TRPA-1: A Protein Target for Drug Development (G8989)

Target Name: TRPA1

NCBI ID: G8989

TRPA-1: A Protein Target for Drug Development

TRPA-1 (Transformation-Sensitive Protein p120) is a protein that is expressed in various tissues and cells throughout the body. It is a key regulator of cell growth and division, and is involved in the development and progression of many diseases, including cancer. In recent years, researchers have become increasingly interested in TRPA-1 as a potential drug target or biomarker, due to its unique biology and its ability to interact with a variety of signaling pathways.

TRPA-1 was first identified in the late 1990s as a protein that was expressed in many tissues, including brain, heart, and muscle. It was found to be involved in the regulation of cell growth, apoptosis (programmed cell death), and DNA damage repair. Since then, researchers have conducted extensive studies to understand the role of TRPA-1 in these processes.

One of the key functions of TRPA-1 is its ability to interact with various signaling pathways. For example, TRPA-1 has been shown to interact with the PI3K/Akt signaling pathway, which is involved in the regulation of cell growth and survival. This interaction suggests that TRPA-1 may be a useful target for drugs that are designed to inhibit the activity of this pathway.

Another important function of TRPA-1 is its role in the regulation of cell apoptosis. Apoptosis is a natural process that is involved in the elimination of damaged or dysfunctional cells. In diseases such as cancer, however, the regulation of apoptosis can become aberrant, leading to the development of cancer cells. TRPA-1 has been shown to play a key role in the regulation of apoptosis, by ensuring that it is properly activated and regulated.

In addition to its role in apoptosis, TRPA-1 is also involved in the regulation of cell division. It has been shown to interact with the p21-p50TG-p21F1/p21G120 cell cycle kinase, which is involved in the regulation of cell division. This interaction suggests that TRPA-1 may be a useful target for drugs that are designed to inhibit the activity of this kinase.

TRPA-1 has also been shown to be involved in the regulation of inflammation. It has been found to interact with various signaling pathways, including the NF-kappa-B signaling pathway, which is involved in the regulation of inflammation. This interaction suggests that TRPA-1 may be a useful target for drugs that are designed to inhibit the activity of this pathway.

In conclusion, TRPA-1 is a protein that is involved in a variety of processes in the body, including cell growth, apoptosis, and inflammation. Its unique biology and its ability to interact with various signaling pathways make it an attractive target for drugs that are designed to inhibit its activity. As research continues to advance, it will be important to determine the full extent of TRPA-1's role in these processes, as well as its potential as a drug target or biomarker.

Protein Name: Transient Receptor Potential Cation Channel Subfamily A Member 1

Functions: Receptor-activated non-selective cation channel involved in pain detection and possibly also in cold perception, oxygen concentration perception, cough, itch, and inner ear function (PubMed:21873995, PubMed:23199233, PubMed:25389312, PubMed:25855297). Shows 8-fold preference for divalent over monovalent cations (PubMed:31447178). Has a central role in the pain response to endogenous inflammatory mediators and to a diverse array of irritants, such as allylthiocyanate (AITC) from mustard oil or wasabi, cinnamaldehyde, diallyl disulfide (DADS) from garlic, and acrolein, an irritant from tears gas and vehicle exhaust fumes (PubMed:25389312, PubMed:27241698, PubMed:30878828, PubMed:20547126). Acts also as an ionotropic cannabinoid receptor by being activated by delta(9)-tetrahydrocannabinol (THC), the psychoactive component of marijuana (PubMed:25389312). Is activated by a large variety of structurally unrelated electrophilic and non-electrophilic chemical compounds. Electrophilic ligands activate TRPA1 by interacting with critical N-terminal Cys residues in a covalent manner, whereas mechanisms of non-electrophilic ligands are not well determined. May be a component for the mechanosensitive transduction channel of hair cells in inner ear, thereby participating in the perception of sounds. Probably operated by a phosphatidylinositol second messenger system (By similarity)

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