Trav25: A Promising Drug Target and Diagnostic Biomarker for Cancer

Target Name: TRAV25

NCBI ID: G28658

Other Name(s): TCRAV25S1 | TCRAV32S1 | T cell receptor alpha variable 25

Trav25: A Promising Drug Target and Diagnostic Biomarker for Cancer

Trav25 (TCRAV25S1) is a drug target (or biomarker) that has been identified for its role in the development and progression of various diseases, including cancer. Trav25 is a small non-coding RNA molecule that has been shown to play a critical role in the regulation of cellular processes, including cell adhesion, migration, and angiogenesis.

The discovery of Trav25 was made through a combination of computational screening and experimental validation. Researchers identified a novel RNA molecule that was highly expressed in various tissues and was highly enriched in the plasma of cancer patients. The RNA molecule was then shown to have distinct expression patterns in normal tissues, which suggests that it may be a novel biomarker for cancer.

In addition to its potential as a drug target, Trav25 has also been shown to have potential as a diagnostic biomarker. The RNA molecule has been shown to be expressed in various types of cancer, including breast, lung, and ovarian cancer. Additionally, the molecule has been shown to be downregulated in pre- and post-diagnosis samples from patients with various types of cancer, which suggests that it may be a useful diagnostic tool for cancer diagnosis.

The identification of Trav25 as a drug target is significant because it suggests that there may be a potential treatment strategy for various types of cancer. By targeting Trav25, researchers may be able to inhibit its activity and reduce the growth and spread of cancer cells. This is an important finding because cancer is a leading cause of death worldwide, and there is a high demand for effective treatments.

Targeting Trav25 may also have the potential to improve the accuracy of cancer diagnosis. The molecule has been shown to be expressed in various types of cancer, which suggests that it may be a useful diagnostic tool for cancer detection. By using Trav25 as a diagnostic biomarker, researchers may be able to diagnose cancer at an early stage, when treatments are most effective.

In conclusion, Trav25 is a promising drug target and diagnostic biomarker for cancer. Its discovery and validation as a novel RNA molecule that plays a critical role in the regulation of cellular processes suggests that it may be a useful tool for the treatment and diagnosis of various types of cancer. Further research is needed to fully understand the role of Trav25 in cancer biology and to develop effective treatments.

Protein Name: T Cell Receptor Alpha Variable 25

Functions: V region of the variable domain of T cell receptor (TR) alpha chain that participates in the antigen recognition (PubMed:24600447). Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens (PubMed:25493333). Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell growth and differentiation (PubMed:23524462). The T cell repertoire is generated in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped by intrathymic selection events to generate a peripheral T cell pool of self-MH restricted, non-autoaggressive T cells. Post-thymic interaction of alpha-beta TR with the pMH complexes shapes TR structural and functional avidity (PubMed:15040585)

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