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Cardiac myoglobin deficit has evolved repeatedly in teleost fishes

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Cardiac myoglobin deficit has evolved repeatedly in teleost fishes. / Macqueen, Daniel J.; Garcia de la Serrana Castillo, Daniel; Johnston, Ian Alistair.

In: Biology Letters, Vol. 10, No. 6, 20140225, 11.06.2014.

Research output: Contribution to journalArticle

Harvard

Macqueen, DJ, Garcia de la Serrana Castillo, D & Johnston, IA 2014, 'Cardiac myoglobin deficit has evolved repeatedly in teleost fishes' Biology Letters, vol. 10, no. 6, 20140225. https://doi.org/10.1098/rsbl.2014.0225

APA

Macqueen, D. J., Garcia de la Serrana Castillo, D., & Johnston, I. A. (2014). Cardiac myoglobin deficit has evolved repeatedly in teleost fishes. Biology Letters, 10(6), [20140225]. https://doi.org/10.1098/rsbl.2014.0225

Vancouver

Macqueen DJ, Garcia de la Serrana Castillo D, Johnston IA. Cardiac myoglobin deficit has evolved repeatedly in teleost fishes. Biology Letters. 2014 Jun 11;10(6). 20140225. https://doi.org/10.1098/rsbl.2014.0225

Author

Macqueen, Daniel J. ; Garcia de la Serrana Castillo, Daniel ; Johnston, Ian Alistair. / Cardiac myoglobin deficit has evolved repeatedly in teleost fishes. In: Biology Letters. 2014 ; Vol. 10, No. 6.

Bibtex - Download

@article{bd8f4d3e5e2a431db04dd96e22d74bda,
title = "Cardiac myoglobin deficit has evolved repeatedly in teleost fishes",
abstract = "Myoglobin (Mb) is the classic vertebrate oxygen-binding protein present in aerobic striated muscles. It functions principally in oxygen delivery and provides muscle with its characteristic red colour. Members of the Antarctic icefish family (Channichthyidae) are widely thought to be extraordinary for lacking cardiac Mb expression, a fact that has been attributed to their low metabolic rate and unusual evolutionary history. Here, we report that cardiac Mb deficit, associated with pale heart colour, has evolved repeatedly during teleost evolution. This trait affects both gill-and air-breathing species from temperate to tropical habitats across a full range of salinities. Cardiac Mb deficit results from total pseudogenization in three-spined stickleback and is associated with a massive reduction in mRNA level in two species that evidently retain functional Mb. The results suggest that near or complete absence of Mb-assisted oxygen delivery to heart muscle is a common facet of teleost biodiversity, even affecting lineages with notable oxygen demands. We suggest that Mb deficit may affect how different teleost species deal with increased tissue oxygen demands arising under climate change.",
keywords = "Myoglobin, Oxygen supply, Fish evolution, Climate change, Thermal tolerance, Limitation, Expression, Oxygen",
author = "Macqueen, {Daniel J.} and {Garcia de la Serrana Castillo}, Daniel and Johnston, {Ian Alistair}",
note = "This study was supported by the Marine Alliance for Science and Technology for Scotland (Scottish Funding Council grant no. HR09011),",
year = "2014",
month = "6",
day = "11",
doi = "10.1098/rsbl.2014.0225",
language = "English",
volume = "10",
journal = "Biology Letters",
issn = "1744-9561",
publisher = "The Royal Society",
number = "6",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Cardiac myoglobin deficit has evolved repeatedly in teleost fishes

AU - Macqueen, Daniel J.

AU - Garcia de la Serrana Castillo, Daniel

AU - Johnston, Ian Alistair

N1 - This study was supported by the Marine Alliance for Science and Technology for Scotland (Scottish Funding Council grant no. HR09011),

PY - 2014/6/11

Y1 - 2014/6/11

N2 - Myoglobin (Mb) is the classic vertebrate oxygen-binding protein present in aerobic striated muscles. It functions principally in oxygen delivery and provides muscle with its characteristic red colour. Members of the Antarctic icefish family (Channichthyidae) are widely thought to be extraordinary for lacking cardiac Mb expression, a fact that has been attributed to their low metabolic rate and unusual evolutionary history. Here, we report that cardiac Mb deficit, associated with pale heart colour, has evolved repeatedly during teleost evolution. This trait affects both gill-and air-breathing species from temperate to tropical habitats across a full range of salinities. Cardiac Mb deficit results from total pseudogenization in three-spined stickleback and is associated with a massive reduction in mRNA level in two species that evidently retain functional Mb. The results suggest that near or complete absence of Mb-assisted oxygen delivery to heart muscle is a common facet of teleost biodiversity, even affecting lineages with notable oxygen demands. We suggest that Mb deficit may affect how different teleost species deal with increased tissue oxygen demands arising under climate change.

AB - Myoglobin (Mb) is the classic vertebrate oxygen-binding protein present in aerobic striated muscles. It functions principally in oxygen delivery and provides muscle with its characteristic red colour. Members of the Antarctic icefish family (Channichthyidae) are widely thought to be extraordinary for lacking cardiac Mb expression, a fact that has been attributed to their low metabolic rate and unusual evolutionary history. Here, we report that cardiac Mb deficit, associated with pale heart colour, has evolved repeatedly during teleost evolution. This trait affects both gill-and air-breathing species from temperate to tropical habitats across a full range of salinities. Cardiac Mb deficit results from total pseudogenization in three-spined stickleback and is associated with a massive reduction in mRNA level in two species that evidently retain functional Mb. The results suggest that near or complete absence of Mb-assisted oxygen delivery to heart muscle is a common facet of teleost biodiversity, even affecting lineages with notable oxygen demands. We suggest that Mb deficit may affect how different teleost species deal with increased tissue oxygen demands arising under climate change.

KW - Myoglobin

KW - Oxygen supply

KW - Fish evolution

KW - Climate change

KW - Thermal tolerance

KW - Limitation

KW - Expression

KW - Oxygen

U2 - 10.1098/rsbl.2014.0225

DO - 10.1098/rsbl.2014.0225

M3 - Article

VL - 10

JO - Biology Letters

T2 - Biology Letters

JF - Biology Letters

SN - 1744-9561

IS - 6

M1 - 20140225

ER -

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