ITGB1 adenovirus

Integrin β1 (ITGB1) is a widely expressed transmembrane receptor subunit that pairs with various α-integrins to form heterodimeric receptors, mediating cell-extracellular matrix (ECM) and cell-cell interactions. These integrin heterodimers (e.g., α5β1, α3β1, α2β1, α6β1, etc.) recognize a variety of ECM ligands, such as fibronectin, collagen, laminin, and vitronectin, thereby coordinating cell adhesion, migration, polarity, survival, proliferation, and differentiation in various tissues. Through interactions with FAK/Src, PI3K–AKT, Rho GTPase, and MAPK pathways, ITGB1 integrates mechanical and chemical signals to regulate cell fate and tissue homeostasis. Functionally, ITGB1 is crucial for developmental morphogenesis, wound healing, angiogenesis, neuronal pathfinding, immune cell trafficking, and maintenance of the stem cell niche. Dysregulation of ITGB1 expression or signaling leads to various diseases, including cancer progression and metastasis, fibrotic remodeling, cardiovascular dysfunction, musculoskeletal degeneration, and certain neurodevelopmental disorders.

The ITGB1 adenovirus vector, based on human adenovirus type 5 (Ad5 dE1/E3, E1/E3 gene deleted) and driven by a CMV promoter for ITGB1 transgene expression, provides a powerful, replication-deficient vector for transient, high-level ITGB1 overexpression in various mammalian cells. This virus is widely used for gain-of-function studies without the need for permanent genomic integration, allowing researchers to investigate how elevated β1 integrin levels affect cell adhesion dynamics, focal adhesion assembly, cytoskeletal organization, and downstream signaling networks. In disease-relevant models, the ITGB1 adenovirus can be used to study epithelial-mesenchymal transition, collective cell migration, invasion through the ECM, angiogenic behavior of endothelial cells, fibroblast activation and matrix deposition, cardiomyocyte survival and remodeling signaling, and neurite extension and synapse stabilization.