2D Gel-Based Multiplexed Proteomic Analysis during Larval Development and Metamorphosis of the Biofouling Polychaete Tubeworm Hydroides elegans
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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.
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.
SponsorsWe 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.
PublisherAmerican Chemical Society (ACS)
JournalJournal of Proteome Research
CollectionsPublications Acknowledging KAUST Support
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