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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ftunivnapoliiris:oai:www.iris.unina.it:11588/365483 2024-09-09T19:30:32+00:00 Ribonucleases with angiogenic and bactericidal activities from the Atlantic salmon PIZZO, ELIODORO VARCAMONTI, MARIO GIANCOLA, CONCETTA D'ALESSIO, GIUSEPPE Di Maro A. ZANFARDINO, ANNA Pizzo, Eliodoro Varcamonti, Mario Di Maro, A. Zanfardino, Anna Giancola, Concetta D'Alessio, Giuseppe 2008 STAMPA http://hdl.handle.net/11588/365483 https://doi.org/10.1111/j.1742-4658.2008.06289.x eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:000253758200021 volume:275 issue:14 firstpage:1283 lastpage:1295 numberofpages:13 journal:THE FEBS JOURNAL http://hdl.handle.net/11588/365483 doi:10.1111/j.1742-4658.2008.06289.x info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-40349089989 info:eu-repo/semantics/closedAccess info:eu-repo/semantics/article 2008 ftunivnapoliiris https://doi.org/10.1111/j.1742-4658.2008.06289.x 2024-06-17T15:19:26Z 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 IRIS Università degli Studi di Napoli Federico II FEBS Journal 275 6 1283 1295 |
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Open Polar |
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IRIS Università degli Studi di Napoli Federico II |
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ftunivnapoliiris |
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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. |
author2 |
Pizzo, Eliodoro Varcamonti, Mario Di Maro, A. Zanfardino, Anna Giancola, Concetta D'Alessio, Giuseppe |
format |
Article in Journal/Newspaper |
author |
PIZZO, ELIODORO VARCAMONTI, MARIO GIANCOLA, CONCETTA D'ALESSIO, GIUSEPPE Di Maro A. ZANFARDINO, ANNA |
spellingShingle |
PIZZO, ELIODORO VARCAMONTI, MARIO GIANCOLA, CONCETTA D'ALESSIO, GIUSEPPE Di Maro A. ZANFARDINO, ANNA Ribonucleases with angiogenic and bactericidal activities from the Atlantic salmon |
author_facet |
PIZZO, ELIODORO VARCAMONTI, MARIO GIANCOLA, CONCETTA D'ALESSIO, GIUSEPPE Di Maro A. ZANFARDINO, ANNA |
author_sort |
PIZZO, ELIODORO |
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 |
publishDate |
2008 |
url |
http://hdl.handle.net/11588/365483 https://doi.org/10.1111/j.1742-4658.2008.06289.x |
genre |
Atlantic salmon |
genre_facet |
Atlantic salmon |
op_relation |
info:eu-repo/semantics/altIdentifier/wos/WOS:000253758200021 volume:275 issue:14 firstpage:1283 lastpage:1295 numberofpages:13 journal:THE FEBS JOURNAL http://hdl.handle.net/11588/365483 doi:10.1111/j.1742-4658.2008.06289.x info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-40349089989 |
op_rights |
info:eu-repo/semantics/closedAccess |
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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1809899516314255360 |