TRGV1 as A Cancer Drug Target and Biomarker (G6973)

Target Name: TRGV1

NCBI ID: G6973

TRGV1

Other Name(s): TCRGV1 | T cell receptor gamma variable 1 (non-functional) | V1S1P | T-cell receptor, gamma, variable region V1 (pseudogene) | T cell receptor gamma variable 1 pseudogene

TRGV1 as A Cancer Drug Target and Biomarker

TRGV1 (Tumor suppressor gene vitamin A receptor gene 1) is a gene that has been identified as a potential drug target or biomarker for cancer. The Vitamin A receptor is a transmembrane protein that is involved in cell signaling pathways, including the regulation of cell growth, differentiation, and survival. The Vitamin A receptor has also been implicated in the development and progression of many types of cancer, including breast, ovarian, and prostate cancers.

One of the reasons why TRGV1 is considered a potential drug target is because it is a gene that has been shown to be highly expressed in a variety of cancer types, including breast cancer. In fact, studies have shown that TRGV1 is highly expressed in breast tissue, cell lines, and primary breast cancers. This suggests that targeting TRGV1 may be a promising strategy for the development of new treatments for breast cancer.

Another reason why TRGV1 is considered a potential drug target is because it is involved in the regulation of cell signaling pathways that are often disrupted in cancer. The Vitamin A receptor is known to play a role in the regulation of cell growth and differentiation, as well as the regulation of cell survival. Many studies have shown that cancer cells often have altered levels of the Vitamin A receptor, which may contribute to their uncontrolled growth and proliferation. By targeting TRGV1, researchers may be able to disrupt these altered levels of the Vitamin A receptor and potentially inhibit the growth and proliferation of cancer cells.

In addition to its potential as a drug target, TRGV1 is also a potential biomarker for cancer. The Vitamin A receptor has been shown to be involved in the regulation of cell signaling pathways, which may be important for the development and progression of cancer. By measuring the levels of the Vitamin A receptor in cancer cells, researchers may be able to identify those cells that are less likely to respond to traditional cancer treatments. This could help doctors to tailor their treatments to specific types of cancer and to improve the overall effectiveness of cancer treatments.

Targeting TRGV1 may also have potential implications for the treatment of other types of cancer, including cardiovascular disease and neurological disorders. The Vitamin A receptor has been shown to play a role in the regulation of blood vessel growth and differentiation, as well as the regulation of neural cell growth and differentiation. Targeting TRGV1 may be a promising strategy for the development of new treatments for cardiovascular disease and neurological disorders.

Overall, TRGV1 is a gene that has been identified as a potential drug target or biomarker for cancer. Its high expression in breast tissue and its involvement in the regulation of cell signaling pathways make it a promising target for the development of new treatments for breast cancer. Further research is needed to fully understand the potential implications of targeting TRGV1 and to develop effective treatments for cancer.

Protein Name: T Cell Receptor Gamma Variable 1 (non-functional)

Functions: Probable non-functional open reading frame (ORF) of V region of the variable domain of T cell receptor (TR) gamma chain (PubMed:24600447). Non-functional ORF generally cannot participate in the synthesis of a productive T cell receptor (TR) chain due to altered V-(D)-J or switch recombination and/or splicing site (at mRNA level) and/or conserved amino acid change (protein level) (PubMed:9619395). Gamma-delta TRs recognize a variety of self and foreign non-peptide antigens frequently expressed at the epithelial boundaries between the host and external environment, including endogenous lipids presented by MH-like protein CD1D and phosphoantigens presented by butyrophilin-like molecule BTN3A1. Upon antigen recognition induces rapid, innate-like immune responses involved in pathogen clearance and tissue repair (PubMed:23348415, PubMed:28920588). Binding of gamma-delta TR complex to antigen triggers phosphorylation of immunoreceptor tyrosine-based activation motifs (ITAMs) in the CD3 chains by the LCK and FYN kinases, allowing the recruitment, phosphorylation, and activation of ZAP70 that facilitates phosphorylation of the scaffolding proteins LCP2 and LAT. This lead to the formation of a supramolecular signalosome that recruits the phospholipase PLCG1, resulting in calcium mobilization and ERK activation, ultimately leading to T cell expansion and differentiation into effector cells (PubMed:25674089). Gamma-delta TRs are produced through somatic rearrangement of a limited repertoire of variable (V), diversity (D), and joining (J) genes. The potential diversity of gamma-delta TRs is conferred by the unique ability to rearrange (D) genes in tandem and to utilize all three reading frames. The combinatorial diversity is considerably increased by the sequence exonuclease trimming and random nucleotide (N) region additions which occur during the V-(D)-J rearrangements (PubMed:24387714)

The "TRGV1 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about TRGV1 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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