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• W996874166 abstract "Fő megallapitasaink: 1. Az arzenit (AsIII) expozicio novelesevel eliminacioja metilacioval lassul (ezt nem a metildonor-kinalat kimerulese okozza), a szovetekben a glutation (GSH) es az ATP depletalodik, az AsIII retinealodik. Mindezek elősegitik az akut As-expozicio okozta toxicitast. 2. Az arzenat (AsV) a szervezetben sokkal mergezőbb AsIII-te redukalodik. Ez a folyamat GSH-fuggő csakugy, mint az AsIII metilacioja es a trivalens arzenvegyuletek (AsIII, metilarzenit) biliaris exkrecioja GSH-konjugatumkent. 3. A gamma-glutamyl transzferaz (GSH-t es GSH-konjugatumokat hidrolizalo enzim) aktivitasa nem befolyasolja a GSH-konjugatumot kepező trivalens arzenmetabolitok sorsat patkanyban. 4. A fenobarbital-indukcio fokozza az AsV redukciojat AsIII-te es az AsIII biliaris exkreciojat. 5. A purin-nukleozid-foszforilaz (PNP) kepes az AsV redukciot katalizalni in vitro, megsem fontos az AsV redukciojaban, sem emberi vvt-ben, sem patkanyban in vivo. 6. A human vvt-ben es patkanymaj citoszolban van PNP-fuggetlen AsV-redukalo mechanizmus is; ez GSH-t, NAD-ot es glikolitikus szubsztratot igenyel. 7. Az AsV glikolizishez kotott redukciojat a gliceraldehid-3-foszfat-dehidrogenaz (GAPDH) katalizalja GSH, NAD es glikolitikus szubsztrat felhasznalasaval. A GAPDH egyedul felelős az AsV redukciojaert emberi eritrocitakban. 8. A majbeli GAPDH inaktivalasaval nyert megfigyeleseink valoszinűsitik, hogy a GAPDH reszt vesz az AsV redukciojaban in vivo is. | Main findings: 1. With increased exposure to arsenite (AsIII), its elimination via methylation slows (not because of compromised methyl donor-availability), tissue glutathione (GSH) as well as ATP become depleted, and AsIII becomes retained. These changes promote toxicity after acute As-exposure. 2. Arsenate (AsV) is reduced in the body to the much more toxic AsIII. This process is GSH dependent, like methylation of AsIII and biliary excretion of trivalent arsenicals (AsIII, methylarsenite) as GSH-conjugates. 3. The activity of gamma-glutamyl transferase (an enzyme hydrolyzing GSH and GSH-conjugates) does not affect the fate of trivalent arsenic metabolites known to form GSH-conjugates. 4. Phenobarbital-induction enhances reduction of AsV to AsIII and the biliary excretion of AsIII. 5. Purine nucleoside phosphorylase (PNP) can catalyze reduction of AsV in vitro, yet it is unimportant in reduction of AsV either in human RBC or in rats in vivo. 6. There is a PNP-independent AsV-reducing mechanism in human RBC and rat liver cytosol; this requires GSH, NAD and glycolytic substrate. 7. The glycolysis-coupled reduction of AsV is catalyzed by glyceraldehyde 3-phosphate dehydrogenase (GAPDH), using GSH, NAD and glycolytic substrate. A GAPDH is solely responsible for reduction of AsV in human erythrocyes. 8. Our observations on rats with inactivated hepatic GAPDH suggest that GAPDH participates in AsV reduction also in vivo." @default.
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• W996874166 date "2007-01-01" @default.
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• W996874166 title "Az arzén toxicitás metabolikus háttere = The metabolic background of arsenic toxicity" @default.
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