Modification of permeability transition pore arginine(s) by phenylglyoxal derivatives in isolated mitochondria and mammalian cells. Structure-function relationship of arginine ligands - PubMed (original) (raw)
. 2005 Apr 1;280(13):12130-6.
doi: 10.1074/jbc.M413454200. Epub 2005 Jan 24.
Eva Milanesi, Marina Franck, Christoffer Johans, Julius Liobikas, Maria Panagiotaki, Lucedio Greci, Giovanni Principato, Paavo K J Kinnunen, Paolo Bernardi, Paola Costantini, Ove Eriksson
Affiliations
- PMID: 15671016
- DOI: 10.1074/jbc.M413454200
Free article
Modification of permeability transition pore arginine(s) by phenylglyoxal derivatives in isolated mitochondria and mammalian cells. Structure-function relationship of arginine ligands
Milena Johans et al. J Biol Chem. 2005.
Free article
Abstract
Methylglyoxal and synthetic glyoxal derivatives react covalently with arginine residue(s) on the mitochondrial permeability transition pore (PTP). In this study, we have investigated how the binding of a panel of synthetic phenylglyoxal derivatives influences the opening and closing of the PTP. Using both isolated mitochondria and mammalian cells, we demonstrate that the resulting arginine-phenylglyoxal adduct can lead to either suppression or induction of permeability transition, depending on the net charge and hydrogen bonding capacity of the adduct. We report that phenylglyoxal derivatives that possess a net negative charge and/or are capable of forming hydrogen bonds induced permeability transition. Derivatives that were overall electroneutral and cannot form hydrogen bonds suppressed permeability transition. When mammalian cells were incubated with low concentrations of negatively charged phenylglyoxal derivatives, the addition of oligomycin caused a depolarization of the mitochondrial membrane potential. This depolarization was completely blocked by cyclosporin A, a PTP opening inhibitor, indicating that the depolarization was due to PTP opening. Collectively, these findings highlight that the target arginine(s) is functionally linked with the opening/closing mechanism of the PTP and that the electric charge and hydrogen bonding of the resulting arginine adduct influences the conformation of the PTP. These results are consistent with a model where the target arginine plays a role as a voltage sensor.
Similar articles
- Ligand-selective modulation of the permeability transition pore by arginine modification. Opposing effects of p-hydroxyphenylglyoxal and phenylglyoxal.
Linder MD, Morkunaite-Haimi S, Kinnunen PK, Bernardi P, Eriksson O. Linder MD, et al. J Biol Chem. 2002 Jan 11;277(2):937-42. doi: 10.1074/jbc.M107610200. Epub 2001 Nov 6. J Biol Chem. 2002. PMID: 11698400 - Inhibition of the mitochondrial cyclosporin A-sensitive permeability transition pore by the arginine reagent phenylglyoxal.
Eriksson O, Fontaine E, Petronilli V, Bernardi P. Eriksson O, et al. FEBS Lett. 1997 Jun 16;409(3):361-4. doi: 10.1016/s0014-5793(97)00549-8. FEBS Lett. 1997. PMID: 9224690 - Chemical modification of arginines by 2,3-butanedione and phenylglyoxal causes closure of the mitochondrial permeability transition pore.
Eriksson O, Fontaine E, Bernardi P. Eriksson O, et al. J Biol Chem. 1998 May 15;273(20):12669-74. doi: 10.1074/jbc.273.20.12669. J Biol Chem. 1998. PMID: 9575230 - Recent progress on regulation of the mitochondrial permeability transition pore; a cyclosporin-sensitive pore in the inner mitochondrial membrane.
Bernardi P, Broekemeier KM, Pfeiffer DR. Bernardi P, et al. J Bioenerg Biomembr. 1994 Oct;26(5):509-17. doi: 10.1007/BF00762735. J Bioenerg Biomembr. 1994. PMID: 7896766 Review. - Amyloid β, α-synuclein and the c subunit of the ATP synthase: Can these peptides reveal an amyloidogenic pathway of the permeability transition pore?
Amodeo GF, Pavlov EV. Amodeo GF, et al. Biochim Biophys Acta Biomembr. 2021 Mar 1;1863(3):183531. doi: 10.1016/j.bbamem.2020.183531. Epub 2020 Dec 10. Biochim Biophys Acta Biomembr. 2021. PMID: 33309700 Review.
Cited by
- Modulation and Pharmacology of the Mitochondrial Permeability Transition: A Journey from F-ATP Synthase to ANT.
Carrer A, Laquatra C, Tommasin L, Carraro M. Carrer A, et al. Molecules. 2021 Oct 26;26(21):6463. doi: 10.3390/molecules26216463. Molecules. 2021. PMID: 34770872 Free PMC article. Review. - The mitochondrial permeability transition: Recent progress and open questions.
Bernardi P, Carraro M, Lippe G. Bernardi P, et al. FEBS J. 2022 Nov;289(22):7051-7074. doi: 10.1111/febs.16254. Epub 2021 Nov 12. FEBS J. 2022. PMID: 34710270 Free PMC article. Review. - The Mitochondrial Permeability Transition in Mitochondrial Disorders.
Šileikytė J, Forte M. Šileikytė J, et al. Oxid Med Cell Longev. 2019 May 5;2019:3403075. doi: 10.1155/2019/3403075. eCollection 2019. Oxid Med Cell Longev. 2019. PMID: 31191798 Free PMC article. Review. - Why F-ATP Synthase Remains a Strong Candidate as the Mitochondrial Permeability Transition Pore.
Bernardi P. Bernardi P. Front Physiol. 2018 Nov 1;9:1543. doi: 10.3389/fphys.2018.01543. eCollection 2018. Front Physiol. 2018. PMID: 30443222 Free PMC article. No abstract available. - Arginine 107 of yeast ATP synthase subunit g mediates sensitivity of the mitochondrial permeability transition to phenylglyoxal.
Guo L, Carraro M, Sartori G, Minervini G, Eriksson O, Petronilli V, Bernardi P. Guo L, et al. J Biol Chem. 2018 Sep 21;293(38):14632-14645. doi: 10.1074/jbc.RA118.004495. Epub 2018 Aug 9. J Biol Chem. 2018. PMID: 30093404 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources