beta-1 (ITGB1) to form the collagen-binding receptor α11β1. This transmembrane glycoprotein mediates cell-extracellular matrix (ECM) adhesion, primarily interacting with fibrillar collagens (types I, IV, and VI) to regulate cellular mechanotransduction and tissue morphogenesis. Functionally, ITGA11 modulates cell migration, proliferation, and differentiation through activation of focal adhesion kinase (FAK) and SRC kinase signaling. It is critically involved in TGF-β pathway activation, facilitating stromal remodeling and fibrosis progression. Key pathways associated with ITGA11 include the PI3K-AKT and MAPK cascades, which influence ECM organization and cellular responses to mechanical stress.
Dysregulation of ITGA11 is implicated in pathological fibrosis (e.g., pulmonary, hepatic, and cardiac fibrosis) and tumor microenvironment modulation, particularly in promoting cancer-associated fibroblast (CAF) activity in carcinomas and sarcomas. Elevated ITGA11 expression correlates with poor prognosis in triple-negative breast cancer and soft tissue sarcomas. Therapeutic targeting of α11β1 is under preclinical investigation, with monoclonal antibodies and small-molecule inhibitors (e.g., compound E7820 derivatives) showing antifibrotic and antitumor efficacy in models. A phase I trial (NCT04818359) recently evaluated an ITGA11-targeting antibody-drug conjugate in solid tumors, highlighting its emerging role in precision oncology.