EGLN3: A Potential Drug Target and Biomarker for Hypoxia-Inducible Factor Prolyl Hydroxylase 3

Target Name: EGLN3

NCBI ID: G112399

EGLN3

EGLN3: A Potential Drug Target and Biomarker for Hypoxia-Inducible Factor Prolyl Hydroxylase 3

Hypoxia-inducible factor prolyl hydroxylase 3 (EGLN3) is a protein that plays a crucial role in the regulation of cellular processes, including cell growth, apoptosis, and inflammation. EGLN3 is a key regulator of the 50kDa prolyl hydroxylase complex, which is involved in the hydrolysis of prolyl hydroxyl groups on target proteins and is essential for protein stability, localization, and interactions. EGLN3 is also involved in the regulation of cellular oxygenation and has been implicated in the pathogenesis of various diseases, including cancer, neurodegenerative diseases, and systemic inflammatory disorders.

Despite its significant implications in cellular processes, EGLN3 has not yet been identified as a potential drug target or biomarker. This lack of recognition has important implications for the development of new therapeutic strategies for these diseases.

Targeting EGLN3: The Potential for Drug Targets

The identification of potential drug targets is an important step in the development of new therapeutic strategies for diseases. EGLN3 is a protein that has not yet been targeted by drugs, making it an attractive target for therapeutic intervention.

One potential approach to targeting EGLN3 is to exploit its role in the regulation of cellular oxygenation. EGLN3 has been shown to play a key role in the regulation of cellular oxygenation and has been implicated in the pathogenesis of diseases that are characterized by chronic hypoxia, such as cancer, neurodegenerative diseases, and systemic inflammatory disorders.

In particular, EGLN3 has been shown to play a crucial role in the regulation of aerobic cellular oxygenation, which is critical for the survival of cancer cells. EGLN3 has been shown to enhance the production of reactive oxygen species (ROS) in cancer cells, which can lead to the formation of reactive oxygen species-derived damage (ROS-DAM) and contribute to the development of cancer.

Another potential approach to targeting EGLN3 is to exploit its role in the regulation of protein stability and localization. EGLN3 has been shown to play a key role in the regulation of protein stability and localization, including the regulation of protein stability and localization in the endoplasmic reticulum (ER) and the cytosol.

In particular, EGLN3 has been shown to play a crucial role in the regulation of protein stability and localization in the ER, where it is involved in the regulation of protein stability and localization in the ER. This suggests that targeting EGLN3 may be an effective way to treat diseases characterized by the accumulation of misfolded or mislocalized proteins, such as neurodegenerative diseases.

Exploring EGLN3 as a Biomarker: The Potential for EGLN3 as a Biomarker

EGLN3 is also an attractive biomarker for the diagnosis and prognosis of various diseases. The regulation of EGLN3 is implicated in the development and progression of diseases, including cancer, neurodegenerative diseases, and systemic inflammatory disorders.

For example, EGLN3 has been shown to be involved in the regulation of cancer cell growth and has been implicated in the development of various cancers. In particular, EGLN3 has been shown to play a key role in the regulation of cell cycle progression and has been shown to enhance the production of pro-inflammatory cytokines in cancer cells.

In addition, EGLN3 has also been shown to be involved in the regulation of neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease. EGLN3 has

Protein Name: Egl-9 Family Hypoxia Inducible Factor 3

Functions: Prolyl hydroxylase that mediates hydroxylation of proline residues in target proteins, such as PKM, TELO2, ATF4 and HIF1A (PubMed:19584355, PubMed:21620138, PubMed:21483450, PubMed:22797300, PubMed:20978507, PubMed:21575608). Target proteins are preferentially recognized via a LXXLAP motif. Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins (PubMed:11595184, PubMed:12181324). Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A (PubMed:11595184, PubMed:12181324). Also hydroxylates HIF2A (PubMed:11595184, PubMed:12181324). Has a preference for the CODD site for both HIF1A and HIF2A (PubMed:11595184, PubMed:12181324). Hydroxylation on the NODD site by EGLN3 appears to require prior hydroxylation on the CODD site (PubMed:11595184, PubMed:12181324). Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex (PubMed:11595184, PubMed:12181324). Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes (PubMed:11595184, PubMed:12181324). ELGN3 is the most important isozyme in limiting physiological activation of HIFs (particularly HIF2A) in hypoxia. Also hydroxylates PKM in hypoxia, limiting glycolysis (PubMed:21620138, PubMed:21483450). Under normoxia, hydroxylates and regulates the stability of ADRB2 (PubMed:19584355). Regulator of cardiomyocyte and neuronal apoptosis. In cardiomyocytes, inhibits the anti-apoptotic effect of BCL2 by disrupting the BAX-BCL2 complex (PubMed:20849813). In neurons, has a NGF-induced proapoptotic effect, probably through regulating CASP3 activity (PubMed:16098468). Also essential for hypoxic regulation of neutrophilic inflammation (PubMed:21317538). Plays a crucial role in DNA damage response (DDR) by hydroxylating TELO2, promoting its interaction with ATR which is required for activation of the ATR/CHK1/p53 pathway (PubMed:22797300). Also mediates hydroxylation of ATF4, leading to decreased protein stability of ATF4 (Probable)

The "EGLN3 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 EGLN3 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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