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Article: 2D gel-based multiplexed proteomic analysis during larval development and metamorphosis of the biofouling polychaete tubeworm hydroides elegans

Title2D gel-based multiplexed proteomic analysis during larval development and metamorphosis of the biofouling polychaete tubeworm hydroides elegans
Authors
Keywords2-DE, multiplexed proteomics
Hydroides elegans
larval development
larval metamorphosis
phosphoproteome
proteome
Issue Date2010
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jprobs
Citation
Journal Of Proteome Research, 2010, v. 9 n. 9, p. 4851-4860 How to Cite?
AbstractLarval settlement and metamorphosis of a common biofouling polychaete worm, Hydroides elegans, involve remarkable structural and physiological changes during this pelagic to sessile habitat shift. The endogenous protein molecules and post-translational modifications that drive this larval transition process are not only of interest to ecologists but also to the antifouling paint industry, which aims to control the settlement of this biofouling species on man-made structures (e.g., ship hulls). On the basis of our recent proteomic studies, we hypothesize that rapid larval settlement of H. elegans could be mediated through changes in phosphorylation status of proteins rather than extensive de novo synthesis of proteins. To test this hypothesis, 2D gel-based multiplexed proteomics technology was used to monitor the changes in protein expression and phosphorylation status during larval development and metamorphosis of H. elegans. The protein expression profiles of larvae before and after they reached competency to attach and metamorphose were similar in terms of major proteins, but the percentage of phosphorylated proteins increased from 41% to 49% after competency. Notably, both the protein and phosphoprotein profiles of the metamorphosed individuals (adult) were distinctly different from that of the larvae, with only 40% of the proteins phosphorylated in the adult stage. The intensity ratio of all phosphoprotein spots to all total protein spots was also the highest in the competent larval stage. Overall, our results indicated that the level of protein phosphorylation might play a crucial role in the initiation of larval settlement and metamorphosis. © 2010 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/130028
ISSN
2015 Impact Factor: 4.173
2015 SCImago Journal Rankings: 1.962
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZhang, Yen_HK
dc.contributor.authorSun, Jen_HK
dc.contributor.authorXiao, Ken_HK
dc.contributor.authorArellano, SMen_HK
dc.contributor.authorThiyagarajan, Ven_HK
dc.contributor.authorQian, PYen_HK
dc.date.accessioned2010-12-23T08:45:42Z-
dc.date.available2010-12-23T08:45:42Z-
dc.date.issued2010en_HK
dc.identifier.citationJournal Of Proteome Research, 2010, v. 9 n. 9, p. 4851-4860en_HK
dc.identifier.issn1535-3893en_HK
dc.identifier.urihttp://hdl.handle.net/10722/130028-
dc.description.abstractLarval settlement and metamorphosis of a common biofouling polychaete worm, Hydroides elegans, involve remarkable structural and physiological changes during this pelagic to sessile habitat shift. The endogenous protein molecules and post-translational modifications that drive this larval transition process are not only of interest to ecologists but also to the antifouling paint industry, which aims to control the settlement of this biofouling species on man-made structures (e.g., ship hulls). On the basis of our recent proteomic studies, we hypothesize that rapid larval settlement of H. elegans could be mediated through changes in phosphorylation status of proteins rather than extensive de novo synthesis of proteins. To test this hypothesis, 2D gel-based multiplexed proteomics technology was used to monitor the changes in protein expression and phosphorylation status during larval development and metamorphosis of H. elegans. The protein expression profiles of larvae before and after they reached competency to attach and metamorphose were similar in terms of major proteins, but the percentage of phosphorylated proteins increased from 41% to 49% after competency. Notably, both the protein and phosphoprotein profiles of the metamorphosed individuals (adult) were distinctly different from that of the larvae, with only 40% of the proteins phosphorylated in the adult stage. The intensity ratio of all phosphoprotein spots to all total protein spots was also the highest in the competent larval stage. Overall, our results indicated that the level of protein phosphorylation might play a crucial role in the initiation of larval settlement and metamorphosis. © 2010 American Chemical Society.en_HK
dc.languageengen_US
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.subject2-DE, multiplexed proteomicsen_HK
dc.subjectHydroides elegansen_HK
dc.subjectlarval developmenten_HK
dc.subjectlarval metamorphosisen_HK
dc.subjectphosphoproteomeen_HK
dc.subjectproteomeen_HK
dc.title2D gel-based multiplexed proteomic analysis during larval development and metamorphosis of the biofouling polychaete tubeworm hydroides elegansen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1535-3893&volume=&spage=In press&epage=&date=2010&atitle=2D+Gel-Based+Multiplexed+Proteomic+Analysis+during+Larval+Development+and+Metamorphosis+of+the+Biofouling+Polychaete+Tubeworm+/Hydroides+elegansen_US
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/pr100645zen_HK
dc.identifier.pmid20666481en_HK
dc.identifier.scopuseid_2-s2.0-77956314945en_HK
dc.identifier.hkuros177922en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-77956314945&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume9en_HK
dc.identifier.issue9en_HK
dc.identifier.spage4851en_HK
dc.identifier.epage4860en_HK
dc.identifier.isiWOS:000281443700048-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridZhang, Y=36038958500en_HK
dc.identifier.scopusauthoridSun, J=8734512600en_HK
dc.identifier.scopusauthoridXiao, K=36117412300en_HK
dc.identifier.scopusauthoridArellano, SM=15831015600en_HK
dc.identifier.scopusauthoridThiyagarajan, V=6602476830en_HK
dc.identifier.scopusauthoridQian, PY=35240648600en_HK

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