Arg354 in the catalytic centre of bovine liver catalase is protected from methylglyoxal-mediated glycation

  • Background: In addition to controlled post-translational modifications proteins can be modified with highly reactive compounds. Usually this leads to a compromised functionality of the protein. Methylglyoxal is one of the most common agents that attack arginine residues. Methylglyoxal is also regarded as a pro-oxidant that affects cellular redox homeostasis by contributing to the formation of reactive oxygen species. Antioxidant enzymes like catalase are required to protect the cell from oxidative damage. These enzymes are also targets for methylglyoxal-mediated modification which could severely affect their catalytic activity in breaking down reactive oxygen species to less reactive or inert compounds. Results: Here, bovine liver catalase was incubated with high levels of methylglyoxal to induce its glycation. This treatment did not lead to a pronounced reduction of enzymatic activity. Subsequently methylglyoxal-mediated arginine modifications (hydroimidazolone and dihydroxyimidazolidine) were quantitatively analysed by sensitive nano high performance liquid chromatography/electron spray ionisation/tandem mass spectrometry. Whereas several arginine residues displayed low to moderate levels of glycation (e.g., Arg93, Arg365, Arg444) Arg354 in the active centre of catalase was never found to be modified. Conclusions: Bovine liver catalase is able to tolerate very high levels of the modifying α-oxoaldehyde methylglyoxal so that its essential enzymatic function is not impaired. Electronic supplementary material: The online version of this article (doi:10.1186/s13104-015-1793-5) contains supplementary material, which is available to authorized users.

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Metadaten
Author:Christian Quintus Scheckhuber
URN:urn:nbn:de:hebis:30:3-397445
DOI:https://doi.org/10.1186/s13104-015-1793-5
ISSN:1756-0500
Parent Title (English):BMC Research Notes
Publisher:BioMed Central
Place of publication:London
Document Type:Part of Periodical
Language:English
Date of Publication (online):2016/12/08
Year of first Publication:2015
Publishing Institution:Universitätsbibliothek Johann Christian Senckenberg
Release Date:2016/12/08
Tag:Arginine; Bovine liver catalase; Dihydroxyimidazolidine; Glycation; Hydroimidazolone; Methylglyoxal; Modification
Volume:8
Issue:830
Page Number:6
Note:
© 2015 Scheckhuber. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
Institutes:Angeschlossene und kooperierende Institutionen / Senckenbergische Naturforschende Gesellschaft
Wissenschaftliche Zentren und koordinierte Programme / LOEWE-Schwerpunkt für Integrative Pilzforschung
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Sammlungen:Universitätspublikationen
Licence (German):License LogoCreative Commons - Namensnennung 4.0