Quantitative proteomics identify molecular targets that are crucial in larval settlement and metamorphosis of bugula neritina
Arellano, Shawn M.
KAUST DepartmentComputational Bioscience Research Center (CBRC)
Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division
Biological and Environmental Sciences and Engineering (BESE) Division
Bioscience Core Lab
Materials Science and Engineering Program
Integrative Systems Biology Lab
Permanent link to this recordhttp://hdl.handle.net/10754/564359
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AbstractThe marine invertebrate Bugula neritina has a biphasic life cycle that consists of a swimming larval stage and a sessile juvenile and adult stage. The attachment of larvae to the substratum and their subsequent metamorphosis have crucial ecological consequences. Despite many studies on this species, little is known about the molecular mechanism of these processes. Here, we report a comparative study of swimming larvae and metamorphosing individuals at 4 and 24 h postattachment using label-free quantitative proteomics. We identified more than 1100 proteins at each stage, 61 of which were differentially expressed. Specifically, proteins involved in energy metabolism and structural molecules were generally down-regulated, whereas proteins involved in transcription and translation, the extracellular matrix, and calcification were strongly up-regulated during metamorphosis. Many tightly regulated novel proteins were also identified. Subsequent analysis of the temporal and spatial expressions of some of the proteins and an assay of their functions indicated that they may have key roles in metamorphosis of B. neritina. These findings not only provide molecular evidence with which to elucidate the substantial changes in morphology and physiology that occur during larval attachment and metamorphosis but also identify potential targets for antifouling treatment. © 2011 American Chemical Society.
SponsorsWe thank Jin Sun for his invaluable discussion and Cherry Hoi Ting Kwan for her comments on the manuscript. This study was supported by award SA-C0040/UK-C0016 from the King Abdullah University of Science and Technology, and grants (N-HKUST602/09 662408 and AoE/P-04/04-II) from the Research Grants Council of the Hong Kong Special Administrative Region to P.Y.Q.
PublisherAmerican Chemical Society (ACS)
JournalJournal of Proteome Research
CollectionsArticles; Biological and Environmental Sciences and Engineering (BESE) Division; Bioscience Program; Material Science and Engineering Program; Computational Bioscience Research Center (CBRC); Bioscience Core Lab; Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division
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