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Glutathione peroxidase and glutathione S-transferase activity of platelets

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Abstract

A low Se intake in dietetically treated patients with phenylketonuria (PKU) or maple syrup urine disease (MSUD) leads to a marked reduction of the platelet glutathione peroxidase activity (GSHPx). The mean value amounted to 2.0 U/1011 platelets with t-butyl hydroperoxide (t-BOOH) (2.2 U/1011 with H2O2) in patients and 5.8 U/1011 with t-BOOH (5.4 U/1011 with H2O2) in the control children. After Se supplementation with yeast rich in Se (dose: 135 μg Se/m2) the GSHPx activities rapidly increased. They reached a plateau after 2–3 weeks and remained there during the following 15–20 weeks of supplementation. After the cessation of supplementation there was a slow decrease, the values reached a low plateau after 24 weeks.

In addition platelet glutathione S-transferase (GSHTf) was estimated with 1-chloro-2,4-dinitrobenzene. No significant difference between the values in healthy and dietetically treated patients in a low or normal Se state was observed. GSHTf did not exhibit peroxidase activity and did not show a compensatory increase when Se dependent GSHPx activity was low.

The patients do not reveal clinical signs of disturbed platelet function. GSHPx may act in platelets via lipoxygenase on the prostaglandin pathway. The physiologic consequence of altered arachidonate metabolism, when GSHPx is deficient in platelets, remains to be elucidated.

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References

  1. Beutler E, Matsumoto F (1975) Ethnic variation in red cell glutathione peroxidase activity. Blood 46:103–110

    Google Scholar 

  2. Bryant RW, Bailey JM (1980) Altered lipoxygenase metabolism and decreased glutathione peroxidase activity in platelets from selenium-deficient rats. Biochem Biophys Res Commun 92: 268–276

    Google Scholar 

  3. Bryant RW, Bailey JM, King JC, Levander OA (1981) Altered platelet peroxidase activity and arachidonic acid metabolism during selenium repletion in a controlled human study. In: Spallholz JE et al (eds) Selenium in biology and medicine. AVI Publ Comp, INC, Westport, Conn, pp 395–399

    Google Scholar 

  4. Burk RF, Lawrence RA, Correia MA (1980) Sex differences in biochemical manifestations of selenium deficiency in rat liver with special reference to heme metabolism. Biochem Pharmacol 29:39–42

    Google Scholar 

  5. Chen X, Guangqi Y, Chen J, Chen Y, Wen Z, Ge K (1980) Studies on the relations of selenium and Keshan disease. Biol Trace Elem Res 2:91–107

    Google Scholar 

  6. Cikryt P, Feuerstein S, Wendel A (1982) Selenium-and nonselenium-dependent glutathione peroxidase in mouse liver. Biochem Pharmacol 31:2873–2877

    Google Scholar 

  7. Günzler WA, Kremers H, Flohé L (1974) An improved coupled test procedure for glutathione peroxidase (EC 1.11.1.9) in blood. Z Klin Chem Klin Biochem 12:444–448

    Google Scholar 

  8. Habig WH, Pabst MJ, Jakoby WB (1974) Glutathione S-transferase, the first enzymatic step in mercapturic acid formation. J Biol Chem 249:7130–7139

    Google Scholar 

  9. Karpatkin S, Weiss HJ (1972) Deficiency of glutathione peroxidase associated with high levels of reduced glutathione in Glanzmann's thrombasthenia. New Engl J Med 21:1062–1072

    Google Scholar 

  10. Kasperek K, Iyengar GV, Kiem J, Borberg H, Feinendegen LE (1979) Elemental composition of platelets. Part III. Determination of Ag, Au, Cd, Co, Cr, Cs, Mo, Rb, Sb and Se in normal human platelets by neutron activation analysis. Clin Chem 25:711–715

    Google Scholar 

  11. Katki AG, Myers CE (1980) Membrane-bound glutathione peroxidase-like activity in mitochondria. Biochem Biophys Res Comm 96:85–91

    Google Scholar 

  12. Konz KH (1979) Die Aktivität des Peroxid-metabolisierenden Systems in Human-Leber. J Clin Chem Clin Biochem 17:353–357

    Google Scholar 

  13. Lawrence RA, Burk RF (1976) Glutathione peroxidase activity in selenium-deficient rat liver. Biochem Biophys Res Comm 71:952–958

    Google Scholar 

  14. Lawrence RA, Burk RF (1978) Species, tissues and subcellular distribution of non-Se-dependent glutathione peroxidase activity. J Nutr 108:211–215

    Google Scholar 

  15. Lawrence RA, Parkhill LK, Burk RF (1978) Hepatic cytosolic nonselenium-dependent glutathione peroxidase activity. Its nature and the effect of selenium deficiency. J Nutr 108:981–987

    Google Scholar 

  16. Levander OA, Morris VC (1981) Dietary selenium and rat platelet glutathione peroxidase. In: McC Howell et al (eds) Trace element metabolism in man and animals. IV. Australian Academy of Science. Canberra, pp 169–171

    Google Scholar 

  17. Lombeck I, Kasperek K, Bachmann D, Feinendegen LE, Bremer HJ (1980) Selenium requirements in patients with inborn errors of amino acid metabolism and selenium deficency. Eur J Pediatr 134:65–68

    Google Scholar 

  18. Lombeck I, Kasperek K, Iyengar GV, Kiem J, Feinendegen LE, Bremer HJ (1981) Selenium in platelets of children with low selenium state. In: Mec Howell et al (eds) Trace element metabolism in man and animals. IV. Australian Academy of Science, Canberra, pp 26–29

    Google Scholar 

  19. Menzel H Unpublished data

  20. Paglia DE, Valentine WN (1967) Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J Lab Clin Med 70:158–169

    Google Scholar 

  21. Pierce S, Tappel AL (1978) Glutathione peroxidase activities from rat liver. Biochim Biophys Acta 523:27–36

    Google Scholar 

  22. Polidoro G, Di Ilio C, Arduini A, Federici C (1982) Glutathione peroxidase and glutathione S-transferase activities in human fetal tissues. Inability of acidic forms of glutathione S-transferase to catalyse the reduction of organic hydroperoxides. Biochem Internat 4:637–645

    Google Scholar 

  23. Prohaska JR, Ganther HE (1977) Glutathione peroxidase activity of glutathione-S-transferase purified from rat liver. Biochem Biophys Res Commun 76:437–445

    Google Scholar 

  24. Ramos Martinez JI, Launay JM, Dreux C (1980) Blood platelet glutathione peroxidase: Some properties and partial purification. Thromb Res 19:73–83

    Google Scholar 

  25. Steiner G, Menzel H, Lombeck I, Ohnesorge FK, Bremer HJ (1982) Plasma glutathione peroxidase after selenium supplementation in patients with reduced selenium state. Eur J Pediatr 138:138–140

    Google Scholar 

  26. Stone WL, Dratz EA (1980) Increased glutathione-S-transferase activity in antitoxidant-deficient rats. Biochim Biophys Acta 631:503–506

    Google Scholar 

  27. Szeinberg A, Golan R, Ben-Ezer J, Sarova-Pinhas I, Kindler D (1981) Glutathione peroxidase activity in various types of blood cells in multiple sclerosis. Acta Neurol Scand 63:67–75

    Google Scholar 

  28. Wang YX, Böcker K, Reuter H, Kiem J, Kasperek K, Iyengar GV, Loogen F, Gross R, Feinendegen LE (1981) Selenium and myocardial infarction: glutathione peroxidase in platets. Klin Wochenschr 59:817–818

    Google Scholar 

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Menzel, H., Steiner, G., Lombeck, I. et al. Glutathione peroxidase and glutathione S-transferase activity of platelets. Eur J Pediatr 140, 244–247 (1983). https://doi.org/10.1007/BF00443370

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