Redox characterization of human cyclophilin D: Identification of a new mammalian mitochondrial redox sensor?

Linard D, Kandlbinder A, Degand H, Morsomme P, Dietz K-J, Knoops B (2009)
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS 491(1-2): 39-45.

Download
Es wurde kein Volltext hochgeladen. Nur Publikationsnachweis!
Zeitschriftenaufsatz | Veröffentlicht | Englisch
Autor
; ; ; ; ;
Abstract / Bemerkung
Mitochondria are metabolically highly active cell organelles that are also implicated in reactive oxygen species production and in cell death regulation. Cyclophilin D, the only human mitochondrial isoform of cyclophilins, plays an essential role in the formation of the mitochondrial permeability transition pore leading to cell necrosis. Recently, it has been shown that redox environment modifies structural and functional properties of some plant cyclophilins. Here, it is shown that oxidation of human cyclophilin D influences the conformation of the enzyme but also its activity. Site-directed mutagenized variants of cyclophilin D allowed the identification of cysteine 203 as an important redox-sensitive residue. Moreover, the redox modulation of cyclophilin D was confirmed in human neuroblastoma SH-SY5Y cells exposed to oxidative stress. Altogether, our results suggest that cyclophilin D may play a role as a redox sensor in mitochondria of mammalian cells transmitting information on the redox environment to target proteins. (C) 2009 Elsevier Inc. All rights reserved.
Erscheinungsjahr
Zeitschriftentitel
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Band
491
Zeitschriftennummer
1-2
Seite
39-45
ISSN
PUB-ID

Zitieren

Linard D, Kandlbinder A, Degand H, Morsomme P, Dietz K-J, Knoops B. Redox characterization of human cyclophilin D: Identification of a new mammalian mitochondrial redox sensor? ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS. 2009;491(1-2):39-45.
Linard, D., Kandlbinder, A., Degand, H., Morsomme, P., Dietz, K. - J., & Knoops, B. (2009). Redox characterization of human cyclophilin D: Identification of a new mammalian mitochondrial redox sensor? ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 491(1-2), 39-45. doi:10.1016/j.abb.2009.09.002
Linard, D., Kandlbinder, A., Degand, H., Morsomme, P., Dietz, K. - J., and Knoops, B. (2009). Redox characterization of human cyclophilin D: Identification of a new mammalian mitochondrial redox sensor? ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS 491, 39-45.
Linard, D., et al., 2009. Redox characterization of human cyclophilin D: Identification of a new mammalian mitochondrial redox sensor? ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 491(1-2), p 39-45.
D. Linard, et al., “Redox characterization of human cyclophilin D: Identification of a new mammalian mitochondrial redox sensor?”, ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, vol. 491, 2009, pp. 39-45.
Linard, D., Kandlbinder, A., Degand, H., Morsomme, P., Dietz, K.-J., Knoops, B.: Redox characterization of human cyclophilin D: Identification of a new mammalian mitochondrial redox sensor? ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS. 491, 39-45 (2009).
Linard, Dominique, Kandlbinder, Andrea, Degand, Herve, Morsomme, Pierre, Dietz, Karl-Josef, and Knoops, Bernard. “Redox characterization of human cyclophilin D: Identification of a new mammalian mitochondrial redox sensor?”. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS 491.1-2 (2009): 39-45.

40 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

A novel role of the mitochondrial permeability transition pore in (-)-gossypol-induced mitochondrial dysfunction.
Warnsmann V, Meyer N, Hamann A, Kögel D, Osiewacz HD., Mech Ageing Dev 170(), 2018
PMID: 28684269
Oxidative stress alters mitochondrial bioenergetics and modifies pancreatic cell death independently of cyclophilin D, resulting in an apoptosis-to-necrosis shift.
Armstrong JA, Cash NJ, Ouyang Y, Morton JC, Chvanov M, Latawiec D, Awais M, Tepikin AV, Sutton R, Criddle DN., J Biol Chem 293(21), 2018
PMID: 29626097
Protein Promiscuity in H2O2 Signaling.
Young D, Pedre B, Ezeriņa D, De Smet B, Lewandowska A, Tossounian MA, Bodra N, Huang J, Astolfi Rosado L, Van Breusegem F, Messens J., Antioxid Redox Signal (), 2018
PMID: 29635930
Divergent Effects of Cyclophilin-D Inhibition on the Female Rat Heart: Acute Versus Chronic Post-Myocardial Infarction.
Parodi-Rullán RM, Soto-Prado J, Vega-Lugo J, Chapa-Dubocq X, Díaz-Cordero SI, Javadov S., Cell Physiol Biochem 50(1), 2018
PMID: 30282073
Mitochondrial Ca2+ and regulation of the permeability transition pore.
Hurst S, Hoek J, Sheu SS., J Bioenerg Biomembr 49(1), 2017
PMID: 27497945
Mitochondrial permeability transition in cardiac ischemia-reperfusion: whether cyclophilin D is a viable target for cardioprotection?
Javadov S, Jang S, Parodi-Rullán R, Khuchua Z, Kuznetsov AV., Cell Mol Life Sci 74(15), 2017
PMID: 28378042
European contribution to the study of ROS: A summary of the findings and prospects for the future from the COST action BM1203 (EU-ROS).
Egea J, Fabregat I, Frapart YM, Ghezzi P, Görlach A, Kietzmann T, Kubaichuk K, Knaus UG, Lopez MG, Olaso-Gonzalez G, Petry A, Schulz R, Vina J, Winyard P, Abbas K, Ademowo OS, Afonso CB, Andreadou I, Antelmann H, Antunes F, Aslan M, Bachschmid MM, Barbosa RM, Belousov V, Berndt C, Bernlohr D, Bertrán E, Bindoli A, Bottari SP, Brito PM, Carrara G, Casas AI, Chatzi A, Chondrogianni N, Conrad M, Cooke MS, Costa JG, Cuadrado A, My-Chan Dang P, De Smet B, Debelec-Butuner B, Dias IHK, Dunn JD, Edson AJ, El Assar M, El-Benna J, Ferdinandy P, Fernandes AS, Fladmark KE, Förstermann U, Giniatullin R, Giricz Z, Görbe A, Griffiths H, Hampl V, Hanf A, Herget J, Hernansanz-Agustín P, Hillion M, Huang J, Ilikay S, Jansen-Dürr P, Jaquet V, Joles JA, Kalyanaraman B, Kaminskyy D, Karbaschi M, Kleanthous M, Klotz LO, Korac B, Korkmaz KS, Koziel R, Kračun D, Krause KH, Křen V, Krieg T, Laranjinha J, Lazou A, Li H, Martínez-Ruiz A, Matsui R, McBean GJ, Meredith SP, Messens J, Miguel V, Mikhed Y, Milisav I, Milković L, Miranda-Vizuete A, Mojović M, Monsalve M, Mouthuy PA, Mulvey J, Münzel T, Muzykantov V, Nguyen ITN, Oelze M, Oliveira NG, Palmeira CM, Papaevgeniou N, Pavićević A, Pedre B, Peyrot F, Phylactides M, Pircalabioru GG, Pitt AR, Poulsen HE, Prieto I, Rigobello MP, Robledinos-Antón N, Rodríguez-Mañas L, Rolo AP, Rousset F, Ruskovska T, Saraiva N, Sasson S, Schröder K, Semen K, Seredenina T, Shakirzyanova A, Smith GL, Soldati T, Sousa BC, Spickett CM, Stancic A, Stasia MJ, Steinbrenner H, Stepanić V, Steven S, Tokatlidis K, Tuncay E, Turan B, Ursini F, Vacek J, Vajnerova O, Valentová K, Van Breusegem F, Varisli L, Veal EA, Yalçın AS, Yelisyeyeva O, Žarković N, Zatloukalová M, Zielonka J, Touyz RM, Papapetropoulos A, Grune T, Lamas S, Schmidt HHHW, Di Lisa F, Daiber A., Redox Biol 13(), 2017
PMID: 28577489
Sex difference in the sensitivity of cardiac mitochondrial permeability transition pore to calcium load.
Milerová M, Drahota Z, Chytilová A, Tauchmannová K, Houštěk J, Ošťádal B., Mol Cell Biochem 412(1-2), 2016
PMID: 26715132
Mitochondrial calcium uniporter regulator 1 (MCUR1) regulates the calcium threshold for the mitochondrial permeability transition.
Chaudhuri D, Artiga DJ, Abiria SA, Clapham DE., Proc Natl Acad Sci U S A 113(13), 2016
PMID: 26976564
Mitochondrial Thioredoxin System as a Modulator of Cyclophilin D Redox State.
Folda A, Citta A, Scalcon V, Calì T, Zonta F, Scutari G, Bindoli A, Rigobello MP., Sci Rep 6(), 2016
PMID: 26975474
Mitochondrial Cyclophilin D in Vascular Oxidative Stress and Hypertension.
Itani HA, Dikalova AE, McMaster WG, Nazarewicz RR, Bikineyeva AT, Harrison DG, Dikalov SI., Hypertension 67(6), 2016
PMID: 27067720
Structural mechanisms of cyclophilin D-dependent control of the mitochondrial permeability transition pore.
Gutiérrez-Aguilar M, Baines CP., Biochim Biophys Acta 1850(10), 2015
PMID: 25445707
Mechanisms of cell death pathway activation following drug-induced inhibition of mitochondrial complex I.
Imaizumi N, Kwang Lee K, Zhang C, Boelsterli UA., Redox Biol 4(), 2015
PMID: 25625582
Interactions between mitochondrial reactive oxygen species and cellular glucose metabolism.
Liemburg-Apers DC, Willems PH, Koopman WJ, Grefte S., Arch Toxicol 89(8), 2015
PMID: 26047665
Involvement of the mitochondrial permeability transition pore in chronic ethanol-mediated liver injury in mice.
King AL, Swain TM, Mao Z, Udoh US, Oliva CR, Betancourt AM, Griguer CE, Crowe DR, Lesort M, Bailey SM., Am J Physiol Gastrointest Liver Physiol 306(4), 2014
PMID: 24356880
Proteome analysis reveals roles of L-DOPA in response to oxidative stress in neurons.
Jami MS, Pal R, Hoedt E, Neubert TA, Larsen JP, Møller SG., BMC Neurosci 15(), 2014
PMID: 25082231
Principles in redox signaling: from chemistry to functional significance.
Bindoli A, Rigobello MP., Antioxid Redox Signal 18(13), 2013
PMID: 23244515
Mitochondria as a source of reactive oxygen and nitrogen species: from molecular mechanisms to human health.
Figueira TR, Barros MH, Camargo AA, Castilho RF, Ferreira JC, Kowaltowski AJ, Sluse FE, Souza-Pinto NC, Vercesi AE., Antioxid Redox Signal 18(16), 2013
PMID: 23244576
Implication of cysteine residues in the selection of oxorhenium inhibitors of cyclophilin hCyp18.
Clavaud C, Le Gal J, Thai R, Dugave C., Metallomics 4(2), 2012
PMID: 22273684
Redox regulation of mitochondrial function.
Handy DE, Loscalzo J., Antioxid Redox Signal 16(11), 2012
PMID: 22146081
Oxidative stress modulates mitochondrial failure and cyclophilin D function in X-linked adrenoleukodystrophy.
López-Erauskin J, Galino J, Bianchi P, Fourcade S, Andreu AL, Ferrer I, Muñoz-Pinedo C, Pujol A., Brain 135(pt 12), 2012
PMID: 23250880
Increased propensity for cell death in diabetic human heart is mediated by mitochondrial-dependent pathways.
Anderson EJ, Rodriguez E, Anderson CA, Thayne K, Chitwood WR, Kypson AP., Am J Physiol Heart Circ Physiol 300(1), 2011
PMID: 21076025
Influence of aging on membrane permeability transition in brain mitochondria.
Toman J, Fiskum G., J Bioenerg Biomembr 43(1), 2011
PMID: 21311961
The mitochondrial permeability transition pore and cyclophilin D in cardioprotection.
Di Lisa F, Carpi A, Giorgio V, Bernardi P., Biochim Biophys Acta 1813(7), 2011
PMID: 21295622
Calcium and reactive oxygen species in acute pancreatitis: friend or foe?
Booth DM, Mukherjee R, Sutton R, Criddle DN., Antioxid Redox Signal 15(10), 2011
PMID: 21861696
Cysteine 203 of cyclophilin D is critical for cyclophilin D activation of the mitochondrial permeability transition pore.
Nguyen TT, Stevens MV, Kohr M, Steenbergen C, Sack MN, Murphy E., J Biol Chem 286(46), 2011
PMID: 21930693
Mitochondrial peroxiredoxin involvement in antioxidant defence and redox signalling.
Cox AG, Winterbourn CC, Hampton MB., Biochem J 425(2), 2010
PMID: 20025614
Chronic ethanol consumption enhances sensitivity to Ca(2+)-mediated opening of the mitochondrial permeability transition pore and increases cyclophilin D in liver.
King AL, Swain TM, Dickinson DA, Lesort MJ, Bailey SM., Am J Physiol Gastrointest Liver Physiol 299(4), 2010
PMID: 20651005

39 References

Daten bereitgestellt von Europe PubMed Central.

Catalysis of protein folding by cyclophilins from different species.
Schonbrunner ER, Mayer S, Tropschug M, Fischer G, Takahashi N, Schmid FX., J. Biol. Chem. 266(6), 1991
PMID: 1825312
Cyclophilin: a specific cytosolic binding protein for cyclosporin A.
Handschumacher RE, Harding MW, Rice J, Drugge RJ, Speicher DW., Science 226(4674), 1984
PMID: 6238408
Immunophilins: for the love of proteins.
Barik S., Cell. Mol. Life Sci. 63(24), 2006
PMID: 17075696
Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts.
Gothel SF, Marahiel MA., Cell. Mol. Life Sci. 55(3), 1999
PMID: 10228556
The cyclophilins.
Wang P, Heitman J., Genome Biol. 6(7), 2005
PMID: 15998457
Human cyclophilin B: a second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence.
Price ER, Zydowsky LD, Jin MJ, Baker CH, McKeon FD, Walsh CT., Proc. Natl. Acad. Sci. U.S.A. 88(5), 1991
PMID: 2000394
Crystal engineering yields crystals of cyclophilin D diffracting to 1.7 A resolution.
Schlatter D, Thoma R, Kung E, Stihle M, Muller F, Borroni E, Cesura A, Hennig M., Acta Crystallogr. D Biol. Crystallogr. 61(Pt 5), 2005
PMID: 15858260
Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death.
Baines CP, Kaiser RA, Purcell NH, Blair NS, Osinska H, Hambleton MA, Brunskill EW, Sayen MR, Gottlieb RA, Dorn GW, Robbins J, Molkentin JD., Nature 434(7033), 2005
PMID: 15800627
Properties of the permeability transition pore in mitochondria devoid of Cyclophilin D.
Basso E, Fante L, Fowlkes J, Petronilli V, Forte MA, Bernardi P., J. Biol. Chem. 280(19), 2005
PMID: 15792954
Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death.
Nakagawa T, Shimizu S, Watanabe T, Yamaguchi O, Otsu K, Yamagata H, Inohara H, Kubo T, Tsujimoto Y., Nature 434(7033), 2005
PMID: 15800626
Cyclophilin catalyzes protein folding in yeast mitochondria.
Matouschek A, Rospert S, Schmid K, Glick BS, Schatz G., Proc. Natl. Acad. Sci. U.S.A. 92(14), 1995
PMID: 7603990
The mitochondrial permeability transition pore.
Crompton M, Virji S, Doyle V, Johnson N, Ward JM., Biochem. Soc. Symp. 66(), 1999
PMID: 10989666
Biochemistry: a pore way to die.
Halestrap A., Nature 434(7033), 2005
PMID: 15800609
The permeability transition pore complex: another view.
Halestrap AP, McStay GP, Clarke SJ., Biochimie 84(2-3), 2002
PMID: 12022946
Suppression of cyclophilin-A activity in rat cardiomyocytes.
Doyle V, Virji S, Crompton M., Biochem. Soc. Trans. 26(4), 1998
PMID: 10047842
Cyclophilin-D promotes the mitochondrial permeability transition but has opposite effects on apoptosis and necrosis.
Li Y, Johnson N, Capano M, Edwards M, Crompton M., Biochem. J. 383(Pt 1), 2004
PMID: 15233627
Cloning and characterization of a 2-Cys peroxiredoxin from Pisum sativum.
Bernier-Villamor L, Navarro E, Sevilla F, Lazaro JJ., J. Exp. Bot. 55(406), 2004
PMID: 15333640
Cyclophilin a binds to peroxiredoxins and activates its peroxidase activity.
Lee SP, Hwang YS, Kim YJ, Kwon KS, Kim HJ, Kim K, Chae HZ., J. Biol. Chem. 276(32), 2001
PMID: 11390385
Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin family.
Knoops B, Clippe A, Bogard C, Arsalane K, Wattiez R, Hermans C, Duconseille E, Falmagne P, Bernard A., J. Biol. Chem. 274(43), 1999
PMID: 10521424
Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 A resolution.
Declercq JP, Evrard C, Clippe A, Stricht DV, Bernard A, Knoops B., J. Mol. Biol. 311(4), 2001
PMID: 11518528
Chloroplast cyclophilin is a target protein of thioredoxin. Thiol modulation of the peptidyl-prolyl cis-trans isomerase activity.
Motohashi K, Koyama F, Nakanishi Y, Ueoka-Nakanishi H, Hisabori T., J. Biol. Chem. 278(34), 2003
PMID: 12923164
Oxidation-reduction properties of chloroplast thioredoxins, ferredoxin:thioredoxin reductase, and thioredoxin f-regulated enzymes.
Hirasawa M, Schurmann P, Jacquot JP, Manieri W, Jacquot P, Keryer E, Hartman FC, Knaff DB., Biochemistry 38(16), 1999
PMID: 10213627
Proteome map of the chloroplast lumen of Arabidopsis thaliana.
Schubert M, Petersson UA, Haas BJ, Funk C, Schroder WP, Kieselbach T., J. Biol. Chem. 277(10), 2001
PMID: 11719511
Active site mutants of human cyclophilin A separate peptidyl-prolyl isomerase activity from cyclosporin A binding and calcineurin inhibition.
Zydowsky LD, Etzkorn FA, Chang HY, Ferguson SB, Stolz LA, Ho SI, Walsh CT., Protein Sci. 1(9), 1992
PMID: 1338979
Redox regulation of cyclophilin A by glutathionylation.
Ghezzi P, Casagrande S, Massignan T, Basso M, Bellacchio E, Mollica L, Biasini E, Tonelli R, Eberini I, Gianazza E, Dai WW, Fratelli M, Salmona M, Sherry B, Bonetto V., Proteomics 6(3), 2006
PMID: 16372262
Mechanisms of tryptophan fluorescence shifts in proteins.
Vivian JT, Callis PR., Biophys. J. 80(5), 2001
PMID: 11325713
Pin1 in Alzheimer's disease.
Butterfield DA, Abdul HM, Opii W, Newman SF, Joshi G, Ansari MA, Sultana R., J. Neurochem. 98(6), 2006
PMID: 16945100

Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®

Quellen

PMID: 19735641
PubMed | Europe PMC

Suchen in

Google Scholar