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Article: Proteomic analysis of larvae during development, attachment, and metamorphosis in the fouling barnacle, Balanus amphitrite

TitleProteomic analysis of larvae during development, attachment, and metamorphosis in the fouling barnacle, Balanus amphitrite
Authors
Issue Date2008
PublisherWiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www.wiley-vch.de/home/proteomics
Citation
Proteomics, 2008, v. 8 n. 15, p. 3164-3172 How to Cite?
AbstractThe barnacle, Balanus amphitrite, is one of the primary model organisms for rocky-shore ecology studies and biofouling research. This barnacle species has a complex life cycle during which the swimming nauplius molts six times and transforms into a cyprid stage. Cyprids must attach to a surface to metamorphose into a juvenile barnacle. To clarify the overall profile of protein expression during larval development and metamorphosis, 2-DE was used to compare the proteome of the nauplius, the swimming cyprid, the attached cyprid, and the metamorphosed cyprid. The proteome of the swimming cyprid was distinctly different from that of other life stages and had about 400 spots. The proteomes of the attached and metamorphosed cyprids were similar with respect to major proteins but had significantly lower numbers of spots compared to that of swimming larval stages. Obviously, synthesis of most proteins from swimming cyprids was switched off after attachment and metamorphosis. Our advanced MS analysis (MALDI-TOF/TOF MS/MS) allowed us to identify the proteins that were differentially and abundantly expressed in the swimming cyprid. These proteins included signal transduction proteins (adenylate cyclase and calmodulin) and juvenile hormone binding proteins. In summary, for the first time, we have analyzed the global protein expression pattern of fouling marine invertebrate larvae during metamorphosis. Our study provides new insights into the mechanisms of barnacle larval metamorphosis and also provides a foundation for exploring novel targets for antifouling treatments. © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.
Persistent Identifierhttp://hdl.handle.net/10722/179070
ISSN
2015 Impact Factor: 4.079
2015 SCImago Journal Rankings: 1.476
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorThiyagarajan, Ven_US
dc.contributor.authorQian, PYen_US
dc.date.accessioned2012-12-19T09:51:45Z-
dc.date.available2012-12-19T09:51:45Z-
dc.date.issued2008en_US
dc.identifier.citationProteomics, 2008, v. 8 n. 15, p. 3164-3172en_US
dc.identifier.issn1615-9853en_US
dc.identifier.urihttp://hdl.handle.net/10722/179070-
dc.description.abstractThe barnacle, Balanus amphitrite, is one of the primary model organisms for rocky-shore ecology studies and biofouling research. This barnacle species has a complex life cycle during which the swimming nauplius molts six times and transforms into a cyprid stage. Cyprids must attach to a surface to metamorphose into a juvenile barnacle. To clarify the overall profile of protein expression during larval development and metamorphosis, 2-DE was used to compare the proteome of the nauplius, the swimming cyprid, the attached cyprid, and the metamorphosed cyprid. The proteome of the swimming cyprid was distinctly different from that of other life stages and had about 400 spots. The proteomes of the attached and metamorphosed cyprids were similar with respect to major proteins but had significantly lower numbers of spots compared to that of swimming larval stages. Obviously, synthesis of most proteins from swimming cyprids was switched off after attachment and metamorphosis. Our advanced MS analysis (MALDI-TOF/TOF MS/MS) allowed us to identify the proteins that were differentially and abundantly expressed in the swimming cyprid. These proteins included signal transduction proteins (adenylate cyclase and calmodulin) and juvenile hormone binding proteins. In summary, for the first time, we have analyzed the global protein expression pattern of fouling marine invertebrate larvae during metamorphosis. Our study provides new insights into the mechanisms of barnacle larval metamorphosis and also provides a foundation for exploring novel targets for antifouling treatments. © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.en_US
dc.languageengen_US
dc.publisherWiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www.wiley-vch.de/home/proteomicsen_US
dc.relation.ispartofProteomicsen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCluster Analysisen_US
dc.subject.meshElectrophoresis, Gel, Two-Dimensionalen_US
dc.subject.meshLarva - Growth & Development - Metabolism - Physiologyen_US
dc.subject.meshMetamorphosis, Biologicalen_US
dc.subject.meshProteome - Analysis - Classificationen_US
dc.subject.meshProteomics - Methodsen_US
dc.subject.meshReproducibility Of Resultsen_US
dc.subject.meshSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionizationen_US
dc.subject.meshThoracica - Growth & Development - Metabolism - Physiologyen_US
dc.titleProteomic analysis of larvae during development, attachment, and metamorphosis in the fouling barnacle, Balanus amphitriteen_US
dc.typeArticleen_US
dc.identifier.emailThiyagarajan, V: rajan@hkucc.hku.hken_US
dc.identifier.authorityThiyagarajan, V=rp00796en_US
dc.description.naturelink_to_OA_fulltexten_US
dc.identifier.doi10.1002/pmic.200700904en_US
dc.identifier.pmid18654988-
dc.identifier.scopuseid_2-s2.0-49749105216en_US
dc.identifier.hkuros223067-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-49749105216&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume8en_US
dc.identifier.issue15en_US
dc.identifier.spage3164en_US
dc.identifier.epage3172en_US
dc.identifier.eissn1615-9861-
dc.identifier.isiWOS:000258503400017-
dc.publisher.placeGermanyen_US
dc.identifier.scopusauthoridThiyagarajan, V=6602476830en_US
dc.identifier.scopusauthoridQian, PY=35240648600en_US

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