Integrin alpha-2 beta-1 receptor (null (commonly referred to by its heterodimeric components, "α2β1 integrin" or "VLA-2", but no standardized, single-letter abbreviation dominates usage)[1][2][7][10])

Integrin alpha-2 beta-1 receptor is a **heterodimeric cell surface receptor** comprised of the **integrin alpha-2 subunit (ITGA2, CD49b)** and **beta-1 subunit (ITGB1, CD29)**. It binds primarily to **collagens** and laminin in the extracellular matrix, mediating key processes such as **cell adhesion, migration, platelet aggregation, and signal transduction**[1][2][3][7][10]. Highly expressed on fibroblasts, endothelial, epithelial, platelet, and immune cells, this integrin is crucial for tissue development, immune regulation, angiogenesis, and wound healing[1][10]. Overexpression or dysregulation is implicated in **cancer progression, metastasis, fibrosis, and inflammatory diseases**[1][9]. Integrin alpha-2 beta-1 signals mainly through its interaction with collagen and relies on divalent cations for ligand binding, playing an important therapeutic and biomarker role in modern oncology and immunology research[1][3][7][9][10].

Other names

Integrin α2β1CD49b/CD29VLA-2Platelet membrane glycoprotein Ia-IIaECMR-IIITGA2/ITGB1

Antagonists block collagen binding, inhibiting adhesion, migration, and survival signaling of tumor or fibrotic cells[1][9] Inhibition of integrin signaling reduces metastatic spread, angiogenesis, or tissue fibrosis[9]