Phospholipid-hydroperoxide glutathione peroxidase (GPx-4) localization in resting platelets, and compartmental change during platelet activation

Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids

Volumn 1761, Issue 10, 2006, Pages 1228-1234

  Januel, Caroline ^a   El Hentati, Fatima Zahra ^a   Carreras, Martine ^a   Arthur, John R ^a   Calzada, Catherine ^a   Lagarde, Michel ^a   Véricel, Evelyne ^a  

^a Univ Lyon   (France)

Author keywords

Confocal microscopy; Glutathione peroxidase; Platelet; Platelet activation; Subcellular fraction

Indexed keywords

CELL ENZYME; PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE PEROXIDASE;

ARTICLE; CARDIOVASCULAR SYSTEM; CELL COMPARTMENTALIZATION; CELL MEMBRANE STEADY POTENTIAL; CELL PROTECTION; CELLULAR DISTRIBUTION; CONFOCAL MICROSCOPY; CYTOSOL; ENZYME LOCALIZATION; ERYTHROCYTE MEMBRANE; HUMAN; HUMAN CELL; MITOCHONDRION; NORMAL HUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; STATISTICAL DISTRIBUTION; STATISTICAL SIGNIFICANCE; THROMBOCYTE; THROMBOCYTE ACTIVATION; THROMBOCYTE FUNCTION;

BLOOD PLATELETS; BLOTTING, WESTERN; CELL COMPARTMENTATION; CELL MEMBRANE; CYTOSOL; FLUORESCENT ANTIBODY TECHNIQUE; GLUTATHIONE PEROXIDASE; HUMANS; MICROSCOPY, CONFOCAL; MITOCHONDRIA; PLATELET ACTIVATION;

EID: 33749637534     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2006.07.015     Document Type: Article

References (41)

1. McCord J.M., and Fridovich I. The biology and pathology of oxygen radicals. Ann. Intern. Med. 89 (1978) 122-127
2. Brigelius-Flohé R. Tissue-specific functions of individual glutathione peroxidases. Free Radic. Biol. Med. 27 (1999) 951-961
3. Arthur J.R. The glutathione peroxidases. Cell. Mol. Life Sci. 57 (2000) 1825-1835
4. Imai H., and Nakagawa Y. Biological significance of phospholipid hydroperoxide glutathione peroxidase (PHGPx, GPx4) in mammalian cells. Free Radic. Biol. Med. 34 (2003) 145-169
5. Ursini F., Maiorino M., Valente M., Ferri L., and Gregolin C. Purification from pig liver of a protein which protects liposomes and biomembranes from peroxidative degradation and exhibits glutathione peroxidase activity on phosphatidylcholine hydroperoxides. Biochim. Biophys. Acta 710 (1982) 197-211
6. Ursini F., Maiorino M., and Gregolin C. The selenoenzyme phospholipid hydroperoxide glutathione peroxidase. Biochim. Biophys. Acta 839 (1985) 62-70
7. Pushpa-Rekha T.R., Burdsall A.L., Oleksa L.M., Chisolm G.M., and Driscoll D.M. Rat phospholipid-hydroperoxide glutathione peroxidase. J. Biol. Chem. 270 (1995) 26993-26999
8. Pfeifer H., Conrad M., Roethlein D., Kyriakopoulos A., Brielmeier M., Bornkamm G.W., and Behne D. Identification of a specific sperm nuclei selenoenzyme necessary for protamine thiol cross-linking during sperm maturation. FASEB 15 (2001) 1236-1238
9. Conrad M., Moreno S.G., Sinowatz F., Ursini F., Kölle S., Roveri A., Brielmeier M., Wurst W., Maiorino M., and Bornkamm G.W. The nuclear form of phospholipid hydroperoxide glutathione peroxidase is a protein thiol peroxidase contributing to sperm chromatin stability. Mol. Cell. Biol. 25 (2005) 7637-7644
10. Maiorino M., Roveri A., Benazzi L., Bosello V., Mauri P., Toppo S., Tosatto S.C.E., and Ursini F. Functional interaction of phospholipid hydroperoxide glutathione peroxidase with sperm mitochondrion-associated cysteine-rich protein discloses the adjacent cysteine motif as a new substrate of the selenoperoxidase. J. Biol. Chem. 280 (2005) 38395-38402
11. Kryukov G.V., Castellano S., Novoselov S.V., Lobanov A.V., Zehtab O., Guigo R., and Gladyshec V.N. Characterization of mammalian selenoproteomes. Science 300 (2003) 1439-1443
12. Roveri A., Maiorino M., Nisil C., and Ursini F. Purification and characterization of phospholipid hydroperoxide glutathione peroxidase from rat testis mitochondrial membranes. Biochim. Biophys. Acta 1208 (1994) 211-221
13. Nomura K., Imai H., Koumura T., Arai M., and Nakagawa Y. Mitochondrial phospholipid hydroperoxide glutathione peroxidase suppresses apoptosis mediated by a mitochondrial death pathway. J. Biol. Chem. 274 (1999) 29294-29302
14. Nomura K., Imai H., Koumura T., and Nakagawa Y. Involvement of mitochondrial phospholipid hydroperoxide glutathione peroxidase as an antiapoptotic factor. Biol. Signals Recept. 10 (2001) 81-92
15. Ran Q., Liang H., Gu M., Qi W., Walter C.A., Roberts II L.J., Herman B., Richardson A., and Van Remmen H. Transgenic mice overexpressing glutathione peroxidase 4 are protected against oxidative stress-induced apoptosis. J. Biol. Chem. 279 (2004) 55137-55146
16. Yant L.J., Ran Q., Rao L., Van Remmen H., Shibatani T., Belter J.G., Motta L., Richardson A., and Prolla T.A. The selenoprotein GPX4 is essential for mouse development and protects from radiation and oxidative damage insults. Free Radic. Biol. Med. 34 (2003) 496-502
17. Hamberg M., Svensson J., and Samuelsson B. Thromboxanes: a new group of biologically active compounds derived from prostaglandin endoperoxides. Proc. Natl. Acad. Sci. U. S. A. 72 (1975) 2994-2998
18. Davi G., Ciabattoni G., Consoli A., Mezzetti A., Falco A., Santarone S., Pennese E., Vitacolonna E., Bucciarelli T., Constantini F., Capani F., and Patrono C. In vivo formation of 8-iso-prostaglandin F2alpha and platelet activation in diabetes mellitus: effects of improved metabolic and vitamin E supplementation. Circulation 99 (1999) 224-229
19. Véricel E., Januel C., Carreras M., Moulin P., and Lagarde M. Diabetic patients without vascular complications display enhanced basal platelet activation and decreased antioxidant status. Diabetes 53 (2004) 1046-1051
20. Bryant R.W., Simon T.C., and Bailey J.M. Role of glutathione peroxidase and hexose monophosphate shunt in the platelet lipoxygenase pathway. J. Biol. Chem. 257 (1982) 14937-14943
21. Hemler M.E., Cook H.W., and Lands W.E.M. Prostaglandin biosynthesis can be triggered by lipid peroxides. Arch. Biochem. Biophys. 193 (1979) 340-345
22. Ludwig P., Holzhütter H.G., Colosimo A., Silvestrini M.C., Schewe T., and Rapoport S.M. Effect of lipid hydroperoxide on lipoxygenase kinetics. Eur. J. Biochem. 168 (1987) 325-337
23. Schilstra M.J., Veldink G.A., and Vliegenthart J.F.G. Effect of lipid hydroperoxide on lipoxygenase kinetics. Biochemistry 31 (1992) 7692-7699
24. Kühn H. Biosynthesis, metabolization and biological importance of the primary 15-lipoxygenase metabolites 15-hydro(pero)XY-5Z,8Z,11Z,13E-eicosatetraenoic acid and 13-hydro(pero)XY-9Z,11E-octadecadienoic acid. Prog. Lipid Res. 35 (1996) 203-226
25. Calzada C., Véricel E., Mitel B., Coulon L., and Lagarde M. 12(S)-hydroperoxy-eicosatetraenoic acid availability in collagen-primed platelets. J. Lipid Res. 42 (2001) 1467-1473
26. Lagarde M., Bryon P.A., Guichardant M., and Dechavanne M. A simple and efficient method for platelet isolation from their plasma. Thromb. Res. 17 (1980) 581-588
27. Mauco G., Fauvel J., Chap H., and Douste-Blazy L. Studies on enzyme related to diacylglycerol production in activated platelets. Biochim. Biophys. Acta 796 (1984) 169-177
28. Lagarde M., Croset M., Authi K., and Crawford N. Subcellular localization and some properties of lipoxygenase activity in blood platelets. Biochem. J. 222 (1984) 495-500
29. Parent C.A., Lagarde M., Venton D.L., and Le Breton G.C. Selective modulation of the human platelet thromboxaneA2/prostaglandin H2 receptor by eicosapentaenoic and docosahexaenoic acids in intact platelets and solubilized platelet membranes. J. Biol. Chem. 267 (1992) 6541-6547
30. Storrie B., and Madden E.A. Isolation of subcellular organelles. Methods Enzymol. 182 (1990) 203-235
31. Wharton D.C., and Tzagoloff A. Cytochrome oxidase from beef heart mitochondria. Methods Enzymol. 10 (1967) 245-250
32. Roveri A., Maiorino M., and Ursini F. Enzymatic and immunological measurements of soluble and membrane-bound phospholipid-hydroperoxide glutathione peroxidase. Methods Enzymol. 233 (1994) 202-212
33. Paglia D.E., and Valentine W.N. Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J. Lab. Clin. Med. 70 (1967) 158-169
34. Rey C., Véricel E., Némoz G., Chen W., Chapuy P., and Lagarde M. Purification and characterization of glutathione peroxidase from human blood platelets. Age-related changes in the enzyme. Biochim. Biophys. Acta 1226 (1994) 219-224
35. Brown K.M., Pickard K., Nicol F., Beckett G.J., Duthie G.G., and Arthur J.R. Effects of organic and inorganic selenium supplementation on selenoenzyme activity in blood lymphocytes, granulocytes, platelets and erythrocytes. Clin. Sci. 98 (2000) 593-599
36. Sutherland M., Shankaranarayanan P., Schewe T., and Nigam S. Evidence for the presence of phospholipid hydroperoxide glutathione peroxidase in human platelets: implications for its involvement in the regulatory network of the 12-lipoxygenase pathway of arachidonic acid metabolism. Biochem. J. 353 (2001) 91-100
37. Nomura K., Imai H., Koumura T., Kobayashi T., and Nakagawa Y. Mitochondrial phospholipid hydroperoxide glutathione peroxidase inhibits the release of cytochrome c from mitochondria by suppressing the peroxidation of cardiolipin in hypoglycaemia-induced apoptosis. Biochem. J. 351 (2000) 183-193
38. Vanags D.M., Orrenius S., and Aguilar-Santelises M. Alterations in Bcl-2/Bax protein levels in platelets form part of an ionomycin-induced process that resembles apoptosis. Br. J. Haematol. 99 (1997) 824-831
39. Imai H., Narashima K., Arai M., Sakamoto H., Chiba N., and Nakagawa Y. Suppression of leukotriene formation in RBL-2H3 cells that overexpressed phospholipid hydroperoxide glutathione peroxidase. J. Biol. Chem. 273 (1998) 1990-1997
40. Sakamoto H., Imai H., and Nakagawa Y. Involvement of phospholipid hydroperoxide glutathione peroxidase in the modulation of prostaglandin D2 synthesis. J. Biol. Chem. 275 (2000) 40028-40035
41. Hamberg M., and Samuelsson B. Prostaglandin endoperoxides. Novel transformations of arachidonic acid in human platelets. Proc. Natl. Acad. Sci. U. S. A. 71 (1974) 3400-3404