A New APEH Cluster with Antioxidant Functions in the Antarctic Hemoglobinless Icefish Chionodraco hamatus

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 highl...

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Main Authors: Riccio, Alessia, Gogliettino, Marta, Palmieri, Gianna, Balestrieri, Marco, Facchiano, Angelo, Rossi, Mosè, Palumbo, Stefania, Monti, Giuseppe, Cocca, Ennio
Format: Online
Language:English
Published: Public Library of Science 2015
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4422685/
id pubmed-4422685
recordtype oai_dc
spelling pubmed-44226852015-05-12 A New APEH Cluster with Antioxidant Functions in the Antarctic Hemoglobinless Icefish Chionodraco hamatus Riccio, Alessia Gogliettino, Marta Palmieri, Gianna Balestrieri, Marco Facchiano, Angelo Rossi, Mosè Palumbo, Stefania Monti, Giuseppe Cocca, Ennio Research Article 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-1Ch and APEH-2Ch) 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-1Tb and APEH-2Tb). 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-2Ch being more efficient than APEH-2Tb 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. Public Library of Science 2015-05-06 /pmc/articles/PMC4422685/ /pubmed/25946123 http://dx.doi.org/10.1371/journal.pone.0125594 Text en © 2015 Riccio et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Riccio, Alessia
Gogliettino, Marta
Palmieri, Gianna
Balestrieri, Marco
Facchiano, Angelo
Rossi, Mosè
Palumbo, Stefania
Monti, Giuseppe
Cocca, Ennio
spellingShingle Riccio, Alessia
Gogliettino, Marta
Palmieri, Gianna
Balestrieri, Marco
Facchiano, Angelo
Rossi, Mosè
Palumbo, Stefania
Monti, Giuseppe
Cocca, Ennio
A New APEH Cluster with Antioxidant Functions in the Antarctic Hemoglobinless Icefish Chionodraco hamatus
author_facet Riccio, Alessia
Gogliettino, Marta
Palmieri, Gianna
Balestrieri, Marco
Facchiano, Angelo
Rossi, Mosè
Palumbo, Stefania
Monti, Giuseppe
Cocca, Ennio
author_sort Riccio, Alessia
title A New APEH Cluster with Antioxidant Functions in the Antarctic Hemoglobinless Icefish Chionodraco hamatus
title_short A New APEH Cluster with Antioxidant Functions in the Antarctic Hemoglobinless Icefish Chionodraco hamatus
title_full A New APEH Cluster with Antioxidant Functions in the Antarctic Hemoglobinless Icefish Chionodraco hamatus
title_fullStr A New APEH Cluster with Antioxidant Functions in the Antarctic Hemoglobinless Icefish Chionodraco hamatus
title_full_unstemmed A New APEH Cluster with Antioxidant Functions in the Antarctic Hemoglobinless Icefish Chionodraco hamatus
title_sort new apeh cluster with antioxidant functions in the antarctic hemoglobinless icefish chionodraco hamatus
description 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-1Ch and APEH-2Ch) 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-1Tb and APEH-2Tb). 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-2Ch being more efficient than APEH-2Tb 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.
publisher Public Library of Science
publishDate 2015
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4422685/
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