PRAME: A Potential Drug Target and Biomarker for Melanoma (G23532)

Target Name: PRAME

NCBI ID: G23532

PRAME

PRAME: A Potential Drug Target and Biomarker for Melanoma

Melanoma is a rare and aggressive form of skin cancer that is characterized by the rapid and uncontrolled growth of skin cells that produce melanin. It is a leading cause of skin cancer death worldwide, and its incidence is increasing, with a rising trend observed in recent years. Despite advances in surgical treatments, the prognosis for melanoma remains poor, with a five-year survival rate of only around 15%.

The search for new treatments and biomarkers for melanoma has led to the exploration of alternative targets, such as the Preferentially Expressed Antigen (PRAME) in cancer cells. PRAME is a transmembrane protein that is expressed in various tissues and is involved in cell signaling processes, including cell adhesion, migration, and invasion.

Recent studies have suggested that PRAME may be a potential drug target for melanoma. By inhibiting the activity of PRAME, researchers have observed a potential mechanism for targeting melanoma cells that could lead to a more effective treatment.

One of the key advantages of PRAME as a drug target is its expressedness in various tissues, including skin, hair, and other organs. This makes it a potential biomarker for monitoring disease progression and response to treatment. Additionally, PRAME has been shown to be involved in several cellular processes that are relevant to cancer progression, including cell adhesion, migration, and invasion. This suggests that targeting PRAME may be a more effective way to inhibit the growth and spread of melanoma cells than targeting individual genes.

Another potential advantage of PRAME is its role in cell signaling processes. PRAME has been shown to be involved in several signaling pathways that are relevant to cancer progression, including the TGF-β pathway. This pathway is involved in cell signaling processes that promote cell growth, differentiation, and survival, and is a potential target for anti-cancer drugs.

In addition to its potential role in cell signaling processes, PRAME has also been shown to be involved in the regulation of cell adhesion. Adhesion is the process by which cells stick together to form tissues and organs, and is a critical process for tissue development and maintenance.

Research has shown that PRAME is involved in the regulation of cell adhesion, and that inhibiting its activity may be a potential way to treat melanoma. One of the ways that PRAME achieves this is by promoting the formation of tight junctions, which are a type of cell-cell adhesion structure that helps to maintain tissue integrity and prevent cells from migrating.

Another potential mechanism by which PRAME may contribute to the development and progression of melanoma is its role in cell migration. Cell migration is the process by which cells move from one location to another in the body, and is a critical process for tissue growth and development.

Research has shown that PRAME is involved in the regulation of cell migration, and that inhibiting its activity may be a potential way to treat melanoma. One of the ways that PRAME achieves this is by promoting the formation of filopodia, which are small, hair-like structures that form on the tips of cells and help to guide cell migration.

In conclusion, PRAME is a potential drug target and biomarker for melanoma. Its expressedness in various tissues and its involvement in cell signaling processes, cell adhesion, and cell migration make it a promising target for anti-cancer drugs. Further research is needed to fully understand the role of PRAME in melanoma and to develop effective treatments.

Protein Name: PRAME Nuclear Receptor Transcriptional Regulator

Functions: Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex, which mediates ubiquitination of target proteins, leading to their degradation (PubMed:21822215, PubMed:26138980). The CRL2(PRAME) complex mediates ubiquitination and degradation of truncated MSRB1/SEPX1 selenoproteins produced by failed UGA/Sec decoding (PubMed:26138980). In the nucleus, the CRL2(PRAME) complex is recruited to epigenetically and transcriptionally active promoter regions bound by nuclear transcription factor Y (NFY) and probably plays a role in chromstin regulation (PubMed:21822215). Functions as a transcriptional repressor, inhibiting the signaling of retinoic acid through the retinoic acid receptors RARA, RARB and RARG: prevents retinoic acid-induced cell proliferation arrest, differentiation and apoptosis (PubMed:16179254)

The "PRAME 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 PRAME 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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