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Integrin subunit beta-5 is a transmembrane protein belonging to the integrin family, which forms heterodimeric receptors (most notably with αV, forming integrin αVβ5) that mediate cell adhesion to the extracellular matrix and are involved in cell-surface mediated signaling[2][3][4][5][1]. Integrins are fundamental to processes such as cell migration, proliferation, angiogenesis, and immune regulation. The αVβ5 integrin specifically recognizes the RGD (Arg-Gly-Asp) motif in ECM proteins like vitronectin and fibronectin[2][3]. ITGB5 is overexpressed in several cancers (including colorectal cancer), playing a role in tumor growth, invasion, metastasis, and modulation of the tumor microenvironment, including immune cell infiltration[1]. It is also implicated as a receptor for certain pathogens, such as adenovirus type C[2]. High ITGB5 expression is associated with poor prognosis in colorectal cancer and may function through activation of the Wnt/β-catenin and TGF-β/EMT signaling pathways, contributing to tumor progression and immune evasion[1].
Inhibition of cell-ECM interaction (e.g., blocking adhesion to vitronectin or fibronectin). Modulation of signaling pathways such as Wnt/β-catenin and PI3K/Akt[1]. Interference with angiogenesis and migration by antagonizing integrin function.
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