Review on ITGA4: Potential Drug Target Or Biomarker (G3676)

Target Name: ITGA4

NCBI ID: G3676

Review on ITGA4: Potential Drug Target Or Biomarker

The VLA-4 receptor is a protein that is expressed in various tissues throughout the body, including the immune system, endothelial cells, and epithelial cells. It is a member of the immunoglobulin family and is involved in the regulation of immune responses and cell-cell adhesion. The alpha 4 subunit of the VLA-4 receptor is a protein that has been identified as a potential drug target or biomarker. This article will review the current research on ITGA4 and its potential as a drug target.

structure and function

The alpha 4 subunit of the VLA-4 receptor is a 230-kDa protein that consists of two heavy chains and two light chains. The heavy chains contain four constant (C) regions and one variable (V) region, while the light chains contain one variable (V) region and one constant (C) region. The alpha 4 subunit is involved in the regulation of cell-cell adhesion and in the development of immune responses.

One of the key functions of the alpha 4 subunit is its role in cell-cell adhesion. This is important for the development of tissues such as the placenta, where cells need to stick together to form a barrier that separates the mother and the baby. The alpha 4 subunit helps to regulate the stickiness of cells to each other, allowing them to stick together and form tissues.

Another function of the alpha 4 subunit is its role in the regulation of immune responses. The alpha 4 subunit is involved in the development of T cells, which are a critical part of the immune system. T cells are responsible for recognizing and responding to foreign substances in the body, and the alpha 4 subunit helps to regulate the development of these cells.

Drug targeting

The alpha 4 subunit of the VLA-4 receptor has been identified as a potential drug target. This is because of its role in the regulation of cell-cell adhesion and immune responses. Drugs that target the alpha 4 subunit have been shown to be effective in treating a variety of diseases, including cancer, autoimmune diseases, and skin diseases.

One of the most promising drugs that targets the alpha 4 subunit is a monoclonal antibody called adalimumab (Humira). Adalimumab is a type of antibody that targets the alpha 4 subunit and is used to treat rheumatoid arthritis, an autoimmune disease. In clinical trials, adalimumab has been shown to be effective in reducing the symptoms of rheumatoid arthritis, and it is also being studied as a potential treatment for other autoimmune diseases.

Another drug that targets the alpha 4 subunit is a small molecule called S100, which is used to treat skin diseases such as psoriasis and seborrheic dermatitis. S100 works by inhibiting the activity of a protein called FAK, which is involved in cell-cell adhesion and immune responses.

Conclusion

The alpha 4 subunit of the VLA-4 receptor is a protein that is involved in the regulation of cell-cell adhesion and immune responses. It has been identified as a potential drug target and is being studied as a potential treatment for a variety of diseases, including cancer, autoimmune diseases, and skin diseases. Further research is needed to fully understand the role of the alpha 4 subunit in these diseases and to develop safe and effective drugs that target this protein.

Protein Name: Integrin Subunit Alpha 4

Functions: Integrins alpha-4/beta-1 (VLA-4) and alpha-4/beta-7 are receptors for fibronectin. They recognize one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. They are also receptors for VCAM1. Integrin alpha-4/beta-1 recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-4/beta-7 is also a receptor for MADCAM1. It recognizes the sequence L-D-T in MADCAM1. On activated endothelial cells integrin VLA-4 triggers homotypic aggregation for most VLA-4-positive leukocyte cell lines. It may also participate in cytolytic T-cell interactions with target cells. ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling (PubMed:23125415). ITGA4:ITGB1 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1 (PubMed:18635536, PubMed:25398877)

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