A novel class of bifunctional acylpeptide hydrolases – potential role in the antioxidant defense systems of the Antarctic fish Trematomus bernacchii
Oxidative challenge is an important factor affecting the adaptive strategies of Antarctic fish, but data on antioxidant defenses in these organisms remain scarce. In this context, a key role could be played by acylpeptide hydrolase ( APEH ), which was recently hypothesized to participate in the degr...
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crwiley:10.1111/febs.12610 2024-06-23T07:47:59+00:00 A novel class of bifunctional acylpeptide hydrolases – potential role in the antioxidant defense systems of the Antarctic fish Trematomus bernacchii Gogliettino, Marta Riccio, Alessia Balestrieri, Marco Cocca, Ennio Facchiano, Angelo D'Arco, Teresa M. Tesoro, Clara Rossi, Mosè Palmieri, Gianna 2013 http://dx.doi.org/10.1111/febs.12610 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Ffebs.12610 https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/febs.12610 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor The FEBS Journal volume 281, issue 1, page 401-415 ISSN 1742-464X 1742-4658 journal-article 2013 crwiley https://doi.org/10.1111/febs.12610 2024-06-11T04:41:28Z Oxidative challenge is an important factor affecting the adaptive strategies of Antarctic fish, but data on antioxidant defenses in these organisms remain scarce. In this context, a key role could be played by acylpeptide hydrolase ( APEH ), which was recently hypothesized to participate in the degradation of oxidized and cytotoxic proteins, although its physiological function is still not fully clarified. This study represents the first report on piscine members of this enzyme family, specifically from the Antarctic teleost Trematomus bernacchii . The c DNA s corresponding to two apeh genes were isolated, and the respective proteins were functionally and structurally characterized with the aim of understanding the biological significance of these proteases in Antarctic fish. Both APEH isoforms ( APEH ‐1 Tb and APEH ‐2 Tb ) showed distinct temperature‐kinetic behavior, with significant differences in the K m values. Moreover, beside the typical acylpeptide hydrolase activity, APEH ‐2 Tb showed remarkable oxidized protein endohydrolase activity towards oxidized BSA , suggesting that this isoform could play a homeostatic role in removing oxidatively damaged proteins, sustaining the antioxidant defense systems. The 3D structures of both APEH s were predicted, and a possible relationship was found between the substrate specificity/affinity and the marked changes in the number of charged residues and hydrophobicity properties surrounding their catalytic sites. Our results demonstrated the occurrence of two APEH isoforms in T. bernacchii , belonging to different phylogenetic clusters, identified for the first time, and showing distinct molecular and temperature–kinetic behaviors. In addition, we suggest that the members of the new cluster ‘ APEH ‐2’ could participate in reactive oxygen species detoxification as phase 3 antioxidant enzymes, enhancing the protein degradation machinery. Article in Journal/Newspaper Antarc* Antarctic Wiley Online Library Antarctic The Antarctic FEBS Journal 281 1 401 415 |
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Open Polar |
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Wiley Online Library |
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crwiley |
language |
English |
description |
Oxidative challenge is an important factor affecting the adaptive strategies of Antarctic fish, but data on antioxidant defenses in these organisms remain scarce. In this context, a key role could be played by acylpeptide hydrolase ( APEH ), which was recently hypothesized to participate in the degradation of oxidized and cytotoxic proteins, although its physiological function is still not fully clarified. This study represents the first report on piscine members of this enzyme family, specifically from the Antarctic teleost Trematomus bernacchii . The c DNA s corresponding to two apeh genes were isolated, and the respective proteins were functionally and structurally characterized with the aim of understanding the biological significance of these proteases in Antarctic fish. Both APEH isoforms ( APEH ‐1 Tb and APEH ‐2 Tb ) showed distinct temperature‐kinetic behavior, with significant differences in the K m values. Moreover, beside the typical acylpeptide hydrolase activity, APEH ‐2 Tb showed remarkable oxidized protein endohydrolase activity towards oxidized BSA , suggesting that this isoform could play a homeostatic role in removing oxidatively damaged proteins, sustaining the antioxidant defense systems. The 3D structures of both APEH s were predicted, and a possible relationship was found between the substrate specificity/affinity and the marked changes in the number of charged residues and hydrophobicity properties surrounding their catalytic sites. Our results demonstrated the occurrence of two APEH isoforms in T. bernacchii , belonging to different phylogenetic clusters, identified for the first time, and showing distinct molecular and temperature–kinetic behaviors. In addition, we suggest that the members of the new cluster ‘ APEH ‐2’ could participate in reactive oxygen species detoxification as phase 3 antioxidant enzymes, enhancing the protein degradation machinery. |
format |
Article in Journal/Newspaper |
author |
Gogliettino, Marta Riccio, Alessia Balestrieri, Marco Cocca, Ennio Facchiano, Angelo D'Arco, Teresa M. Tesoro, Clara Rossi, Mosè Palmieri, Gianna |
spellingShingle |
Gogliettino, Marta Riccio, Alessia Balestrieri, Marco Cocca, Ennio Facchiano, Angelo D'Arco, Teresa M. Tesoro, Clara Rossi, Mosè Palmieri, Gianna A novel class of bifunctional acylpeptide hydrolases – potential role in the antioxidant defense systems of the Antarctic fish Trematomus bernacchii |
author_facet |
Gogliettino, Marta Riccio, Alessia Balestrieri, Marco Cocca, Ennio Facchiano, Angelo D'Arco, Teresa M. Tesoro, Clara Rossi, Mosè Palmieri, Gianna |
author_sort |
Gogliettino, Marta |
title |
A novel class of bifunctional acylpeptide hydrolases – potential role in the antioxidant defense systems of the Antarctic fish Trematomus bernacchii |
title_short |
A novel class of bifunctional acylpeptide hydrolases – potential role in the antioxidant defense systems of the Antarctic fish Trematomus bernacchii |
title_full |
A novel class of bifunctional acylpeptide hydrolases – potential role in the antioxidant defense systems of the Antarctic fish Trematomus bernacchii |
title_fullStr |
A novel class of bifunctional acylpeptide hydrolases – potential role in the antioxidant defense systems of the Antarctic fish Trematomus bernacchii |
title_full_unstemmed |
A novel class of bifunctional acylpeptide hydrolases – potential role in the antioxidant defense systems of the Antarctic fish Trematomus bernacchii |
title_sort |
novel class of bifunctional acylpeptide hydrolases – potential role in the antioxidant defense systems of the antarctic fish trematomus bernacchii |
publisher |
Wiley |
publishDate |
2013 |
url |
http://dx.doi.org/10.1111/febs.12610 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Ffebs.12610 https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/febs.12610 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
The FEBS Journal volume 281, issue 1, page 401-415 ISSN 1742-464X 1742-4658 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1111/febs.12610 |
container_title |
FEBS Journal |
container_volume |
281 |
container_issue |
1 |
container_start_page |
401 |
op_container_end_page |
415 |
_version_ |
1802638309937119232 |