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Plasma proteomic analysis of active and torpid greater mouse-eared bats (Myotis myotis)
Hibernation is a physiological adaptation to overcome extreme environmental conditions. It is characterized by prolonged periods of torpor interrupted by temporary arousals during winter. During torpor, body functions are suppressed and restored rapidly to almost pre-hibernation levels during arousa...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4653738/ https://www.ncbi.nlm.nih.gov/pubmed/26586174 http://dx.doi.org/10.1038/srep16604 |
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author | Hecht, Alexander M. Braun, Beate C. Krause, Eberhard Voigt, Christian C. Greenwood, Alex D. Czirják, Gábor Á. |
author_facet | Hecht, Alexander M. Braun, Beate C. Krause, Eberhard Voigt, Christian C. Greenwood, Alex D. Czirják, Gábor Á. |
author_sort | Hecht, Alexander M. |
collection | PubMed |
description | Hibernation is a physiological adaptation to overcome extreme environmental conditions. It is characterized by prolonged periods of torpor interrupted by temporary arousals during winter. During torpor, body functions are suppressed and restored rapidly to almost pre-hibernation levels during arousal. Although molecular studies have been performed on hibernating rodents and bears, it is unclear how generalizable the results are among hibernating species with different physiology such as bats. As targeted blood proteomic analysis are lacking in small hibernators, we investigated the general plasma proteomic profile of European Myotis myotis and hibernation associated changes between torpid and active individuals by two-dimensional gel electrophoresis. Results revealed an alternation of proteins involved in transport, fuel switching, innate immunity and blood coagulation between the two physiological states. The results suggest that metabolic changes during hibernation are associated with plasma proteomic changes. Further characterization of the proteomic plasma profile identified transport proteins, coagulation proteins and complement factors and detected a high abundance of alpha-fetoprotein. We were able to establish for the first time a basic myotid bat plasma proteomic profile and further demonstrated a modulated protein expression during torpor in Myotis myotis, indicating both novel physiological pathways in bats in general, and during hibernation in particular. |
format | Online Article Text |
id | pubmed-4653738 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-46537382015-11-25 Plasma proteomic analysis of active and torpid greater mouse-eared bats (Myotis myotis) Hecht, Alexander M. Braun, Beate C. Krause, Eberhard Voigt, Christian C. Greenwood, Alex D. Czirják, Gábor Á. Sci Rep Article Hibernation is a physiological adaptation to overcome extreme environmental conditions. It is characterized by prolonged periods of torpor interrupted by temporary arousals during winter. During torpor, body functions are suppressed and restored rapidly to almost pre-hibernation levels during arousal. Although molecular studies have been performed on hibernating rodents and bears, it is unclear how generalizable the results are among hibernating species with different physiology such as bats. As targeted blood proteomic analysis are lacking in small hibernators, we investigated the general plasma proteomic profile of European Myotis myotis and hibernation associated changes between torpid and active individuals by two-dimensional gel electrophoresis. Results revealed an alternation of proteins involved in transport, fuel switching, innate immunity and blood coagulation between the two physiological states. The results suggest that metabolic changes during hibernation are associated with plasma proteomic changes. Further characterization of the proteomic plasma profile identified transport proteins, coagulation proteins and complement factors and detected a high abundance of alpha-fetoprotein. We were able to establish for the first time a basic myotid bat plasma proteomic profile and further demonstrated a modulated protein expression during torpor in Myotis myotis, indicating both novel physiological pathways in bats in general, and during hibernation in particular. Nature Publishing Group 2015-11-20 /pmc/articles/PMC4653738/ /pubmed/26586174 http://dx.doi.org/10.1038/srep16604 Text en Copyright © 2015, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Hecht, Alexander M. Braun, Beate C. Krause, Eberhard Voigt, Christian C. Greenwood, Alex D. Czirják, Gábor Á. Plasma proteomic analysis of active and torpid greater mouse-eared bats (Myotis myotis) |
title | Plasma proteomic analysis of active and torpid greater mouse-eared bats (Myotis myotis) |
title_full | Plasma proteomic analysis of active and torpid greater mouse-eared bats (Myotis myotis) |
title_fullStr | Plasma proteomic analysis of active and torpid greater mouse-eared bats (Myotis myotis) |
title_full_unstemmed | Plasma proteomic analysis of active and torpid greater mouse-eared bats (Myotis myotis) |
title_short | Plasma proteomic analysis of active and torpid greater mouse-eared bats (Myotis myotis) |
title_sort | plasma proteomic analysis of active and torpid greater mouse-eared bats (myotis myotis) |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4653738/ https://www.ncbi.nlm.nih.gov/pubmed/26586174 http://dx.doi.org/10.1038/srep16604 |
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