Disease relevance of G6pd2

• In contrast, mortality after cecal ligation and puncture-induced sepsis was similar in G6PD-deficient and wild-type animals either in saline-resuscitated or antibiotic-treated animals [1].
• MEASUREMENTS AND MAIN RESULTS: Lipopolysaccharide in vivo (lipopolysaccharide from Escherichia coli, 10-35 mg/kg body weight intraperitoneally) resulted in greater interleukin-1beta, interleukin-6, and interleukin-10 levels in serum and peritoneal lavage in G6PD-deficient mice compared with wild type [1].
• Individuals with a G-6-PD deficiency have long been known to be at increased risk to experience acute hemolysis following exposure to elevated levels of certain oxidant drugs and industrial chemicals [2].
• This differential susceptibility to sodium chlorite toxicity between the high and low G-6-PD mouse strains suggests that further research designed to validate the efficacy of this mouse model as a predictor of the human situation is warranted [2].

High impact information on G6pd2

• Mouse embryonic stem (ES) glucose-6-phosphate (G6P) dehydrogenase-deleted cells ( G6pd delta), obtained by transient Cre recombinase expression in a G6pd -loxed cell line, are unable to produce G6P dehydrogenase (G6PD) protein (EC 1.1.1.42) [3].
• Prevailing doses of lipopolysaccharide in vivo increased mortality in G6PD-deficient animals (40-70%) as compared with wild type (5-40%) [1].
• Splenic and blood phagocytes from septic G6PD-deficient and wild-type animals displayed attenuated ex vivo lipopolysaccharide responsiveness [1].
• OBJECTIVE: Glucose-6-phosphate dehydrogenase (G6PD) deficiency is a common human genetic polymorphism [1].
• G6pd-2 does not contain introns and appears to represent a retroposed gene [4].

Chemical compound and disease context of G6pd2

• Our results indicate that G6PD-deficient, genetically slow acetylators, having high microsomal activity, would be most susceptible to Promizole- or DDS-induced hemolysis, compared to other metabolic phenotypes [5].

Biological context of G6pd2

• G6pd-2 is one of the very few known expressed retroposons encoding a functional protein, and the presence of this gene is probably related to X chromosome inactivation during spermatogenesis [4].
• Several of the hybrids contained a complete red kangaroo X chromosome and expressed the kangaroo form of the enzymes HPRT, G6PD, and PGKA [6].

Anatomical context of G6pd2

• Under the same conditions, G6PD tetramers were also found in extracts of spermatids and spermatozoa, indicating the presence of G6pd-2-encoded isoenzyme in these cell types [4].
• We found that in the presence of induced (high hydroxylase activity) microsomes, thiazolsulfone (Promizole) or DDS in unacetylated form caused the highest level of GSH depletion in G6PD-deficient red cells [5].
• The very low levels of activity of G6PD in tammar oocytes may be due to transcriptional, translational or metabolic differences compared with the mouse [7].

Associations of G6pd2 with chemical compounds

• Preliminary results indicate that the mouse strain with low G-6-PD activity is markedly more susceptible to sodium chlorite than mice of the high G-6-PD strain [2].

Analytical, diagnostic and therapeutic context of G6pd2

• Effects of environmental oxidant stressors on individuals with a G-6-PD deficiency with particular reference to an animal model [2].

References