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Identification of The Canidae Iron Regulatory Hormone Hepcidin

Hepcidins are an evolutionarily conserved class of liver-expressed peptide, from which the twenty-five amino acid hormone, hepcidin-25 (herein hepcidin), has gained significant notoriety as the master regulator of iron homeostasis in mammals. Hepcidin maintains iron homeostasis by controlling the di...

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Autores principales: Mead, Martin K., Claus, Melissa, Litton, Edward, Smart, Lisa, Raisis, Anthea, Rossi, Gabriele, Trengove, Robert D., Gummer, Joel P. A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6920140/
https://www.ncbi.nlm.nih.gov/pubmed/31852911
http://dx.doi.org/10.1038/s41598-019-55009-w
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author Mead, Martin K.
Claus, Melissa
Litton, Edward
Smart, Lisa
Raisis, Anthea
Rossi, Gabriele
Trengove, Robert D.
Gummer, Joel P. A.
author_facet Mead, Martin K.
Claus, Melissa
Litton, Edward
Smart, Lisa
Raisis, Anthea
Rossi, Gabriele
Trengove, Robert D.
Gummer, Joel P. A.
author_sort Mead, Martin K.
collection PubMed
description Hepcidins are an evolutionarily conserved class of liver-expressed peptide, from which the twenty-five amino acid hormone, hepcidin-25 (herein hepcidin), has gained significant notoriety as the master regulator of iron homeostasis in mammals. Hepcidin maintains iron homeostasis by controlling the dietary absorption of iron and the mechanisms of recycling cellular iron stores. With the physiological significance of this hormone well established, it has emerged as an informative biomarker. In a comparison of the genome, transcriptome and peptidome of Canis lupis familiaris, we reveal the size of the hepcidin peptide in the canine, previous reports of which were contradictory to the evolutionary conservation predicted by genome annotation. Here, measurement of the peptide by mass spectrometry, following isolation from greyhound blood serum, revealed an amino acid sequence and peptide mass, differing from all accounts to date, yet demonstrating perfect sequence identity to that of the greater Canidae lineage of the Carnivora. Importantly, in the greyhound, the measured hepcidin peptide showed a similar temporal pattern to total serum iron, consistent with our understanding of hepcidin regulating iron homeostasis, in agreement with human diagnostics, and providing added translational evidence of the measured peptide being the iron regulatory hormone of the Canidae.
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spelling pubmed-69201402019-12-19 Identification of The Canidae Iron Regulatory Hormone Hepcidin Mead, Martin K. Claus, Melissa Litton, Edward Smart, Lisa Raisis, Anthea Rossi, Gabriele Trengove, Robert D. Gummer, Joel P. A. Sci Rep Article Hepcidins are an evolutionarily conserved class of liver-expressed peptide, from which the twenty-five amino acid hormone, hepcidin-25 (herein hepcidin), has gained significant notoriety as the master regulator of iron homeostasis in mammals. Hepcidin maintains iron homeostasis by controlling the dietary absorption of iron and the mechanisms of recycling cellular iron stores. With the physiological significance of this hormone well established, it has emerged as an informative biomarker. In a comparison of the genome, transcriptome and peptidome of Canis lupis familiaris, we reveal the size of the hepcidin peptide in the canine, previous reports of which were contradictory to the evolutionary conservation predicted by genome annotation. Here, measurement of the peptide by mass spectrometry, following isolation from greyhound blood serum, revealed an amino acid sequence and peptide mass, differing from all accounts to date, yet demonstrating perfect sequence identity to that of the greater Canidae lineage of the Carnivora. Importantly, in the greyhound, the measured hepcidin peptide showed a similar temporal pattern to total serum iron, consistent with our understanding of hepcidin regulating iron homeostasis, in agreement with human diagnostics, and providing added translational evidence of the measured peptide being the iron regulatory hormone of the Canidae. Nature Publishing Group UK 2019-12-18 /pmc/articles/PMC6920140/ /pubmed/31852911 http://dx.doi.org/10.1038/s41598-019-55009-w Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Mead, Martin K.
Claus, Melissa
Litton, Edward
Smart, Lisa
Raisis, Anthea
Rossi, Gabriele
Trengove, Robert D.
Gummer, Joel P. A.
Identification of The Canidae Iron Regulatory Hormone Hepcidin
title Identification of The Canidae Iron Regulatory Hormone Hepcidin
title_full Identification of The Canidae Iron Regulatory Hormone Hepcidin
title_fullStr Identification of The Canidae Iron Regulatory Hormone Hepcidin
title_full_unstemmed Identification of The Canidae Iron Regulatory Hormone Hepcidin
title_short Identification of The Canidae Iron Regulatory Hormone Hepcidin
title_sort identification of the canidae iron regulatory hormone hepcidin
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6920140/
https://www.ncbi.nlm.nih.gov/pubmed/31852911
http://dx.doi.org/10.1038/s41598-019-55009-w
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