counteract oxidative damage and protect mouse erythrocytes. Regulation can also occur through genetic pathways. The isoform, G6PDH, is regulated by transcription and posttranscription factors. Moreover, G6PD is one of a number of glycolytic enzymes activated by the transcription factor hypoxia-inducible factor 1 (HIF1). Clinical significance G6PD is remarkable for its genetic diversity. Many variants of G6PD, mostly produced from missense mutations, have been described with wide-ranging levels of enzyme activity and associated clinical symptoms. Two transcript variants encoding different isoforms have been found for this gene. Glucose-6-phosphate dehydrogenase deficiency is very common worldwide, and causes acute hemolytic anemia in the presence of simple infection, ingestion of fava beans, or reaction with certain medicines, antibiotics, antipyretics, and antimalarials. Cell growth and proliferation are affected by G6PD. Pharmacologically ablating G6PD has been shown to overcome cross-tolerance of breast cancer cells to anthracyclines. G6PD inhibitors are under investigation to treat cancers and other conditions. In vitro cell proliferation assay indicates that G6PD inhibitors, DHEA (dehydroepiandrosterone) and ANAD (6-aminonicotinamide), effectively decrease the growth of AML cell lines. G6PD is hypomethylated at K403 in acute myeloid leukemia, SIRT2 activates G6PD to enhance NADPH production and promote leukemia cell proliferation. See also Glucose-6-phosphate dehydrogenase deficiency Genetic resistance to malaria References Further reading External links - G6PD Deficiency Website ATSDR - G6PD Deficiency EC 1.1.1 NADPH-dependent enzymes Enzymes of known structure