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<title lang=en>The rapid cold hardening response of Drosophila melanogaster: complex regulation across different levels of biological organization.</title>
<creator>Overgaard, Johannes</creator>
<creator>Sørensen, Jesper Givskov</creator>
<creator>Com, Emmanuelle</creator>
<creator>Colinet, Hervé</creator>
<contributor>Aarhus University [Aarhus]</contributor>
<contributor>Institut de recherche, santé, environnement et travail [Rennes] (Irset) ; Université d'Angers (UA) - Université des Antilles et de la Guyane (UAG) - Université de Rennes 1 (UR1) - École des Hautes Études en Santé Publique [EHESP] (EHESP) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )</contributor>
<contributor>Ecosystèmes, biodiversité, évolution [Rennes] (ECOBIO) ; Université de Rennes 1 (UR1) - INEE - Observatoire des Sciences de l'Univers de Rennes (OSUR) - Centre National de la Recherche Scientifique (CNRS)</contributor>
<contributor>This study was supported by Sapere Aude DFF-Starting Grants (JO & JGS) from The Danish Council for Independent Research: Natural Sciences and The Centre National de la Recherche Scientifique - CNRS (HC)</contributor>
<description>International audience</description>
<source>ISSN: 0022-1910</source>
<source>EISSN: 0022-1910</source>
<source>Journal of Insect Physiology</source>
<publisher>Elsevier</publisher>
<identifier>hal-00991032</identifier>
<identifier>https://hal-univ-rennes1.archives-ouvertes.fr/hal-00991032</identifier>
<source>https://hal-univ-rennes1.archives-ouvertes.fr/hal-00991032</source>
<source>Journal of Insect Physiology, Elsevier, 2014, 62, pp.46-53. 〈10.1016/j.jinsphys.2014.01.009〉</source>
<identifier>DOI : 10.1016/j.jinsphys.2014.01.009</identifier>
<relation>info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jinsphys.2014.01.009</relation>
<identifier>PUBMED : 24508557</identifier>
<relation>info:eu-repo/semantics/altIdentifier/pmid/24508557</relation>
<language>en</language>
<subject lang=en>Acclimation</subject>
<subject lang=en>Cold tolerance</subject>
<subject lang=en>Glycogen Phosphorylase</subject>
<subject lang=en>Proteomics</subject>
<subject lang=en>Fruit fly</subject>
<subject>[SDE.BE] Environmental Sciences/Biodiversity and Ecology</subject>
<type>info:eu-repo/semantics/article</type>
<type>Journal articles</type>
<description lang=en>Rapid cold hardening (RCH) is a form of thermal acclimation that allows ectotherms to fine-tune their physiological state to match rapid changes in thermal environment. Despite progress in recent years, there is still a considerable uncertainty regarding the physiological basis of RCH in insects. Here we investigated the physiological response of adult Drosophila melanogaster to a gradual reduction of temperature from 25 to 0°C followed by 1h at 0°C. As expected, this RCH treatment promoted cold tolerance, and so we hypothesized that this change could be detected at the proteomic level. Using 2D-DIGE, we found that only a few proteins significantly changed in abundance, and of these, we identified a set of four proteins of particular interest. These were identified as two different variants of glycogen phosphorylase (GlyP) of which three spots were up-regulated and another was down regulated. In subsequent experiments, we quantified upstream events by measuring the GlyP mRNA amount, but we found no marked effect of RCH. We also examined downstream events by measuring GlyP activity and the level of free sugars. We found no effect of RCH on GlyP activity. On the other hand, screening of whole animal sugar contents revealed a small increase in glucose levels following RCH while trehalose content was unaltered. This study highlights a complex regulation of GlyP in relation to RCH where we found associations between the cold tolerance, the protein abundance and the metabolite concentrations but no changes in mRNA expression and enzyme activity. These data stress the necessity of combining the hypothesis-generating power of an 'Omics' approach with subsequent targeted validations across several levels of the biological organization. We discuss reasons why different biological linked levels do not necessarily change stoichiometrically.</description>
<date>2014-03</date>
</dc>
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