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- Publisher Website: 10.1002/pmic.200700904
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- PMID: 18654988
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Article: Proteomic analysis of larvae during development, attachment, and metamorphosis in the fouling barnacle, Balanus amphitrite
Title | Proteomic analysis of larvae during development, attachment, and metamorphosis in the fouling barnacle, Balanus amphitrite |
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Authors | |
Keywords | 2-DE Barnacle Larval metamorphosis Larval settlement |
Issue Date | 2008 |
Publisher | Wiley - 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? |
Abstract | The 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 Identifier | http://hdl.handle.net/10722/179070 |
ISSN | 2023 Impact Factor: 3.4 2023 SCImago Journal Rankings: 1.011 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Thiyagarajan, V | en_US |
dc.contributor.author | Qian, PY | en_US |
dc.date.accessioned | 2012-12-19T09:51:45Z | - |
dc.date.available | 2012-12-19T09:51:45Z | - |
dc.date.issued | 2008 | en_US |
dc.identifier.citation | Proteomics, 2008, v. 8 n. 15, p. 3164-3172 | en_US |
dc.identifier.issn | 1615-9853 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/179070 | - |
dc.description.abstract | The 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.language | eng | en_US |
dc.publisher | Wiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www.wiley-vch.de/home/proteomics | en_US |
dc.relation.ispartof | Proteomics | en_US |
dc.subject | 2-DE | - |
dc.subject | Barnacle | - |
dc.subject | Larval metamorphosis | - |
dc.subject | Larval settlement | - |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Cluster Analysis | en_US |
dc.subject.mesh | Electrophoresis, Gel, Two-Dimensional | en_US |
dc.subject.mesh | Larva - Growth & Development - Metabolism - Physiology | en_US |
dc.subject.mesh | Metamorphosis, Biological | en_US |
dc.subject.mesh | Proteome - Analysis - Classification | en_US |
dc.subject.mesh | Proteomics - Methods | en_US |
dc.subject.mesh | Reproducibility Of Results | en_US |
dc.subject.mesh | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | en_US |
dc.subject.mesh | Thoracica - Growth & Development - Metabolism - Physiology | en_US |
dc.title | Proteomic analysis of larvae during development, attachment, and metamorphosis in the fouling barnacle, Balanus amphitrite | en_US |
dc.type | Article | en_US |
dc.identifier.email | Thiyagarajan, V: rajan@hkucc.hku.hk | en_US |
dc.identifier.authority | Thiyagarajan, V=rp00796 | en_US |
dc.description.nature | link_to_OA_fulltext | en_US |
dc.identifier.doi | 10.1002/pmic.200700904 | en_US |
dc.identifier.pmid | 18654988 | - |
dc.identifier.scopus | eid_2-s2.0-49749105216 | en_US |
dc.identifier.hkuros | 223067 | - |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-49749105216&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 8 | en_US |
dc.identifier.issue | 15 | en_US |
dc.identifier.spage | 3164 | en_US |
dc.identifier.epage | 3172 | en_US |
dc.identifier.eissn | 1615-9861 | - |
dc.identifier.isi | WOS:000258503400017 | - |
dc.publisher.place | Germany | en_US |
dc.identifier.scopusauthorid | Thiyagarajan, V=6602476830 | en_US |
dc.identifier.scopusauthorid | Qian, PY=35240648600 | en_US |
dc.identifier.issnl | 1615-9853 | - |