All bodily cells contain the enzyme glucose-6-phosphate dehydrogenase (G6PD), which is located in the cytoplasm. It is a maintenance enzyme that is essential for preventing cellular damage caused by ROS (reactive oxygen species). By offering substrates to stop oxidative damage, it achieves this.

Due to their function in the transport of oxygen and the incapacity to replenish cellular components as adult cells, red cells are especially prone to ROS. In periods of heightened Ros generation, inherited G6PD deficits can cause severe hemolytic anemia.

Stress, exposure to foods like fava beans that are strong in oxidative chemicals, or specific drugs could all contribute to this. In individuals with G6PD deficiency, anti-malarial medications, in particular, show a substantial correlation with the development of hemolytic anemia.

The drugs listed below are more frequently prescribed in the U.s and have been documented to cause hemolytic crises in people with G6PD deficit; nevertheless, the Italian G6PD Deficit Association has released a more extensive list of drugs to avoid.

In patients with G6PD deficiency, common drugs that should be avoided or taken with caution include:

• Chloramphenicol
• Colchicine
• Acetaminophen
• Glyburide
• Diaminodiphenyl sulfone
• L-Dopa
• Streptomycin
• Primaquine
• Methylene blue
• Sulfacetamide
• Sulfapyridine
• Sulfanilamide
• Sulfaguanidine
• Sulfisoxazole
• Sulfacytine
• Sulfamethoxazole
• Sulfadiazine
• Sulfisoxazole
• Tripelennamine
• Isoniazid
• Vitamin K

The most prevalent human enzyme deficiency, known as G6PD, affects around 400 million individuals worldwide. Because of X-linked heredity, men would be more frequently impacted than women. Areas that are tropical, as well as subtropical, are where it is most common.

It’s interesting to note that there is evidence that G6PD deficit protects against simple instances of malaria but not serious conditions. Malaria and G6PD deficiency have protective mechanism that is currently being researched.

Individuals of African, Asian, or Mediterranean heritage are more likely to have a G6PD deficit than those of other ethnicities, possibly because of the condition’s potential to protect against malaria.

The pentose phosphate route employs glucose-6-phosphate to transform nicotinamide adenine dinucleotide phosphate (NADP) into its reduced form, NADPH. The rate-limiting initial step of this system uses G6PD as a catalyst.

When oxygen-free electrons attack the intracellular structures of RBC cells, NADPH plays a crucial protective role.

This is accomplished by acting as a substrate for the glutathione reductase enzyme. RBCs have a lower capacity for repair after they reach maturity. Thus, reduced glutathione can be employed to avoid injury to cellular components and turn hydrogen peroxide into water.

The G6PD enzyme is encoded by the Gd gene. Since this gene is on the long arm of chromosome X, it is inherited exclusively through chromosome X. A lack of G6PD may result from mutations that alter the structure of the protein and, as a result, decrease its activity or the quantity of enzyme generated.

There are now 186 known human G6PD alterations, the majority of which are single-nucleotide point mutations. None of the human mutation types that affect G6PD result in its total inactivation since doing so would be fatal to an embryo.

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https://www.ncbi.nlm.nih.gov/books/NBK470315/