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Article: 2D gel-based proteome and phosphoproteome analysis during larval metamorphosis in two major marine biofouling invertebrates

Title2D gel-based proteome and phosphoproteome analysis during larval metamorphosis in two major marine biofouling invertebrates
Authors
Keywords2DE
Barnacle
Bugula
Larval metamorphosis
Larval proteomics
Phosphoproteome
Issue Date2009
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jprobs
Citation
Journal Of Proteome Research, 2009, v. 8 n. 6, p. 2708-2719 How to Cite?
AbstractLarvae of some benthic invertebrates respond (metamorphose or not) to chemical cues within minutes or hours and often without excessive transcription or translation. Although protein phosphorylation is one of the most important molecular switching mechanisms that govern variety of rapid cellular responses in higher organisms, this is the first study to analyze the global protein expression and protein phosphorylation status during larval metamorphosis in two major marine biofouling invertebrates (a bryozoan Bugula neritina and a barnacle Balanus amphitrite). Results indicate that larval proteomic response to metamorphosis (inhibiton or induction) involves substantial change in the phosphorylation status of proteins rather than de novo protein synthesis. An abundantly expressed and an unnamed phosphoprotein that appears to play key regulatory role in larval metamorphosis was identified. When larvae of bryozoan and barnacle were challenged with a metamorphosis (and kinase) inhibitor, the genistein, the number of phosphoproteins in bryozoan were substantially reduced but drastically increased in barnacle. Taken together, this is the first time that the usefulness of employing 2DE-based proteomic and phosphoproteomic approaches was demonstrated for us to understand the molecular mechanisms of larval metamorphosis and to study the mode-of-action of chemical cues in marine organisms. © 2009 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/60655
ISSN
2015 Impact Factor: 4.173
2015 SCImago Journal Rankings: 1.962
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorThiyagarajan, Ven_HK
dc.contributor.authorWong, Ten_HK
dc.contributor.authorQian, PYen_HK
dc.date.accessioned2010-05-31T04:15:56Z-
dc.date.available2010-05-31T04:15:56Z-
dc.date.issued2009en_HK
dc.identifier.citationJournal Of Proteome Research, 2009, v. 8 n. 6, p. 2708-2719en_HK
dc.identifier.issn1535-3893en_HK
dc.identifier.urihttp://hdl.handle.net/10722/60655-
dc.description.abstractLarvae of some benthic invertebrates respond (metamorphose or not) to chemical cues within minutes or hours and often without excessive transcription or translation. Although protein phosphorylation is one of the most important molecular switching mechanisms that govern variety of rapid cellular responses in higher organisms, this is the first study to analyze the global protein expression and protein phosphorylation status during larval metamorphosis in two major marine biofouling invertebrates (a bryozoan Bugula neritina and a barnacle Balanus amphitrite). Results indicate that larval proteomic response to metamorphosis (inhibiton or induction) involves substantial change in the phosphorylation status of proteins rather than de novo protein synthesis. An abundantly expressed and an unnamed phosphoprotein that appears to play key regulatory role in larval metamorphosis was identified. When larvae of bryozoan and barnacle were challenged with a metamorphosis (and kinase) inhibitor, the genistein, the number of phosphoproteins in bryozoan were substantially reduced but drastically increased in barnacle. Taken together, this is the first time that the usefulness of employing 2DE-based proteomic and phosphoproteomic approaches was demonstrated for us to understand the molecular mechanisms of larval metamorphosis and to study the mode-of-action of chemical cues in marine organisms. © 2009 American Chemical Society.en_HK
dc.languageengen_HK
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jprobsen_HK
dc.relation.ispartofJournal of Proteome Researchen_HK
dc.subject2DEen_HK
dc.subjectBarnacleen_HK
dc.subjectBugulaen_HK
dc.subjectLarval metamorphosisen_HK
dc.subjectLarval proteomicsen_HK
dc.subjectPhosphoproteomeen_HK
dc.subject.meshBugula-
dc.subject.meshBarnacle-
dc.subject.meshLarval Metamorphosis-
dc.subject.mesh2DE-
dc.subject.meshLarval Proteomics-
dc.title2D gel-based proteome and phosphoproteome analysis during larval metamorphosis in two major marine biofouling invertebratesen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1535-3893&volume=8&issue=6&spage=2708&epage=2719&date=2009&atitle=2D+Gel-based+proteome+and+phosphoproteome+analysis+during+larval+metamorphosis+in+two+major+marine+biofouling+invertebratesen_HK
dc.identifier.emailThiyagarajan, V: rajan@hkucc.hku.hken_HK
dc.identifier.authorityThiyagarajan, V=rp00796en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1021/pr800976uen_HK
dc.identifier.pmid19341272-
dc.identifier.scopuseid_2-s2.0-67149128374en_HK
dc.identifier.hkuros161449en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-67149128374&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume8en_HK
dc.identifier.issue6en_HK
dc.identifier.spage2708en_HK
dc.identifier.epage2719en_HK
dc.identifier.eissn1535-3907-
dc.identifier.isiWOS:000266719400010-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridThiyagarajan, V=6602476830en_HK
dc.identifier.scopusauthoridWong, T=37015028500en_HK
dc.identifier.scopusauthoridQian, PY=35240648600en_HK

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