Quantitative proteomics identify molecular targets that are crucial in larval settlement and metamorphosis of bugula neritina

Handle URI:
http://hdl.handle.net/10754/564359
Title:
Quantitative proteomics identify molecular targets that are crucial in larval settlement and metamorphosis of bugula neritina
Authors:
Zhang, Huoming ( 0000-0001-5416-0358 ) ; Wong, Yuehim; Wang, Hao; Chen, Zhangfan; Arellano, Shawn M.; Ravasi, Timothy ( 0000-0002-9950-465X ) ; Qian, Peiyuan
Abstract:
The 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.
KAUST Department:
Biosciences Core Lab; Biological and Environmental Sciences and Engineering (BESE) Division; Bioscience Program; Computational Bioscience Research Center (CBRC); Materials Science and Engineering Program; Integrative Systems Biology Lab
Publisher:
American Chemical Society (ACS)
Journal:
Journal of Proteome Research
Issue Date:
7-Jan-2011
DOI:
10.1021/pr100817v
PubMed ID:
21090758
Type:
Article
ISSN:
15353893
Sponsors:
We 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.
Appears in Collections:
Articles; Bioscience Program; Biosciences Core Lab; Materials Science and Engineering Program; Computational Bioscience Research Center (CBRC); Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorZhang, Huomingen
dc.contributor.authorWong, Yuehimen
dc.contributor.authorWang, Haoen
dc.contributor.authorChen, Zhangfanen
dc.contributor.authorArellano, Shawn M.en
dc.contributor.authorRavasi, Timothyen
dc.contributor.authorQian, Peiyuanen
dc.date.accessioned2015-08-04T06:24:52Zen
dc.date.available2015-08-04T06:24:52Zen
dc.date.issued2011-01-07en
dc.identifier.issn15353893en
dc.identifier.pmid21090758en
dc.identifier.doi10.1021/pr100817ven
dc.identifier.urihttp://hdl.handle.net/10754/564359en
dc.description.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.en
dc.description.sponsorshipWe 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.en
dc.publisherAmerican Chemical Society (ACS)en
dc.subjectBiofoulingen
dc.subjectBugula neritinaen
dc.subjectLabel-free quantitative proteomicsen
dc.subjectLarval attachment and metamorphosisen
dc.titleQuantitative proteomics identify molecular targets that are crucial in larval settlement and metamorphosis of bugula neritinaen
dc.typeArticleen
dc.contributor.departmentBiosciences Core Laben
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.contributor.departmentBioscience Programen
dc.contributor.departmentComputational Bioscience Research Center (CBRC)en
dc.contributor.departmentMaterials Science and Engineering Programen
dc.contributor.departmentIntegrative Systems Biology Laben
dc.identifier.journalJournal of Proteome Researchen
dc.contributor.institutionHong Kong University of Science and Technology, Hong Kongen
kaust.authorZhang, Huomingen
kaust.authorWang, Haoen
kaust.authorRavasi, Timothyen
kaust.authorWong, Yuehimen
kaust.authorChen, Zhangfanen
kaust.authorArellano, Shawn M.en
kaust.authorQian, Peiyuanen
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