ADAM17: A Snake Venom-like Protease as a Potential Drug Target or Biomarker

Target Name: ADAM17

NCBI ID: G6868

ADAM17: A Snake Venom-like Protease as a Potential Drug Target or Biomarker

Snake venom is a well-known source of biologically active molecules that have been shown to have potential therapeutic applications. One of the most promising of these molecules is snake venom-like proteases (ADAMs), which are a group of enzymes that share a common catalytic mechanism with snake venom serpins. In this article, we will explore the potential implications of ADAM17 as a drug target or biomarker.

The Problem

ADAMs have been identified as potential drug targets due to their unique structure and the various functions they have been shown to play in various biological processes. One of the primary functions of ADAMs is the regulation of protein interactions, which is critical for many cellular processes. This is particularly relevant for diseases that are characterized by misregulated protein interactions, such as cancer, where abnormal protein-protein interactions can lead to the formation of cancer cells.

Additionally, ADAMs have been shown to play important roles in the immune system, where they can help to regulate the production and presentation of antibodies. This is important for diseases where the immune system is impaired, such as autoimmune disorders.

The Potential Role of ADAM17 as a Drug Target

One of the ADAMs that has generated particular interest is ADAM17. This enzyme is characterized by its unique structure, which is similar to that of snake venom serpins. ADAM17 is expressed in many different tissues, including the heart, liver, and pancreas, and has been shown to play a role in a variety of biological processes, including cell signaling, inflammation, and proteassembly.

In addition to its role in cellular signaling, ADAM17 has also been shown to be involved in the regulation of proteasome activity, which is a critical mechanism for the degradation of damaged or unnecessary proteins. This is important for diseases where the proteasome is impaired, such as neurodegenerative disorders.

Furthermore, ADAM17 has been shown to play a role in the regulation of inflammation, which is a critical aspect of many diseases. In addition, ADAM17 has been shown to regulate the production of pro-inflammatory cytokines, which are important for the recruitment of immune cells to the site of inflammation.

The Potential Role of ADAM17 as a Biomarker

In addition to its potential as a drug target, ADAM17 may also be a useful biomarker for some diseases. For example, ADAM17 has been shown to be expressed in a variety of cancer types, including breast, ovarian, and colorectal cancer. This suggests that it may be a useful biomarker for these diseases, as it could be used as a target for new therapies.

Additionally, ADAM17 has been shown to be involved in the regulation of cellular processes that are important for many diseases, such as cancer, autoimmune disorders, and neurodegenerative disorders. This suggests that it may be a useful biomarker for these diseases as well.

Conclusion

In conclusion, ADAM17 is a promising molecule that has a wide range of potential applications, including as a drug target and biomarker. Its unique structure and various functions make it an attractive target for new therapies, and its potential as a biomarker for a variety of diseases adds to its importance. Further research is needed to fully understand the potential of ADAM17 as a drug target and biomarker.

Protein Name: ADAM Metallopeptidase Domain 17

Functions: Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form (PubMed:9034191). 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 p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth factor-alpha, L-selectin, growth hormone receptor, MUC1 and the amyloid precursor protein (PubMed:12441351). Acts as an activator of Notch pathway by mediating cleavage of Notch, generating the membrane-associated intermediate fragment called Notch extracellular truncation (NEXT) (PubMed:24226769). Plays a role in the proteolytic processing of ACE2 (PubMed:24227843). Plays a role in hemostasis through shedding of GP1BA, the platelet glycoprotein Ib alpha chain (By similarity). Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3 (By similarity). Mediates the proteolytic cleavage of IL6R, leading to the release of secreted form of IL6R (PubMed:26876177, PubMed:28060820). Mediates the proteolytic cleavage and shedding of FCGR3A upon NK cell stimulation, a mechanism that allows for increased NK cell motility and detachment from opsonized target cells

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