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Comparative proteome analysis of Milnesium tardigradum in early embryonic state versus adults in active and anhydrobiotic state

Tardigrades have fascinated researchers for more than 300 years because of their extraordinary capability to undergo cryptobiosis and survive extreme environmental conditions. However, the survival mechanisms of tardigrades are still poorly understood mainly due to the absence of detailed knowledge...

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Autores principales: Schokraie, Elham, Warnken, Uwe, Hotz-Wagenblatt, Agnes, Grohme, Markus A., Hengherr, Steffen, Förster, Frank, Schill, Ralph O., Frohme, Marcus, Dandekar, Thomas, Schnölzer, Martina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3459984/
https://www.ncbi.nlm.nih.gov/pubmed/23029181
http://dx.doi.org/10.1371/journal.pone.0045682
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author Schokraie, Elham
Warnken, Uwe
Hotz-Wagenblatt, Agnes
Grohme, Markus A.
Hengherr, Steffen
Förster, Frank
Schill, Ralph O.
Frohme, Marcus
Dandekar, Thomas
Schnölzer, Martina
author_facet Schokraie, Elham
Warnken, Uwe
Hotz-Wagenblatt, Agnes
Grohme, Markus A.
Hengherr, Steffen
Förster, Frank
Schill, Ralph O.
Frohme, Marcus
Dandekar, Thomas
Schnölzer, Martina
author_sort Schokraie, Elham
collection PubMed
description Tardigrades have fascinated researchers for more than 300 years because of their extraordinary capability to undergo cryptobiosis and survive extreme environmental conditions. However, the survival mechanisms of tardigrades are still poorly understood mainly due to the absence of detailed knowledge about the proteome and genome of these organisms. Our study was intended to provide a basis for the functional characterization of expressed proteins in different states of tardigrades. High-throughput, high-accuracy proteomics in combination with a newly developed tardigrade specific protein database resulted in the identification of more than 3000 proteins in three different states: early embryonic state and adult animals in active and anhydrobiotic state. This comprehensive proteome resource includes protein families such as chaperones, antioxidants, ribosomal proteins, cytoskeletal proteins, transporters, protein channels, nutrient reservoirs, and developmental proteins. A comparative analysis of protein families in the different states was performed by calculating the exponentially modified protein abundance index which classifies proteins in major and minor components. This is the first step to analyzing the proteins involved in early embryonic development, and furthermore proteins which might play an important role in the transition into the anhydrobiotic state.
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spelling pubmed-34599842012-10-01 Comparative proteome analysis of Milnesium tardigradum in early embryonic state versus adults in active and anhydrobiotic state Schokraie, Elham Warnken, Uwe Hotz-Wagenblatt, Agnes Grohme, Markus A. Hengherr, Steffen Förster, Frank Schill, Ralph O. Frohme, Marcus Dandekar, Thomas Schnölzer, Martina PLoS One Research Article Tardigrades have fascinated researchers for more than 300 years because of their extraordinary capability to undergo cryptobiosis and survive extreme environmental conditions. However, the survival mechanisms of tardigrades are still poorly understood mainly due to the absence of detailed knowledge about the proteome and genome of these organisms. Our study was intended to provide a basis for the functional characterization of expressed proteins in different states of tardigrades. High-throughput, high-accuracy proteomics in combination with a newly developed tardigrade specific protein database resulted in the identification of more than 3000 proteins in three different states: early embryonic state and adult animals in active and anhydrobiotic state. This comprehensive proteome resource includes protein families such as chaperones, antioxidants, ribosomal proteins, cytoskeletal proteins, transporters, protein channels, nutrient reservoirs, and developmental proteins. A comparative analysis of protein families in the different states was performed by calculating the exponentially modified protein abundance index which classifies proteins in major and minor components. This is the first step to analyzing the proteins involved in early embryonic development, and furthermore proteins which might play an important role in the transition into the anhydrobiotic state. Public Library of Science 2012-09-27 /pmc/articles/PMC3459984/ /pubmed/23029181 http://dx.doi.org/10.1371/journal.pone.0045682 Text en © 2012 Schokraie et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Schokraie, Elham
Warnken, Uwe
Hotz-Wagenblatt, Agnes
Grohme, Markus A.
Hengherr, Steffen
Förster, Frank
Schill, Ralph O.
Frohme, Marcus
Dandekar, Thomas
Schnölzer, Martina
Comparative proteome analysis of Milnesium tardigradum in early embryonic state versus adults in active and anhydrobiotic state
title Comparative proteome analysis of Milnesium tardigradum in early embryonic state versus adults in active and anhydrobiotic state
title_full Comparative proteome analysis of Milnesium tardigradum in early embryonic state versus adults in active and anhydrobiotic state
title_fullStr Comparative proteome analysis of Milnesium tardigradum in early embryonic state versus adults in active and anhydrobiotic state
title_full_unstemmed Comparative proteome analysis of Milnesium tardigradum in early embryonic state versus adults in active and anhydrobiotic state
title_short Comparative proteome analysis of Milnesium tardigradum in early embryonic state versus adults in active and anhydrobiotic state
title_sort comparative proteome analysis of milnesium tardigradum in early embryonic state versus adults in active and anhydrobiotic state
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3459984/
https://www.ncbi.nlm.nih.gov/pubmed/23029181
http://dx.doi.org/10.1371/journal.pone.0045682
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