ADH4: A Potential Drug Target for ADI (G127)

Target Name: ADH4

NCBI ID: G127

ADH4: A Potential Drug Target for ADI

Autosomal dominant inheritance (ADI) is a genetic condition that affects approximately 1 in 2,000 people worldwide. It is characterized by the inheritance of a single gene from an affected parent, which leads to the development of the disease in the affected individual. One of the most well-known genetic disorders associated with ADI is aldehyde reductase (AR) deficiency.

AR is a enzyme that plays a crucial role in the detoxification of xenobiotics, which are harmful substances found in the environment and in our food. Xenobiotics can cause a wide range of health problems, including cancer, neurodegenerative diseases, and reproductive disorders. AR is also involved in the detoxification of environmental toxins, such as polycyclic aromatic hydrocarbons (PAHs) and polycyclic aromatic nitrogen compounds (PANs), which are found in air, water, and soil.

The defect in AR gene has been identified as a key cause of ADI. Individuals with ADI are at increased risk of developing cancer, neurodegenerative diseases, and reproductive disorders due to their increased sensitivity to environmental toxins. Treatment options for ADI have been limited, and the availability of effective drugs and biomarkers has been a significant hindrance.

Recent studies have identified potential drug targets and biomarkers for ADI caused by AR gene defects. One of these drug targets is the enzyme ADH4, which has been shown to be involved in the detoxification of xenobiotics and has been identified as a potential drug target for ADI.

The Role of ADH4 in the detoxification of xenobiotics

Xenobiotics are harmful substances that can cause a wide range of health problems, including cancer, neurodegenerative diseases, and reproductive disorders. These substances can be found in the environment and in our food, and they can be ingested or inhaled.

AR is involved in the detoxification of xenobiotics, and its activity has been shown to reduce the toxicity of these substances. AR helps to convert xenobiotics to less toxic forms, which are then excreted from the body. This process is critical for the detoxification of xenobiotics, and it is a crucial function for maintaining the health and integrity of the body.

The Role of ADH4 in the detoxification of xenobiotics

ADH4 is an enzyme that is involved in the detoxification of xenobiotics. It is a critical enzyme for the detoxification of polycyclic aromatic hydrocarbons (PAHs) and polycyclic aromatic nitrogen compounds (PANs), which are found in air, water, and soil.

Studies have shown that individuals with ADI are at increased risk of developing cancer, neurodegenerative diseases, and reproductive disorders due to their increased sensitivity to environmental toxins. This is because individuals with ADI have defective or reduced levels of the enzyme AR, which is responsible for the detoxification of these toxins.

The activity of ADH4 has been shown to reduce the toxicity of PAHs and PANs, which are believed to be potential causes of cancer, neurodegenerative diseases, and reproductive disorders. By converting these toxins to less toxic forms, ADH4 may help to reduce the risk of these conditions in individuals with ADI.

The Potential of ADH4 as a Drug Target

The identification of potential drug targets and biomarkers for ADI has the potential to lead to the development of new treatments for this disease. One of these drug targets is ADH4, which has been shown to be involved in the detoxification of xenobiotics and has been identified as a potential drug target for ADI.

Studies have shown that individuals with

Protein Name: Alcohol Dehydrogenase 4 (class II), Pi Polypeptide

Functions: Catalyzes the NAD-dependent oxidation of either all-trans-retinol or 9-cis-retinol (PubMed:17279314). Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate (PubMed:16081420). Also catalyzes the reduction of benzoquinones (PubMed:10514444)

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