Intraluminal hydrogen peroxide induces a permeability change of the endoplasmic reticulum membrane

FEBS Letters

Volumn 582, Issue 30, 2008, Pages 4131-4136

  Margittai, Éva ^a   Löw, Péter ^b   Szarka, András ^c   Csala, Miklós ^a   Benedetti, Angelo ^d   Bánhegyi, Gábor ^a,d  

^a SEMMELWEIS UNIVERSITY   (Hungary)

^b EÖTVÖS LORÁND UNIVERSITY   (Hungary)

^c BUDAPEST UNIVERSITY OF TECHNOLOGY AND ECONOMICS   (Hungary)

^d UNIVERSITY OF SIENA   (Italy)

Author keywords

ER stress; Glutathione; Gulonolactone oxidase; Hydrogen peroxide; Membrane permeability; Oxidative protein folding

Indexed keywords

GLUTATHIONE; GULONOLACTONE; HYDROGEN PEROXIDE; LACTONE DERIVATIVE; UNCLASSIFIED DRUG;

ANIMAL TISSUE; ARTICLE; CELL ORGANELLE; CELL STRESS; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; MALE; MEMBRANE PERMEABILITY; MEMBRANE TRANSPORT; MICROSOME MEMBRANE; MOLECULAR WEIGHT; MOUSE; NONHUMAN; OXIDATION REDUCTION STATE; PRIORITY JOURNAL;

ANIMALS; ASCORBIC ACID; ENDOPLASMIC RETICULUM; GLUTATHIONE; HYDROGEN PEROXIDE; INTRACELLULAR MEMBRANES; LIVER; MALE; MICE; MICE, INBRED STRAINS; MICROSCOPY, ELECTRON; MICROSOMES, LIVER; OXIDATION-REDUCTION; PERMEABILITY; SUGAR ACIDS;

MUS;

EID: 57049168093     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.11.012     Document Type: Article

References (28)

1. Jessop C.E., Chakravarthi S., Watkins R.H., and Bulleid N.J. Oxidative protein folding in the mammalian endoplasmic reticulum. Biochem. Soc. Trans. 32 (2004) 655-658
2. Sevier C.S., and Kaiser C.A. Conservation and diversity of the cellular disulfide bond formation pathways. Antioxid. Redox Signal. 8 (2006) 797-811
3. Sevier C.S., and Kaiser C.A. Ero1 and redox homeostasis in the endoplasmic reticulum. Biochim. Biophys. Acta 1783 (2008) 549-556
4. Tu B.P., and Weissman J.S. The FAD- and O(2)-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum. Mol. Cell 10 (2002) 983-994
5. Gross E., Sevier C.S., Heldman N., Vitu E., Bentzur M., Kaiser C.A., Thorpe C., and Fass D. Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p. Proc. Natl. Acad. Sci. USA 103 (2006) 299-304
6. Malhotra J.D., and Kaufman R.J. Endoplasmic reticulum stress and oxidative stress: a vicious cycle or a double-edged sword?. Antioxid. Redox Signal. 9 (2007) 2277-2293
7. Bánhegyi G., Benedetti A., Csala M., and Mandl J. Stress on redox. FEBS Lett. 581 (2007) 3634-3640
8. Kiuchi K., Nishikimi M., and Yagi K. Purification and characterization of l-gulonolactone oxidase from chicken kidney microsomes. Biochemistry 21 (1982) 5076-5082
9. Bánhegyi G., Csala M., Braun L., Garzó T., and Mandl J. Ascorbate synthesis-dependent glutathione consumption in mouse liver. FEBS Lett. 381 (1996) 39-41
10. Puskás F., Braun L., Csala M., Kardon T., Marcolongo P., Benedetti A., Mandl J., and Bánhegyi G. Gulonolactone oxidase activity-dependent intravesicular glutathione oxidation in rat liver microsomes. FEBS Lett. 430 (1998) 293-296
11. Margittai E., and Bánhegyi G. Isocitrate dehydrogenase: A NADPH-generating enzyme in the lumen of the endoplasmic reticulum. Arch. Biochem. Biophys. 471 (2008) 184-190
12. Burchell A., Hume R., and Burchell B. A new microtechnique for the analysis of the human hepatic microsomal glucose-6-phosphatase system. Clin. Chim. Acta 173 (1988) 183-191
13. Fulceri R., Bánhegyi G., Gamberucci A., Giunti R., Mandl J., and Benedetti A. Evidence for the intraluminal positioning of p-nitrophenol UDP-glucuronosyltransferase activity in rat liver microsomal vesicles. Arch. Biochem. Biophys. 309 (1994) 43-46
14. Frand A.R., and Kaiser C.A. Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum. Mol. Biol. Cell 11 (2000) 2833-2843
15. Bánhegyi G., Marcolongo P., Fulceri R., Hinds C., Burchell A., and Benedetti A. Demonstration of a metabolically active glucose-6-phosphate pool in the lumen of liver microsomal vesicles. J. Biol. Chem. 272 (1997) 13584-13590
16. Nagy G., Kardon T., Wunderlich L., Szarka A., Kiss A., Schaff Z., Bánhegyi G., and Mandl J. Acetaminophen induces ER dependent signaling in mouse liver. Arch. Biochem. Biophys. 459 (2007) 273-279
17. Bánhegyi G., Lusini L., Puskás F., Rossi R., Fulceri R., Braun L., Mile V., di Simplicio P., Mandl J., and Benedetti A. Preferential transport of glutathione versus glutathione disulfide in rat liver microsomal vesicles. J. Biol. Chem. 274 (1999) 12213-12216
18. Csala M., Fulceri R., Mandl J., Benedetti A., and Bánhegyi G. Glutathione transport in the endo/sarcoplasmic reticulum. Biofactors 17 (2003) 27-35
19. Sato P., and Udenfriend S. Scurvy-prone animals, including man, monkey, and guinea pig, do not express the gene for gulonolactone oxidase. Arch. Biochem. Biophys. 187 (1978) 158-162
20. Griffith O.W. Biologic and pharmacologic regulation of mammalian glutathione synthesis. Free Radic. Biol. Med. 27 (1999) 922-935
21. Bienert G.P., Møller A.L., Kristiansen K.A., Schulz A., Møller I.M., Schjoerring J.K., and Jahn T.P. Specific aquaporins facilitate the diffusion of hydrogen peroxide across membranes. J. Biol. Chem. 282 (2007) 1183-1192
22. Bienert G.P., Schjoerring J.K., and Jahn T.P. Membrane transport of hydrogen peroxide. Biochim. Biophys. Acta 1758 (2006) 994-1003
23. 2 permeation through cytoplasmic and peroxisomal membranes: comparison with experimental data. Biochim. Biophys. Acta 1673 (2004) 149-159
24. Higo T., Hattori M., Nakamura T., Natsume T., Michikawa T., and Mikoshiba K. Subtype-specific and ER lumenal environment-dependent regulation of inositol 1, 4, 5-trisphosphate receptor type 1 by ERp44. Cell 120 (2005) 85-98
25. Kang S., Kang J., Kwon H., Frueh D., Yoo S.H., Wagner G., and Park S. Effects of redox potential and Ca2+ on Inositol 1, 4, 5-trisphosphate receptor L3-1 loop region: implications for receptor regulation. J. Biol. Chem. 283 (2008) 25567-25575
26. 2+ mobilization. Arterioscler. Thromb. Vasc. Biol. 28 (2008) 1774-1781
27. 2+ release channel from skeletal muscle sarcoplasmic reticulum. J. Biol. Chem. 270 (1995) 25557-25563
28. Kemmerling U., Muñoz P., Müller M., Sánchez G., Aylwin M.L., Klann E., Carrasco M.A., and Hidalgo C. Calcium release by ryanodine receptors mediates hydrogen peroxide-induced activation of ERK and CREB phosphorylation in N2a cells and hippocampal neurons. Cell Calcium 41 (2007) 491-502