Integrin alpha 2 beta 1 (α2β1) (α2β1)

Integrin alpha 2 beta 1 (α2β1), also known as VLA-2 or the platelet glycoprotein Ia/IIa complex, is a transmembrane heterodimeric receptor that primarily mediates cell adhesion to extracellular matrix components like collagen and laminin [1, 6]. It is widely expressed on platelets, epithelial cells, fibroblasts, and various immune cells, playing a critical role in physiological processes such as hemostasis, wound healing, and T-cell activation [1, 8]. In the context of disease, α2β1 is a key player in the metastatic cascade of several cancers, including breast, prostate, and ovarian cancer, where its expression levels often correlate with invasive potential and patient prognosis [16, 18]. It also serves as a receptor for certain viruses, such as rotavirus and echovirus, facilitating their entry into host cells [6, 13]. Therapeutic targeting of α2β1 is being explored for its potential to inhibit thrombosis and prevent cancer metastasis, with strategies ranging from monoclonal antibodies like vatelizumab to small molecule inhibitors [4, 9]. However, drug development faces challenges due to the receptor's complex, context-dependent roles in tumor progression and the potential for increased bleeding risks [4, 16].

Other names

VLA-2CD49b/CD29Platelet glycoprotein Ia/IIaGPIa/IIaCollagen receptorITGA2/ITGB1Very Late Antigen-2

Antagonism of collagen binding, inhibition of ITGA2 gene expression, and allosteric modulation of the integrin complex.