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dc.contributor.authorChandramouli, Kondethimmanahalli
dc.contributor.authorZhang, Yu
dc.contributor.authorWong, Yue Him
dc.contributor.authorQian, Pei-Yuan
dc.date.accessioned2016-02-28T07:59:14Z
dc.date.available2016-02-28T07:59:14Z
dc.date.issued2011-12-15
dc.identifier.citationChandramouli KH, Zhang Y, Wong YH, Qian P-Y (2012) Comparative Glycoproteome Analysis: Dynamics of Protein Glycosylation during Metamorphic Transition from Pelagic to Benthic Life Stages in Three Invertebrates. Journal of Proteome Research 11: 1330–1340. Available: http://dx.doi.org/10.1021/pr200982k.
dc.identifier.issn1535-3893
dc.identifier.issn1535-3907
dc.identifier.pmid22111546
dc.identifier.doi10.1021/pr200982k
dc.identifier.urihttp://hdl.handle.net/10754/600217
dc.description.abstractThe life cycle of most benthic marine invertebrates has two distinct stages: the pelagic larval stage and the sessile juvenile stage. The transition between the larval stage and the juvenile stage is often abrupt and may be triggered by post-translational modification of proteins. Glycosylation, a very important post-translational modification, influences the biological activity of proteins. We used two-dimensional gel electrophoresis (2-DE) followed by glycoprotein-specific fluorescence staining and mass spectrometry with the goal of identifying glycosylation pattern changes during larval settlement and metamorphosis in barnacles, bryozoans, and polychaetes. Our results revealed substantial changes in the protein glycosylation patterns from larval to juvenile stages. Before metamorphosis, the degree of protein glycosylation was high in the barnacle Balanus (=Amphibalanus) amphitrite and the spionid polychaete Pseudopolydora vexillosa, whereas it increased after metamorphosis in the bryozoan Bugula neritina. We identified 19 abundant and differentially glycosylated proteins in these three species. Among the proteins, cellular stress- and metabolism-related proteins exhibited distinct glycosylation in B. amphitrite and B. neritina, whereas fatty acid metabolism-related proteins were abundantly glycosylated in P. vexillosa. Furthermore, the protein and gene expression analysis of some selected glycoproteins revealed that the degree of protein glycosylation did not always complement with transcriptional and translational changes associated with the larval-juvenile transition. The current study provides preliminary information on protein glycosylation in marine invertebrates that will serve as a solid basis for future comprehensive analysis of glycobiology during larval settlement and metamorphosis. © 2011 American Chemical Society.
dc.description.sponsorshipThe authors thank Dr. Flora S. Y. Mok for her help in collecting P. vexillosa larvae, Dr. Kiyotaka Matsumura for his critical review of the manuscript, and Cherry Kwan for proof-reading the manuscript. This study was supported by an award from King Abdullah University of Science and Technology (SA-C0040/UK-00016) and a grant from the Research Grants Council of the Hong Kong Special Administrative Region (AoE/P-04/04-II) to P.-Y. Qian.
dc.publisherAmerican Chemical Society (ACS)
dc.subject2-DE
dc.subjectglycoproteomics
dc.subjectlarval metamorphosis
dc.subjectmarine invertebrates
dc.subjecttranscription
dc.subjecttranslation
dc.titleComparative Glycoproteome Analysis: Dynamics of Protein Glycosylation during Metamorphic Transition from Pelagic to Benthic Life Stages in Three Invertebrates
dc.typeArticle
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.contributor.departmentComputational Bioscience Research Center (CBRC)
dc.identifier.journalJournal of Proteome Research
dc.contributor.institutionHong Kong University of Science and Technology, Hong Kong, China
kaust.personChandramouli, Kondethimmanahalli
kaust.personZhang, Yu
kaust.personWong, Yue Him
kaust.personQian, Pei-Yuan
kaust.grant.numberSA-C0040
kaust.grant.numberUK-00016
kaust.grant.programKAUST Global Collaborative Research Program
dc.date.published-online2011-12-15
dc.date.published-print2012-02-03


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