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.
Zeitschriftenaufsatz
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Autor*in
Linard, Dominique;
Kandlbinder, AndreaUniBi;
Degand, Herve;
Morsomme, Pierre;
Dietz, Karl-JosefUniBi;
Knoops, Bernard
Einrichtung
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.
Stichworte
Cyclophilin;
Oxidative stress;
Redox sensor;
Mitochondria
Erscheinungsjahr
2009
Zeitschriftentitel
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Band
491
Ausgabe
1-2
Seite(n)
39-45
ISSN
0003-9861
Page URI
https://pub.uni-bielefeld.de/record/1589748
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. https://doi.org/10.1016/j.abb.2009.09.002
Linard, Dominique, Kandlbinder, Andrea, Degand, Herve, Morsomme, Pierre, Dietz, Karl-Josef, and Knoops, Bernard. 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.
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.
Daten bereitgestellt von European Bioinformatics Institute (EBI)
UNIPROT
5 Einträge gefunden, die diesen Artikel zitieren
Peptidyl-prolyl cis-trans isomerase D (UNIPROT: E5KN55)
Organism: Homo sapiens
Download in FASTA format
Organism: Homo sapiens
Download in FASTA format
Peptidyl-prolyl cis-trans isomerase D (UNIPROT: E5KN59)
Organism: Homo sapiens
Download in FASTA format
Organism: Homo sapiens
Download in FASTA format
Peptidyl-prolyl cis-trans isomerase D (UNIPROT: Q08752)
Organism: Homo sapiens
Download in FASTA format
Organism: Homo sapiens
Download in FASTA format
Peptidyl-prolyl cis-trans isomerase (UNIPROT: Q05DH6)
Organism: Homo sapiens
Download in FASTA format
Organism: Homo sapiens
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