Ribonucleases with angiogenic and bactericidal activities from the Atlantic salmon

The importance of fish in vertebrate evolution has been better recognized in recent years after the intense work carried out on fish genomics. The recent discovery that fish genomes comprise homologs of ribonucleases, studied before only in tetrapods, and the isolation of ribonucleases from zebrafis...

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Published in:FEBS Journal
Main Authors: Pizzo, Elio, Varcamonti, Mario, Maro, Antimo D., Zanfardino, Anna, Giancola, Concetta, D’Alessio, Giuseppe
Format: Article in Journal/Newspaper
Language:English
Published: Wiley 2008
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Online Access:http://dx.doi.org/10.1111/j.1742-4658.2008.06289.x
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spelling crwiley:10.1111/j.1742-4658.2008.06289.x 2024-06-23T07:51:19+00:00 Ribonucleases with angiogenic and bactericidal activities from the Atlantic salmon Pizzo, Elio Varcamonti, Mario Maro, Antimo D. Zanfardino, Anna Giancola, Concetta D’Alessio, Giuseppe 2008 http://dx.doi.org/10.1111/j.1742-4658.2008.06289.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1742-4658.2008.06289.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1742-4658.2008.06289.x en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor The FEBS Journal volume 275, issue 6, page 1283-1295 ISSN 1742-464X 1742-4658 journal-article 2008 crwiley https://doi.org/10.1111/j.1742-4658.2008.06289.x 2024-06-11T04:42:25Z The importance of fish in vertebrate evolution has been better recognized in recent years after the intense work carried out on fish genomics. The recent discovery that fish genomes comprise homologs of ribonucleases, studied before only in tetrapods, and the isolation of ribonucleases from zebrafish have suggested an experimental model for studying fish and vertebrate evolution. Thus, the cDNAs encoding the RNases from the Atlantic salmon were expressed, and the recombinant RNases (Ss‐RNase‐1 and Ss‐RNase‐2) were isolated and characterized as both proteins and for their biological activities. Salmon RNases are less active than RNase A in degrading RNA, but are both sensitive to the action of the human cytosolic RNase inhibitor. The two enzymes possess both angiogenic and bactericidal activities. However, catalytically inactivated Ss‐RNases do not exert any angiogenic activity, but preserve their full bactericidal activity, which is surprisingly preserved even when the enzyme proteins are fully denatured. Analyses of the conformational stability of the two RNases has revealed that they are as stable as typical RNases of the superfamily, and Ss‐RNase‐2, the most active as an enzyme, is also the most resistant to thermal and chemical denaturation. The implications of these findings in terms of the evolution of early RNases, in particular of the physiological significance of the angiogenic and bactericidal activities of fish RNases, are analyzed and discussed. Article in Journal/Newspaper Atlantic salmon Wiley Online Library FEBS Journal 275 6 1283 1295
institution Open Polar
collection Wiley Online Library
op_collection_id crwiley
language English
description The importance of fish in vertebrate evolution has been better recognized in recent years after the intense work carried out on fish genomics. The recent discovery that fish genomes comprise homologs of ribonucleases, studied before only in tetrapods, and the isolation of ribonucleases from zebrafish have suggested an experimental model for studying fish and vertebrate evolution. Thus, the cDNAs encoding the RNases from the Atlantic salmon were expressed, and the recombinant RNases (Ss‐RNase‐1 and Ss‐RNase‐2) were isolated and characterized as both proteins and for their biological activities. Salmon RNases are less active than RNase A in degrading RNA, but are both sensitive to the action of the human cytosolic RNase inhibitor. The two enzymes possess both angiogenic and bactericidal activities. However, catalytically inactivated Ss‐RNases do not exert any angiogenic activity, but preserve their full bactericidal activity, which is surprisingly preserved even when the enzyme proteins are fully denatured. Analyses of the conformational stability of the two RNases has revealed that they are as stable as typical RNases of the superfamily, and Ss‐RNase‐2, the most active as an enzyme, is also the most resistant to thermal and chemical denaturation. The implications of these findings in terms of the evolution of early RNases, in particular of the physiological significance of the angiogenic and bactericidal activities of fish RNases, are analyzed and discussed.
format Article in Journal/Newspaper
author Pizzo, Elio
Varcamonti, Mario
Maro, Antimo D.
Zanfardino, Anna
Giancola, Concetta
D’Alessio, Giuseppe
spellingShingle Pizzo, Elio
Varcamonti, Mario
Maro, Antimo D.
Zanfardino, Anna
Giancola, Concetta
D’Alessio, Giuseppe
Ribonucleases with angiogenic and bactericidal activities from the Atlantic salmon
author_facet Pizzo, Elio
Varcamonti, Mario
Maro, Antimo D.
Zanfardino, Anna
Giancola, Concetta
D’Alessio, Giuseppe
author_sort Pizzo, Elio
title Ribonucleases with angiogenic and bactericidal activities from the Atlantic salmon
title_short Ribonucleases with angiogenic and bactericidal activities from the Atlantic salmon
title_full Ribonucleases with angiogenic and bactericidal activities from the Atlantic salmon
title_fullStr Ribonucleases with angiogenic and bactericidal activities from the Atlantic salmon
title_full_unstemmed Ribonucleases with angiogenic and bactericidal activities from the Atlantic salmon
title_sort ribonucleases with angiogenic and bactericidal activities from the atlantic salmon
publisher Wiley
publishDate 2008
url http://dx.doi.org/10.1111/j.1742-4658.2008.06289.x
https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1742-4658.2008.06289.x
https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1742-4658.2008.06289.x
genre Atlantic salmon
genre_facet Atlantic salmon
op_source The FEBS Journal
volume 275, issue 6, page 1283-1295
ISSN 1742-464X 1742-4658
op_rights http://onlinelibrary.wiley.com/termsAndConditions#vor
op_doi https://doi.org/10.1111/j.1742-4658.2008.06289.x
container_title FEBS Journal
container_volume 275
container_issue 6
container_start_page 1283
op_container_end_page 1295
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