Abstract
Integrins refer to heterodimers consisting of subunits α and β. They serve as receptors on cell membranes and interact with extracellular ligands to mediate intracellular molecular signals. One of the least-studied members of the integrin family is integrin-α9β1, which is widely distributed in various human tissues and organs. Integrin-α9β1 regulates the physiological state of cells through a variety of complex signaling pathways to participate in the specific pathological processes of some intractable diseases. In recent years, an increasing amount of research has focused on the role of α9β1 in the molecular mechanisms of different refractory diseases and its promising potential as a therapeutic target. Accordingly, this review introduces and summarizes recent research related to integrin-α9β1, describes the synergistic functions of α9β1 and its corresponding ligands in cancer, autoimmune diseases, nerve injury and thrombosis and, more importantly, highlights the potential of α9β1 as a distinctive target for the treatment of these intractable diseases.
Highlights
Integrins are specific transmembrane proteins that function as receptors on the surface of cell membranes
It binds to a diversity of ligands in the extracellular matrix, like the a-disintegrin and metalloprotease (ADAM) family, elastic microfibril interface-located protein1 (EMILIN1), vascular endothelial growth factor (VEGF), the extra domain A (EDA) of fibronectin, tenascin-C (TNC), osteopontin (OPN), vascular cell adhesion molecule-1 (VCAM-1) and C-motif-ligand-1 (XCL1)/lymphotactin [21,22,23,24,25]
The antibody of the LRSKSR SFQVSDEQY sequence shows an ability to diminish the pathological features of arthritis. These results indicate that matrix metalloproteinase (MMP)-3 and MMP-7 promote the development of rheumatoid arthritis (RA) via interaction between OPN and integrin-a9b1 [133]
Summary
Integrins are specific transmembrane proteins that function as receptors on the surface of cell membranes. Integrin-a9b1 plays an important role in cell adhesion and migration, but more and more research is showing that it has roles far beyond that It binds to a diversity of ligands in the extracellular matrix, like the a-disintegrin and metalloprotease (ADAM) family, elastic microfibril interface-located protein (EMILIN1), vascular endothelial growth factor (VEGF), the extra domain A (EDA) of fibronectin, tenascin-C (TNC), osteopontin (OPN), vascular cell adhesion molecule-1 (VCAM-1) and C-motif-ligand-1 (XCL1)/lymphotactin [21,22,23,24,25]. The interaction between these proteins and integrin-a9b1 is vital for organismal growth and development and cellular physiological activities (Table 1). The expression of miR-125b is clearly decreased in primary melanoma, and even
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