PL EN


Preferences help
enabled [disable] Abstract
Number of results
2007 | 54 | 4 | 797-803
Article title

Response of Acanthamoeba castellanii mitochondria to oxidative stress

Content
Title variants
Languages of publication
EN
Abstracts
EN
The purpose of this study was to examine the effects of oxidative stress caused by hydroperoxide (H2O2) in the presence of iron ions (Fe2+) on mitochondria of the amoeba Acanthamoeba castellanii. We used isolated mitochondria of A. castellanii and exposed them to four levels of H2O2 concentration: 0.5, 5, 15, and 25 mM. We measured basic energetics of mitochondria: oxygen consumption in phosphorylation state (state 3) and resting state (state 4), respiratory coefficient rates (RC), ADP/O ratios, membrane potential (ΔΨm), ability to accumulate Ca2+ , and cytochrome c release. Our results show that the increasing concentrations of H2O2 stimulates respiration in states 3 and 4. The highest concentration of H2O2 caused a 3-fold increase in respiration in state 3 compared to the control. Respiratory coefficients and ADP/O ratios decreased with increasing stress conditions. Membrane potential significantly collapsed with increasing hydroperoxide concentration. The ability to accumulate Ca2+ also decreased with the increasing stress treatment. The lowest stress treatment (0.5 mM H2O2) significantly decreased oxygen consumption in state 3 and 4, RC, and membrane potential. The ADP/O ratio decreased significantly under 5 mM H2O2 treatment, while Ca2+ accumulation rate decreased significantly at 15 mM H2O2. We also observed cytochrome c release under increasing stress conditions. However, this release was not linear. These results indicate that as low as 0.5 mM H2O2 with Fe2+ damage the basic energetics of mitochondria of the unicellular eukaryotic organism Acanthamoeba castellanii.
Year
Volume
54
Issue
4
Pages
797-803
Physical description
Dates
published
2007
received
2007-08-22
revised
2007-11-14
accepted
2007-12-03
(unknown)
2007-12-13
References
  • Belzacq AS, Vieira HLA, Kroemer G, Brenner C (2002) The adenine nucleotide translocator in apoptosis. Biochimie 84: 167-176.
  • Bernardi P (1999) Mitochondrial transport of cations: channels, exchangers and permeability transition. Physiol Rev 79: 1127-1155.
  • Chen Q, Vazquez EJ, Moghaddas S, Hoppel CL, Lesnefsky EJ (2003) Production of reactive oxygen species by mitochondria: Central role of complex III. J Biol Chem 278: 36027-36031.
  • Czarna M, Jarmuszkiewicz W (2005) Activation of alternative oxidase and uncoupling protein lowers hydrogen peroxide formation in amoeba Acanthamoeba castellanii mitochondria. FEBS Lett 579: 3136-3140.
  • Domka-Popek A, Michejda JW (1986) The upake of Ca^2+ by mitochondria of amoeba supported by malate or ATP. Bull Soc Sci Lett 25.
  • Fleury C, Mignotte B, Vayssière JL (2002) Mitochondrial reactive oxygen species in cell death signaling. Biochimie 84: 131-141.
  • Garnier M, Dimchev A, Boujard N, Price J, Musto N, Papadopoulos V (1994) In vitro reconstitution of a functional benzodiazepine receptor from mouse Leyding tumor cells. Mol Pharmacol 45: 201-211.
  • Gincel D, Zaid H, Shoshan-Bermatz V (2001) Calcium binding and translocation by the voltage-dependent anion channel: a possible regulatory mechanism in mitochondrial function. Biochem J 358: 147-155.
  • Halestrap AP, McStay GP, Clarke SJ (2002) The permeability transition pore complex: another view. Biochimie 84: 153-166.
  • Jarmuszkiewicz W, Wagner AM, Wagner JM, Hryniewiecka L (1997) Immunological identification of the alternative oxidase of Acanthamoeba castellanii mitochondria. FEBS Lett 411: 110-114.
  • Kowaltowski A, Castilho R, Verces A (1996) Opening of the mitochondrial transition pore by uncoupling or inorganic phosphate in the presence of Ca^2+ is dependent on mitochondrial-generated reactive oxygen species. FEBS Lett 378: 150-152.
  • Kroemer G, Zamzani N, Susin SA (1997) Mitochondrial control of apoptosis. Immunol Today 18: 44-51.
  • Lenaz G, Bovina C, FormigginiG. Castelli-Parenti G (1999) Mitochondria, oxidative stress, and antioxidant defences. Acta Biochim Polon 46: 1-21.
  • Li Y, Trush MA (1998) Diphenyleneiodonium, an NAD(P)H oxidase inhibitor, also potently inhibits mitochondrial reactive oxygen species production. Biochem Biophys Res Commun 253: 295-299.
  • Martinou JC, Deshager S, Antonsson B (2000) Cytochrome c release from mitochondria: all or nothing. Nature Cell Biol 2: E41-E43.
  • Maxwell DP, Wang Y, McIntosh L (1999) The alternative oxidase lowers mitochondrial reactive oxygen production in plant cells. Proc Natl Acad Sci USA 96: 8271-8276.
  • Michejda JW, Schöneich J, Hryniewiecka L (1988) Activity of catalase in Acanthamoeba castellanii grown in conditions preferring the activity of cytochrome or alternative respiratory pathways. Bull Soc Sci Lett 26.
  • Minotti G, Aust SD (1987) The requirement for iron (III) in the initiation of lipid peroxidation by iron (II) and hydrogen peroxide. J Biol Chem 262: 1098-1104.
  • Papa S, Skulachev VP (1997) Reactive oxygen species, mitochondria, apoptosis and aging. Mol Cell Biochem 174: 305-319.
  • Purvis AC (1997) Role of the alternative oxidase in limiting superoxide production by plant mitochondria. Physiol Plant 100: 165-170.
  • Radi R, Bush KM, Freeman BA (1993) The role of cytochrome c and mitochondrial catalase in hydroperoxide-induced heart mitochondrial lipid peroxidation. Arch Biochem Biophys 300: 409-415.
  • Schein SJ, Colombini M, Finkelstein A (1976) Reconstitution in planar lipid bilayers of a voltage-dependent anion-selective channel obtained from Paramecium mitochondria. J Membr Biol 30: 99-120.
  • Shimizu S, Narita M, Tsujimoto Y (1999) Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature 399: 483-487.
  • Shimizu S, Ide T, Yanagida T, Tsujimoto Y (2000) Electrophysiological study of novel large pore formed by Bax and the voltage-dependent anion channel that is permeable to cytochrome c. J Biol Chem 275: 12321-12325.
  • Stridh H, Kimland M, Jones DP, Orrenius S, Hampton MB (1998) Cytochrome c release and caspase activation in hydrogen peroxide- and tributyltin-induced apoptosis. FEBS Lett 429: 351-355.
  • Sweetlove LJ, Heazlewood JL, Herald V, Holtzapffel R, Day DA, Leaver CJ, Millar AH (2002) The impact of oxidative stress on Arabidopsis mitochondria. Plant J 32: 891-904.
  • Ślesak I, Libik M, Karpińska B, Karpiński S, Miszalski Z (2007) The role of hydrogen peroxide in regulation of plant metabolism and cellular signalling in response to environmental stresses. Acta Biochim Polon 54: 39-50.
  • Tiwari BS, Belenghi B, Levine A (2002) Oxidative stress increased respiration and generation of reactive oxygen species, resulting in ATP depletion, opening of mitochondrial permeability transition, and programmed cell death. Plant Physiol 128: 1271-1281.
  • Vyssokikh M, Brdiczka D (2003) The function of complexes between the outer mitochondrial membrane pore (VDAC) and the adenine nucleotide translocase in regulation of energy metabolism and apoptosis. Acta Biochim Polon 50: 389-404.
  • Wudarczyk J, Dębska G, Lenartowicz E (1999) Zinc as inducer of the membrane permeability transition pore in rat liver mitochondria. Arch Biochem Biophys 363: 1-8.
Document Type
Publication order reference
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv54p797kz
Identifiers
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.