ADAM10: A promising drug target and biomarker for inflammatory diseases

Target Name: ADAM10

NCBI ID: G102

ADAM10: A promising drug target and biomarker for inflammatory diseases

The protein ADAM10, also known as ADAM10, is a highly conserved protein that is expressed in various cell types of the human body. It is a part of the superfamily A (Adam) family, which includes proteins that are involved in various cellular processes, including cell signaling, adhesion, and migration. One of the unique features of ADAM10 is its potential as a drug target and biomarker for inflammatory diseases. In this article, we will explore the structure, function, and potential clinical applications of ADAM10.

Structure and Function

ADAM10 is a 144 amino acid protein that consists of a single domain containing a catalytic catalytic active site, a transmembrane region, and a cytoplasmic tail. The catalytic active site is the site of the protein's catalytic activity, where it can interact with small molecules, including drugs, toxins, and other substances in the body.

ADAM10 is a potent enzyme that is involved in the regulation of various cellular processes, including cell signaling, adhesion, and migration. One of its most significant functions is the regulation of cell-cell adhesion, which is critical for the maintenance of tissue structure and the development of various diseases.

In addition to its role in cell-cell adhesion, ADAM10 is also involved in the regulation of cell migration, which is critical for the development and progression of various diseases, including cancer. It is known to play a role in the regulation of angiogenesis, the formation of new blood vessels, which can contribute to the development of tumors.

Potential Clinical Applications

ADAM10 has the potential to be a drug target for various inflammatory diseases, including arthritis, asthma, and heart disease. Its involvement in cell-cell adhesion and migration makes it an attractive target for diseases that are characterized by the destruction of tissue structure and the migration of cells to sites of infection or damage.

One of the advantages of ADAM10 as a drug target is its adaptability to various drug classes. Its catalytic active site makes it a potential target for small molecules, including inhibitors of enzymes involved in cell signaling pathways. Additionally, its cytoplasmic tail allows it to be targeted to various cell types within the body.

In addition to its potential as a drug target, ADAM10 also has the potential to be a biomarker for various inflammatory diseases. Its involvement in the regulation of cell-cell adhesion and migration makes it an attractive target for biomarkers that can be used to diagnose and monitor the progression of inflammatory diseases.

Conclusion

ADAM10 is a highly conserved protein that is involved in various cellular processes in the body. Its unique structure and function make it an attractive target for drugs and biomarkers that can be used to treat and diagnose inflammatory diseases. As further research is conducted, it is likely that the potential clinical applications for ADAM10 will continue to grow, making it an important molecule for the development of new treatments for a variety of inflammatory diseases.

Protein Name: ADAM Metallopeptidase Domain 10

Functions: Cleaves the membrane-bound precursor of TNF-alpha at '76-Ala-|-Val-77' to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface (PubMed:20592283). Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP) (PubMed:26686862, PubMed:11786905, PubMed:29224781). Contributes to the normal cleavage of the cellular prion protein (PubMed:11477090). Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity (PubMed:12475894). Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis (By similarity). Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form (PubMed:17557115). Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B (PubMed:19114711, PubMed:21288900). Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3 (By similarity). Mediates the proteolytic cleavage of IL6R and IL11RA, leading to the release of secreted forms of IL6R and IL11RA (PubMed:26876177). Enhances the cleavage of CHL1 by BACE1 (By similarity). Cleaves NRCAM (By similarity). Cleaves TREM2, resulting in shedding of the TREM2 ectodomain (PubMed:24990881). Involved in the development and maturation of glomerular and coronary vasculature (By similarity). During development of the cochlear organ of Corti, promotes pillar cell separation by forming a ternary complex with CADH1 and EPHA4 and cleaving CADH1 at adherens junctions (By similarity). May regulate the EFNA5-EPHA3 signaling (PubMed:16239146)

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