Myoglobin enhances cardiac performance in antarctic icefish species that express the protein
Channichthyid icefishes of Antarctica are unique among adult vertebrates. All icefish species lack hemoglobin and red blood cells in their circulating blood. All icefishes examined to date also lack the intracellular oxygen-binding protein myoglobin (Mb) in their oxidative skeletal muscles. However,...
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ftunivnapoliiris:oai:www.iris.unina.it:11588/499627 2024-06-23T07:47:58+00:00 Myoglobin enhances cardiac performance in antarctic icefish species that express the protein R. Acierno B. Tota B. D. Sidell AGNISOLA, CLAUDIO R., Acierno Agnisola, Claudio B., Tota B. D., Sidell 1997 STAMPA http://hdl.handle.net/11588/499627 eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:A1997XK68000013 volume:273 firstpage:R100 lastpage:R106 numberofpages:7 journal:AMERICAN JOURNAL OF PHYSIOLOGY. REGULATORY, INTEGRATIVE AND COMPARATIVE PHYSIOLOGY http://hdl.handle.net/11588/499627 info:eu-repo/semantics/article 1997 ftunivnapoliiris 2024-06-10T14:58:49Z Channichthyid icefishes of Antarctica are unique among adult vertebrates. All icefish species lack hemoglobin and red blood cells in their circulating blood. All icefishes examined to date also lack the intracellular oxygen-binding protein myoglobin (Mb) in their oxidative skeletal muscles. However, some icefish species do express Mb in their heart ventricles. It is unknown whether Mb in those species in which it is present represents an evolutionary relic or has functional significance. To address this problem, we compared mechanical performance of isolated, perfused hearts from two species of icefish in which Mb is either present (Chionodraco rastrospinosus) or is absent (Chaenocephalus aceratus). Hearts were challenged with increasing afterload (2.5-4.0 kPa) under conditions of defined basal flow (similar to 100 ml . min(-1). kg(-1)), in both the presence and absence of 5 mM sodium nitrite, a Mb poison. Unlike hearts from C. aceratus, which were unable to maintain a constant cardiac output under pressure loading, those from C. rastrospinosus retained a constant flow up to 3.5 kPa afterload. At the upper range of power outputs, hearts of Mb-lacking C. aceratus display greater oxygen utilization than those of Mb-containing C. rastrospinosus. Poisoning of Mb significantly impaired the ability of C. rastrospinosus hearts to face pressure loading without reduction in flow, whereas those of C. aceratus were refractory to the treatment. The results strongly support a functional role for Mb in the former species. Article in Journal/Newspaper Antarc* Antarctic Antarctica Icefish IRIS Università degli Studi di Napoli Federico II Antarctic |
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IRIS Università degli Studi di Napoli Federico II |
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ftunivnapoliiris |
language |
English |
description |
Channichthyid icefishes of Antarctica are unique among adult vertebrates. All icefish species lack hemoglobin and red blood cells in their circulating blood. All icefishes examined to date also lack the intracellular oxygen-binding protein myoglobin (Mb) in their oxidative skeletal muscles. However, some icefish species do express Mb in their heart ventricles. It is unknown whether Mb in those species in which it is present represents an evolutionary relic or has functional significance. To address this problem, we compared mechanical performance of isolated, perfused hearts from two species of icefish in which Mb is either present (Chionodraco rastrospinosus) or is absent (Chaenocephalus aceratus). Hearts were challenged with increasing afterload (2.5-4.0 kPa) under conditions of defined basal flow (similar to 100 ml . min(-1). kg(-1)), in both the presence and absence of 5 mM sodium nitrite, a Mb poison. Unlike hearts from C. aceratus, which were unable to maintain a constant cardiac output under pressure loading, those from C. rastrospinosus retained a constant flow up to 3.5 kPa afterload. At the upper range of power outputs, hearts of Mb-lacking C. aceratus display greater oxygen utilization than those of Mb-containing C. rastrospinosus. Poisoning of Mb significantly impaired the ability of C. rastrospinosus hearts to face pressure loading without reduction in flow, whereas those of C. aceratus were refractory to the treatment. The results strongly support a functional role for Mb in the former species. |
author2 |
R., Acierno Agnisola, Claudio B., Tota B. D., Sidell |
format |
Article in Journal/Newspaper |
author |
R. Acierno B. Tota B. D. Sidell AGNISOLA, CLAUDIO |
spellingShingle |
R. Acierno B. Tota B. D. Sidell AGNISOLA, CLAUDIO Myoglobin enhances cardiac performance in antarctic icefish species that express the protein |
author_facet |
R. Acierno B. Tota B. D. Sidell AGNISOLA, CLAUDIO |
author_sort |
R. Acierno |
title |
Myoglobin enhances cardiac performance in antarctic icefish species that express the protein |
title_short |
Myoglobin enhances cardiac performance in antarctic icefish species that express the protein |
title_full |
Myoglobin enhances cardiac performance in antarctic icefish species that express the protein |
title_fullStr |
Myoglobin enhances cardiac performance in antarctic icefish species that express the protein |
title_full_unstemmed |
Myoglobin enhances cardiac performance in antarctic icefish species that express the protein |
title_sort |
myoglobin enhances cardiac performance in antarctic icefish species that express the protein |
publishDate |
1997 |
url |
http://hdl.handle.net/11588/499627 |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic Antarctica Icefish |
genre_facet |
Antarc* Antarctic Antarctica Icefish |
op_relation |
info:eu-repo/semantics/altIdentifier/wos/WOS:A1997XK68000013 volume:273 firstpage:R100 lastpage:R106 numberofpages:7 journal:AMERICAN JOURNAL OF PHYSIOLOGY. REGULATORY, INTEGRATIVE AND COMPARATIVE PHYSIOLOGY http://hdl.handle.net/11588/499627 |
_version_ |
1802638285028196352 |