Disease relevance of G6PD

• Median corpuscular fragility showed a positive correlation with the severity of parasitemia (r=0.81, P<0.0005) and a negative correlation with the activities of GSH-Px (r=-0.78, P<0.0001), SOD (r=-0.71, P<0.0005), catalase (r=-0.53, P<0.018) and G6PD (r=-0.58, P<0.0005) [1].
• Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides is a reliable internal standard for radiation-inactivation studies of membranes in the frozen state [2].
• The glucose-6-phosphate dehydrogenase from Neisseria gonorrhoeae was inhibited by long-chain fatty acid acyl-coenzyme A derivatives [3].
• 0. Kinetic and other characteristics of the enzyme are presented, and the possible role of glucose-6-phosphate dehydrogenase as a target for fatty acid toxicity in gonococci, mediated in the form of the acyl-coenzyme A derivatives, is discussed [3].
• However, when activity per cell was adjusted for cell size, subcutaneous depots had greater fatty acid synthae, glucose 6-phosphate dehydrogenase, and NADP-malate dehydrogenase activities than omental and perirenal, indicating that other factors such as nutrient supply may restrict hypertrophy of carcass adipocytes [4].

High impact information on G6PD

• In this study reported here the activity of glucose-6-phosphate dehydrogenase, the first and rate-limiting enzyme of the oxidative pentose phosphate shunt, was very low in the human heart and was of the same order of magnitude in the myocardium of various animal species [5].
• A RBC glucose-6-phosphate dehydrogenase level should be obtained before administration of primaquine [6].
• These results support the involvement of both an Fc and a lectin-like macrophage receptor in the recognition and phagocytosis of Phz-oxidized and G6PD-deficient RBCs and suggest opsonization as a possible physiologic process for the removal of severe damaged RBCs [7].
• G6PD-deficient RBCs were recognized and phagocytosed by murine macrophages without preexposure to oxidants in vitro (mean of 19 RBCs/100 macrophages) [7].
• Phagocytosis of phenylhydrazine oxidized and G-6-PD-deficient red blood cells: the role of cell-bound immunoglobulins [7].

Chemical compound and disease context of G6PD

• By contrast, the target size of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides was found to be essentially invariant when frozen in a variety of buffers and in the presence or absence of either cryoprotectant (sucrose or glycerol) or different membrane preparations [2].

Biological context of G6PD

• Equal expression of X-linked genes such as G6PD and PGK in females and males and the initiation of X-chromosome inactivation are critically dependent on the expression of the X-inactive specific transcript (Xist) [8].
• Sperm motility as well as viability was significantly less (p<0.05) in group II than that in group I. SOD, GPx and G6PD activities in spermatozoa of both the groups were negatively correlated to lipid peroxidation of spermatozoa cell membrane [9].
• G6PD and GPx could not lower this oxidative stress [10].
• Finally, high glucose stimulated phosphorylation of G6PD [11].
• High glucose-induced inhibition of G6PD predisposed cells to cell death [11].

Anatomical context of G6PD

• G6PD transcript levels were significantly increased in IVP blastocysts compared with in vivo-generated and parthenogenetic embryos [8].
• CONCLUSIONS: Overexpression of G6PD in vascular endothelial cells decreases reactive oxygen species accumulation in response to exogenous and endogenous oxidant stress and improves levels of bioavailable NO [12].
• SOD, GPx and G6PD in both the groups showed a similar pattern of change i.e. the activities declined successively in spermatozoa and increased in the seminal plasma [9].
• Parental and hybrid cells were characterized for isozyme patterns of lactic dehydrogenase malate dehydrogenase, glucose-6-phosphate dehydrogenase, and glutamate oxalate transaminase [13].
• BCB staining determines the activity of glucose-6-phosphate dehydrogenase (G6PD), an enzyme synthesized in growing oocytes but with less activity in grown oocytes [14].

Associations of G6PD with chemical compounds

• METHODS AND RESULTS: Adenoviral-mediated gene transfer of G6PD increased G6PD expression, activity, and NADPH levels in bovine aortic endothelial cells (BAECs) [12].
• BAECs overexpressing G6PD maintained intracellular glutathione stores when exposed to oxidants because of increased activity of glutathione reductase, an effect that was not observed in endothelial cells with normal G6PD activity [12].
• Overexpression of G6PD was also associated with enhanced nitric oxide synthase activity, resulting in elevated levels of cGMP, nitrate, and nitrite, and this response was increased after stimulation with bradykinin [12].
• Amount of MDA produced in spermatozoa of both the groups was negatively correlated while SOD, GPx and G6PD activities in spermatozoa were positively correlated to the motility and viability of spermatozoa [9].
• The bovine genes for phosphoglycerate kinase, glucose-6-phosphate dehydrogenase, alpha-galactosidase, and hypoxanthine phosphoribosyltransferase are linked to the X chromosome in cattle-mouse cell hybrids [15].

Other interactions of G6PD

• Levels of G6PD and HPRT RNA were also higher in female morulae and blastocysts than in males, but only G6PD levels were significantly different between the sexes [16].
• Results showed that XIST expression was significantly higher (p < 0.05) in XXX cells compared to XX and XXY cells and that G6PD [17].
• Activities of antioxidant enzymes, viz. glucose-6-phosphate dehydrogenase (G6PD) and glutamate peroxidase (GPx) were also significantly increased (p<0.01) in group II [10].
• Frequently, genes that may be stress induced such as SOX, MnSOD, BAX, IFtau, and G6PD were highly transcribed in in vitro produced embryos and in embryos with slow developmental speed [18].
• The assumed centromere transposition between HSAX and BTAX associated with the rearranged chromosome segments is supported by cytogenetic assignments of the genes BGN and G6PD to BTAX [19].

Analytical, diagnostic and therapeutic context of G6PD

• Using a semiquantitative sensitive reverse transcriptase-polymerase chain reaction (RT-PCR) assay, we detected G6PD and HPRT mRNA expression at the early blastocyst stage in all bovine embryos analyzed [20].
• These mutants were analyzed for G6PD enzyme activity and the presence of immunologically cross-reactive proteins using immunoblotting techniques and antiserum directed against bovine G6PD [21].
• We also studied whether alpha-crystallin could renature G6PD denatured by MDA. alpha-Crystallin was prepared from bovine lenses by gel chromatography [22].
• The present data demonstrate that the cytochemical bioassay of PTH in a vitamin D-depleted animal is based on a dose-dependent difference in the time course of G6PD activity [23].
• Glucose 6-phosphate dehydrogenase was purified 450-fold with a yield of 91% by anion exchange chromatography and 2',5'-ADP agarose affinity chromatography [24].

References