Integrin alpha 2
Integrin alpha 2 (CD49b) is a protein that in humans is encoded by the ITGA2 gene. This protein is a member of the integrin family, which are cell surface receptors involved in cell adhesion and recognition in a variety of processes including embryogenesis, hemostasis, tissue repair, immune response, and metastatic diffusion of tumor cells.
Structure[edit | edit source]
Integrin alpha 2 forms a heterodimer with a beta integrin and primarily interacts with collagen. This interaction is crucial for the adhesion of platelets and other cell types to the extracellular matrix. The alpha 2 beta 1 integrin is recognized for its role in cell adhesion and cellular signaling, mediating interactions between cells and the extracellular matrix (ECM).
Function[edit | edit source]
The primary function of integrin alpha 2 is to facilitate cell-cell and cell-matrix interactions. This integrin is involved in various cellular processes, including the regulation of cell migration, cellular differentiation, and apoptosis. It plays a significant role in the immune system, aiding in the immune response by promoting leukocyte adhesion and migration. In the context of hemostasis, integrin alpha 2 on platelets binds to collagen, initiating platelet adhesion and aggregation at sites of vascular injury.
Clinical Significance[edit | edit source]
Alterations in the expression or function of integrin alpha 2 have been associated with several diseases. Its role in cell adhesion and migration makes it a critical factor in cancer progression and metastasis. Increased expression of integrin alpha 2 has been observed in various tumors, suggesting its potential as a marker for cancer diagnosis and prognosis. Furthermore, due to its involvement in platelet adhesion, integrin alpha 2 has been studied in relation to thrombosis and other cardiovascular diseases.
Research[edit | edit source]
Research on integrin alpha 2 has focused on its potential as a therapeutic target. Inhibitors of integrin alpha 2 have been explored for their ability to prevent tumor metastasis and to treat other conditions related to abnormal cell adhesion and migration. Additionally, understanding the mechanisms regulating its expression and function may lead to new therapeutic strategies for diseases associated with integrin dysfunction.
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Contributors: Prab R. Tumpati, MD