Sexual dimorphism in Grp78 and Hsp90A heat shock protein expression in the estuarine copepod Eurytemora affinis.
Identifieur interne : 000121 ( PubMed/Checkpoint ); précédent : 000120; suivant : 000122Sexual dimorphism in Grp78 and Hsp90A heat shock protein expression in the estuarine copepod Eurytemora affinis.
Auteurs : Celine Boulangé-Lecomte [France] ; Joëlle Forget-Leray ; Benoit XuerebSource :
- Cell stress & chaperones [ 1466-1268 ] ; 2014.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Arthropod Proteins, HSP90 Heat-Shock Proteins, Heat-Shock Proteins.
- genetics : Copepoda.
- physiology : Copepoda.
- Animals, Female, Gene Expression Regulation, Male, Reproduction, Sex Characteristics.
Abstract
Aquatic organisms are constantly exposed to both natural and anthropogenic stressors. Under stress conditions, they elicit a cellular stress response, involving heat shock proteins (HSPs). HSPs are essential to protect proteins against aggregation and to help in the folding of native proteins or refolding of damaged ones. Because of their conservation among taxons and their inducibility after environmental/chemical stress, HSPs are commonly used as ecological and ecotoxicological biomarkers. However, the appropriate use of such molecular tools requires the investigation of the influence of biotic factors on their basal levels. As a first step in biomarker characterization, the present study aims to evaluate the impact of the reproductive cycle on the expression of the two major HSPs, Grp78 and Hsp90A in the estuarine copepod Eurytemora affinis. The constitutive expression of both genes in males was weak when compared to female levels suggesting gender-specific stress tolerance. Transcript levels gradually increased during oogenesis and maximal levels were recorded in ovigerous females. The present data support the view that the reproductive condition of individuals has to be considered as a confounding factor in stress evaluation by HSP quantification.
DOI: 10.1007/s12192-013-0482-3
PubMed: 24337963
Affiliations:
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Under stress conditions, they elicit a cellular stress response, involving heat shock proteins (HSPs). HSPs are essential to protect proteins against aggregation and to help in the folding of native proteins or refolding of damaged ones. Because of their conservation among taxons and their inducibility after environmental/chemical stress, HSPs are commonly used as ecological and ecotoxicological biomarkers. However, the appropriate use of such molecular tools requires the investigation of the influence of biotic factors on their basal levels. As a first step in biomarker characterization, the present study aims to evaluate the impact of the reproductive cycle on the expression of the two major HSPs, Grp78 and Hsp90A in the estuarine copepod Eurytemora affinis. The constitutive expression of both genes in males was weak when compared to female levels suggesting gender-specific stress tolerance. Transcript levels gradually increased during oogenesis and maximal levels were recorded in ovigerous females. The present data support the view that the reproductive condition of individuals has to be considered as a confounding factor in stress evaluation by HSP quantification.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24337963</PMID><DateCreated><Year>2014</Year><Month>6</Month><Day>3</Day></DateCreated><DateCompleted><Year>2015</Year><Month>01</Month><Day>12</Day></DateCompleted><DateRevised><Year>2015</Year><Month>4</Month><Day>22</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1466-1268</ISSN><JournalIssue CitedMedium="Internet"><Volume>19</Volume><Issue>4</Issue><PubDate><Year>2014</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Cell stress & chaperones</Title><ISOAbbreviation>Cell Stress Chaperones</ISOAbbreviation></Journal><ArticleTitle>Sexual dimorphism in Grp78 and Hsp90A heat shock protein expression in the estuarine copepod Eurytemora affinis.</ArticleTitle><Pagination><MedlinePgn>591-7</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s12192-013-0482-3</ELocationID><Abstract><AbstractText>Aquatic organisms are constantly exposed to both natural and anthropogenic stressors. Under stress conditions, they elicit a cellular stress response, involving heat shock proteins (HSPs). HSPs are essential to protect proteins against aggregation and to help in the folding of native proteins or refolding of damaged ones. Because of their conservation among taxons and their inducibility after environmental/chemical stress, HSPs are commonly used as ecological and ecotoxicological biomarkers. However, the appropriate use of such molecular tools requires the investigation of the influence of biotic factors on their basal levels. As a first step in biomarker characterization, the present study aims to evaluate the impact of the reproductive cycle on the expression of the two major HSPs, Grp78 and Hsp90A in the estuarine copepod Eurytemora affinis. The constitutive expression of both genes in males was weak when compared to female levels suggesting gender-specific stress tolerance. Transcript levels gradually increased during oogenesis and maximal levels were recorded in ovigerous females. The present data support the view that the reproductive condition of individuals has to be considered as a confounding factor in stress evaluation by HSP quantification.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Boulangé-Lecomte</LastName><ForeName>Celine</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Normandie University, ULH, Laboratory of Ecotoxicology (LEMA; EA3222, SFR SCALE 4116), 25 rue Philippe Lebon, BP 1123-76063, Le Havre Cedex, France, celine.lecomte@univ-lehavre.fr.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Forget-Leray</LastName><ForeName>Joëlle</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Xuereb</LastName><ForeName>Benoit</ForeName><Initials>B</Initials></Author></AuthorList><Language>ENG</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>Dec</Month><Day>12</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Cell Stress Chaperones</MedlineTA><NlmUniqueID>9610925</NlmUniqueID><ISSNLinking>1355-8145</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D060829">Arthropod Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018841">HSP90 Heat-Shock Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006360">Heat-Shock Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C048690">molecular chaperone GRP78</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>Int J Mol Med. 1999 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MajorTopicYN="N">Gene Expression Regulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018841" MajorTopicYN="N">HSP90 Heat-Shock Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006360" MajorTopicYN="N">Heat-Shock Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008297" MajorTopicYN="N">Male</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012098" MajorTopicYN="N">Reproduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012727" MajorTopicYN="N">Sex Characteristics</DescriptorName></MeshHeading></MeshHeadingList><OtherID Source="NLM">PMC4041948</OtherID></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>10</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2013</Year><Month>11</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2013</Year><Month>11</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>12</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>12</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>1</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24337963</ArticleId><ArticleId IdType="doi">10.1007/s12192-013-0482-3</ArticleId><ArticleId IdType="pmc">PMC4041948</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country></list><tree><noCountry><name sortKey="Forget Leray, Joelle" sort="Forget Leray, Joelle" uniqKey="Forget Leray J" first="Joëlle" last="Forget-Leray">Joëlle Forget-Leray</name><name sortKey="Xuereb, Benoit" sort="Xuereb, Benoit" uniqKey="Xuereb B" first="Benoit" last="Xuereb">Benoit Xuereb</name></noCountry><country name="France"><noRegion><name sortKey="Boulange Lecomte, Celine" sort="Boulange Lecomte, Celine" uniqKey="Boulange Lecomte C" first="Celine" last="Boulangé-Lecomte">Celine Boulangé-Lecomte</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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