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dc.contributor.authorZhang, Yu
dc.contributor.authorSun, Jin
dc.contributor.authorXiao, Kang
dc.contributor.authorArellano, Shawn M.
dc.contributor.authorThiyagarajan, Vengatesen
dc.contributor.authorQian, Pei-Yuan
dc.date.accessioned2016-02-28T07:59:10Z
dc.date.available2016-02-28T07:59:10Z
dc.date.issued2010-09-03
dc.identifier.citationZhang Y, Sun J, Xiao K, Arellano SM, Thiyagarajan V, et al. (2010) 2D Gel-Based Multiplexed Proteomic Analysis during Larval Development and Metamorphosis of the Biofouling Polychaete Tubeworm Hydroides elegans. Journal of Proteome Research 9: 4851–4860. Available: http://dx.doi.org/10.1021/pr100645z.
dc.identifier.issn1535-3893
dc.identifier.issn1535-3907
dc.identifier.pmid20666481
dc.identifier.doi10.1021/pr100645z
dc.identifier.urihttp://hdl.handle.net/10754/600214
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.
dc.description.sponsorshipWe thank Dr. Priscilla Leung, Mr. Jack Man (Genome Research Centre, HKU), and Ms Yin Ki Tam (Coastal Marine Laboratory, HKUST) for MS analysis, Dr. Kondethimmanahalli Chandramouli and Dr. Huoming Zhang for proof-reading the manuscripts, and other colleagues for constructive comments on this work. This work is supported by award SA-00040/UK-C0016 from the King Abdullah University of Science and Technology, and grants from China Ocean Mineral Resources Research and Development Association (COMRRDA06/07.Sc02) and RGC of HKSAR (N-HKUST602/09, 662408 and AoE/P-04/04-II) to P.-Y.Q.
dc.publisherAmerican Chemical Society (ACS)
dc.subject2-DE, multiplexed proteomics
dc.subjectHydroides elegans
dc.subjectlarval development
dc.subjectlarval metamorphosis
dc.subjectphosphoproteome
dc.subjectproteome
dc.title2D Gel-Based Multiplexed Proteomic Analysis during Larval Development and Metamorphosis of the Biofouling Polychaete Tubeworm Hydroides elegans
dc.typeArticle
dc.identifier.journalJournal of Proteome Research
dc.contributor.institutionDepartment of Biology, Hong Kong Baptist University, Hong Kong, Hong Kong
dc.contributor.institutionSwire Institute of Marine Science, School of Biological Sciences, University of Hong Kong, Hong Kong, Hong Kong
kaust.personZhang, Yu
kaust.personXiao, Kang
kaust.personArellano, Shawn M.
kaust.personQian, Pei-Yuan
kaust.grant.numberSA-00040
kaust.grant.numberUK-C0016
kaust.grant.programKAUST Global Collaborative Research Program


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