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Conference Paper: Response of larval barnacle proteome to CO 2-driven seawater acidification

TitleResponse of larval barnacle proteome to CO 2-driven seawater acidification
Authors
Issue Date2011
PublisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/cbpd
Citation
Comparative Biochemistry And Physiology - Part D: Genomics And Proteomics, 2011, v. 6 n. 3, p. 310-321 How to Cite?
AbstractThe majority of benthic marine invertebrates have a complex life cycle, during which the pelagic larvae select a suitable substrate, attach to it, and then metamorphose into benthic adults. Anthropogenic ocean acidification (OA) is postulated to affect larval metamorphic success through an altered protein expression pattern (proteome structure) and post-translational modifications. To test this hypothesis, larvae of an economically and ecologically important barnacle species Balanus amphitrite, were cultured from nauplius to the cyprid stage in the present (control) and in the projected elevated concentrations of CO 2 for the year 2100 (the OA treatment). Cyprid response to OA was analyzed at the total proteome level as well as two protein post-translational modification (phosphorylation and glycosylation) levels using a 2-DE based proteomic approach. The cyprid proteome showed OA-driven changes. Proteins that were differentially up or down regulated by OA come from three major groups, namely those related to energy-metabolism, respiration, and molecular chaperones, illustrating a potential strategy that the barnacle larvae may employ to tolerate OA stress. The differentially expressed proteins were tentatively identified as OA-responsive, effectively creating unique protein expression signatures for OA scenario of 2100. This study showed the promise of using a sentinel and non-model species to examine the impact of OA at the proteome level. © 2011 Elsevier Inc. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/179610
ISSN
2015 Impact Factor: 2.254
2015 SCImago Journal Rankings: 1.064
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWong, KKWen_US
dc.contributor.authorLane, ACen_US
dc.contributor.authorLeung, PTYen_US
dc.contributor.authorThiyagarajan, Ven_US
dc.date.accessioned2012-12-19T10:00:11Z-
dc.date.available2012-12-19T10:00:11Z-
dc.date.issued2011en_US
dc.identifier.citationComparative Biochemistry And Physiology - Part D: Genomics And Proteomics, 2011, v. 6 n. 3, p. 310-321en_US
dc.identifier.issn1744-117Xen_US
dc.identifier.urihttp://hdl.handle.net/10722/179610-
dc.description.abstractThe majority of benthic marine invertebrates have a complex life cycle, during which the pelagic larvae select a suitable substrate, attach to it, and then metamorphose into benthic adults. Anthropogenic ocean acidification (OA) is postulated to affect larval metamorphic success through an altered protein expression pattern (proteome structure) and post-translational modifications. To test this hypothesis, larvae of an economically and ecologically important barnacle species Balanus amphitrite, were cultured from nauplius to the cyprid stage in the present (control) and in the projected elevated concentrations of CO 2 for the year 2100 (the OA treatment). Cyprid response to OA was analyzed at the total proteome level as well as two protein post-translational modification (phosphorylation and glycosylation) levels using a 2-DE based proteomic approach. The cyprid proteome showed OA-driven changes. Proteins that were differentially up or down regulated by OA come from three major groups, namely those related to energy-metabolism, respiration, and molecular chaperones, illustrating a potential strategy that the barnacle larvae may employ to tolerate OA stress. The differentially expressed proteins were tentatively identified as OA-responsive, effectively creating unique protein expression signatures for OA scenario of 2100. This study showed the promise of using a sentinel and non-model species to examine the impact of OA at the proteome level. © 2011 Elsevier Inc. All rights reserved.en_US
dc.languageengen_US
dc.publisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/cbpden_US
dc.relation.ispartofComparative Biochemistry and Physiology - Part D: Genomics and Proteomicsen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCarbon Dioxide - Chemistryen_US
dc.subject.meshElectrophoresis, Gel, Two-Dimensionalen_US
dc.subject.meshHydrogen-Ion Concentrationen_US
dc.subject.meshLarva - Physiologyen_US
dc.subject.meshMetamorphosis, Biological - Physiologyen_US
dc.subject.meshProtein Processing, Post-Translationalen_US
dc.subject.meshProteome - Analysisen_US
dc.subject.meshProteomics - Methodsen_US
dc.subject.meshSeawater - Chemistryen_US
dc.subject.meshThoracica - Physiologyen_US
dc.titleResponse of larval barnacle proteome to CO 2-driven seawater acidificationen_US
dc.typeConference_Paperen_US
dc.identifier.emailThiyagarajan, V: rajan@hkucc.hku.hken_US
dc.identifier.authorityThiyagarajan, V=rp00796en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.cbd.2011.07.001en_US
dc.identifier.pmid21831737-
dc.identifier.scopuseid_2-s2.0-80052029763en_US
dc.identifier.hkuros195693-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-80052029763&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume6en_US
dc.identifier.issue3en_US
dc.identifier.spage310en_US
dc.identifier.epage321en_US
dc.identifier.isiWOS:000294938200008-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridWong, KKW=50263582600en_US
dc.identifier.scopusauthoridLane, AC=50262349900en_US
dc.identifier.scopusauthoridLeung, PTY=35740926800en_US
dc.identifier.scopusauthoridThiyagarajan, V=6602476830en_US

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