Senckenbergische Naturforschende Gesellschaft
Refine
Document Type
- Part of Periodical (2) (remove)
Language
- English (2)
Has Fulltext
- yes (2)
Is part of the Bibliography
- no (2)
Keywords
- Arginine (1)
- Atlantic (1)
- Bovine liver catalase (1)
- Dihydroxyimidazolidine (1)
- Glycation (1)
- Hydroimidazolone (1)
- Mauretanaspis longichaeta gen. et spec. nov. (1)
- Methylglyoxal (1)
- Modification (1)
- deep sea (1)
A new genus and species of Sternaspidae (Annelida: Polychaeta) from the deep eastern Atlantic
(2020)
Based on specimens recently collected in sediments from 2700 m depth off Mauritania (Northwest Africa; type locality) and from 2700–4400 m depth off Angola (Southwest Africa), a new genus and species, Mauretanaspis longichaeta gen. et spec. nov., is described. The new genus and species are characterized by a unique combination of characters: ventro-caudal shield covered by firmly adhering sediment, lateral margins strongly bent and merging into integument; introvert hooks tapering; eight pre-shield segments; absence of peg chaetae; exceptionally long posteriormost lateral chaetae equaling body length; posterior shield chaetae equaling shield length. A comparative table of characters for all currently recognised sternaspid genera and a key to all species with ventro-caudal shield covered by firmly adhering sediment are provided.
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.