ArticlePloS one2015
A New APEH Cluster with Antioxidant Functions in the Antarctic Hemoglobinless Icefish Chionodraco hamatus.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 17 citations in OpenAlex.
- Chromosome-scale genome assembly and annotation of Jonah's icefish Neopagetopsis ionah.Scientific data · 2026Article
- Ligand binding Pro-miscuity of acylpeptide hydrolase, structural analysis of a detoxifying serine hydrolase.Protein science : a publication of the Protein Society · 2025Article
- Acylamino acid-releasing enzyme, a bifunctional protease with a potential role in aging.Journal of experimental botany · 2025Review
- A deeply conserved protease, acylamino acid-releasing enzyme (AARE), acts in ageing in Physcomitrella and Arabidopsis.Communications biology · 2023Article
- A strategy to recover a poor-quality ligase product.Journal of biological methods · 2023Article
- In Vitro Assays for the Bifunctional Acylpeptide Hydrolase (APEH) Enzyme from Antarctic Fish.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Oxidized Substrates of APEH as a Tool to Study the Endoprotease Activity of the Enzyme.International journal of molecular sciences · 2021Article
- The loss of hemoglobin and myoglobin does not minimize oxidative stress in Antarctic icefishes.The Journal of experimental biology · 2018Article
- Unusual Antioxidant Properties of 26S Proteasome Isolated from Cold-Adapted Organisms.International journal of molecular sciences · 2017Article
- APEH Inhibition Affects Osteosarcoma Cell Viability via Downregulation of the Proteasome.International journal of molecular sciences · 2016Article
- Uncommon functional properties of the first piscine 26S proteasome from the Antarctic notothenioid Trematomus bernacchii.Bioscience reports · 2016Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
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Abstract
Acylpeptide hydrolase (APEH) is a ubiquitous cytosolic protease that plays an important role in the detoxification of oxidised proteins. In this work, to further explore the physiological role of this enzyme, two apeh cDNAs were isolated from the Chionodraco hamatus icefish, which lives in the highly oxygenated Antarctic marine environment. The encoded proteins (APEH-1(Ch) and APEH-2(Ch)) were characterised in comparison with the uniquely expressed isoform from the temperate fish Dicentrarchus labrax (APEH-1Dl) and the two APEHs from the red-blooded Antarctic fish Trematomus bernacchii (APEH-1(Tb) and APEH-2(Tb)). Homology modelling and kinetic characterisation of the APEH isoforms provided new insights into their structure/function properties. APEH-2 isoforms were the only ones capable of hydrolysing oxidised proteins, with APEH-2(Ch) being more efficient than APEH-2(Tb) at this specific function. Therefore, this ability of APEH-2 isoforms is the result of an evolutionary adaptation due to the pressure of a richly oxygenated environment. The lack of expression of APEH-2 in the tissues of the temperate fish used as the controls further supported this hypothesis. In addition, analysis of gene expression showed a significant discrepancy between the levels of transcripts and those of proteins, especially for apeh-2 genes, which suggests the presence of post-transcriptional regulation mechanisms, triggered by cold-induced oxidative stress, that produce high basal levels of APEH-2 mRNA as a reserve that is ready to use in case of the accumulation of oxidised proteins.
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