Expression of Calmodulin and Myosin Light Chain Kinase during Larval Settlement of the Barnacle Balanus amphitrite

Handle URI:
http://hdl.handle.net/10754/334586
Title:
Expression of Calmodulin and Myosin Light Chain Kinase during Larval Settlement of the Barnacle Balanus amphitrite
Authors:
Chen, Zhang-Fan; Wang, Hao; Matsumura, Kiyotaka; Qian, Pei-Yuan
Abstract:
Barnacles are one of the most common organisms in intertidal areas. Their life cycle includes seven free-swimming larval stages and sessile juvenile and adult stages. The transition from the swimming to the sessile stages, referred to as larval settlement, is crucial for their survivor success and subsequent population distribution. In this study, we focused on the involvement of calmodulin (CaM) and its binding proteins in the larval settlement of the barnacle, Balanus (= Amphibalanus) amphitrite. The full length of CaM gene was cloned from stage II nauplii of B. amphitrite (referred to as Ba-CaM), encoding 149 amino acid residues that share a high similarity with published CaMs in other organisms. Quantitative real-time PCR showed that Ba-CaM was highly expressed in cyprids, the stage at which swimming larvae are competent to attach and undergo metamorphosis. In situ hybridization revealed that the expressed Ba-CaM gene was localized in compound eyes, posterior ganglion and cement glands, all of which may have essential functions during larval settlement. Larval settlement assays showed that both the CaM inhibitor compound 48/80 and the CaM-dependent myosin light chain kinase (MLCK) inhibitor ML-7 effectively blocked barnacle larval settlement, whereas Ca 2+/CaM-dependent kinase II (CaMKII) inhibitors did not show any clear effects. The subsequent real-time PCR assay showed a higher expression level of Ba-MLCK gene in larval stages than in adults, suggesting an important role of Ba-MLCK gene in larval development and competency. Overall, the results suggest that CaM and CaM-dependent MLCK function during larval settlement of B. amphitrite. © 2012 Chen et al.
Citation:
Chen Z-F, Wang H, Matsumura K, Qian P-Y (2012) Expression of Calmodulin and Myosin Light Chain Kinase during Larval Settlement of the Barnacle Balanus amphitrite. PLoS ONE 7: e31337. doi:10.1371/journal.pone.0031337.
Publisher:
Public Library of Science (PLoS)
Journal:
PLoS ONE
KAUST Grant Number:
SA-C0040; UK-C0016
Issue Date:
13-Feb-2012
DOI:
10.1371/journal.pone.0031337
PubMed ID:
22348072
PubMed Central ID:
PMC3278446
Type:
Article
ISSN:
1932-6203
Sponsors:
This work was supported by an award (SA-C0040/UK-C0016) from King Abdullah University of Science and Technology and an Areas of Excellence (AoE) project of Hong Kong Special Administrative Region (AOE/P-04/04-2-II) to Pei-Yuan Qian. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
Appears in Collections:
Publications Acknowledging KAUST Support

Full metadata record

DC FieldValue Language
dc.contributor.authorChen, Zhang-Fanen
dc.contributor.authorWang, Haoen
dc.contributor.authorMatsumura, Kiyotakaen
dc.contributor.authorQian, Pei-Yuanen
dc.date.accessioned2014-11-11T14:30:58Z-
dc.date.available2014-11-11T14:30:58Z-
dc.date.issued2012-02-13en
dc.identifier.citationChen Z-F, Wang H, Matsumura K, Qian P-Y (2012) Expression of Calmodulin and Myosin Light Chain Kinase during Larval Settlement of the Barnacle Balanus amphitrite. PLoS ONE 7: e31337. doi:10.1371/journal.pone.0031337.en
dc.identifier.issn1932-6203en
dc.identifier.pmid22348072en
dc.identifier.doi10.1371/journal.pone.0031337en
dc.identifier.urihttp://hdl.handle.net/10754/334586en
dc.description.abstractBarnacles are one of the most common organisms in intertidal areas. Their life cycle includes seven free-swimming larval stages and sessile juvenile and adult stages. The transition from the swimming to the sessile stages, referred to as larval settlement, is crucial for their survivor success and subsequent population distribution. In this study, we focused on the involvement of calmodulin (CaM) and its binding proteins in the larval settlement of the barnacle, Balanus (= Amphibalanus) amphitrite. The full length of CaM gene was cloned from stage II nauplii of B. amphitrite (referred to as Ba-CaM), encoding 149 amino acid residues that share a high similarity with published CaMs in other organisms. Quantitative real-time PCR showed that Ba-CaM was highly expressed in cyprids, the stage at which swimming larvae are competent to attach and undergo metamorphosis. In situ hybridization revealed that the expressed Ba-CaM gene was localized in compound eyes, posterior ganglion and cement glands, all of which may have essential functions during larval settlement. Larval settlement assays showed that both the CaM inhibitor compound 48/80 and the CaM-dependent myosin light chain kinase (MLCK) inhibitor ML-7 effectively blocked barnacle larval settlement, whereas Ca 2+/CaM-dependent kinase II (CaMKII) inhibitors did not show any clear effects. The subsequent real-time PCR assay showed a higher expression level of Ba-MLCK gene in larval stages than in adults, suggesting an important role of Ba-MLCK gene in larval development and competency. Overall, the results suggest that CaM and CaM-dependent MLCK function during larval settlement of B. amphitrite. © 2012 Chen et al.en
dc.description.sponsorshipThis work was supported by an award (SA-C0040/UK-C0016) from King Abdullah University of Science and Technology and an Areas of Excellence (AoE) project of Hong Kong Special Administrative Region (AOE/P-04/04-2-II) to Pei-Yuan Qian. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.en
dc.language.isoenen
dc.publisherPublic Library of Science (PLoS)en
dc.rightsChen et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.en
dc.subject1 (5 iodo 1 naphthalenesulfonyl)hexahydro 1h 1,4 diazepineen
dc.subjectamino aciden
dc.subjectcalcium calmodulin dependent protein kinase IIen
dc.subjectcalmodulinen
dc.subjectmyosin light chain kinaseen
dc.subjectprotein kinase inhibitoren
dc.subjectcalmodulinen
dc.subjectmyosin light chain kinaseen
dc.subjectBalanus amphitriteen
dc.subjectbarnacleen
dc.subjectCaM geneen
dc.subjectcypris (larva)en
dc.subjectenzyme activityen
dc.subjectganglionen
dc.subjectgeneen
dc.subjectgene expression profilingen
dc.subjectgene locationen
dc.subjectin situ hybridizationen
dc.subjectlarval stageen
dc.subjectmetamorphosisen
dc.subjectmolecular cloningen
dc.subjectnauplius (larva)en
dc.subjectnucleotide sequenceen
dc.subjectprotein expressionen
dc.subjectquantitative analysisen
dc.subjectreverse transcription polymerase chain reactionen
dc.subjectbarnacleen
dc.subjectbiosynthesisen
dc.subjectDNA sequenceen
dc.subjectgeneticsen
dc.subjectlarvaen
dc.subjectlife cycle stageen
dc.subjectmetamorphosisen
dc.subjectphysiologyen
dc.subjectBalanus amphitriteen
dc.subjectCyprididaeen
dc.subjectThoracicaen
dc.subjectCalmodulinen
dc.subjectCloning, Molecularen
dc.subjectLarvaen
dc.subjectLife Cycle Stagesen
dc.subjectMetamorphosis, Biologicalen
dc.subjectMyosin-Light-Chain Kinaseen
dc.subjectSequence Analysis, DNAen
dc.subjectThoracicaen
dc.titleExpression of Calmodulin and Myosin Light Chain Kinase during Larval Settlement of the Barnacle Balanus amphitriteen
dc.typeArticleen
dc.identifier.journalPLoS ONEen
dc.identifier.pmcidPMC3278446en
dc.eprint.versionPublisher's Version/PDFen
dc.contributor.institutionKAUST Global Collaborative Research Program, Division of Life Science, The Hong Kong University of Science and Technology, Hong Kong SAR, Chinaen
dc.contributor.affiliationKing Abdullah University of Science and Technology (KAUST)en
kaust.authorWang, Haoen
kaust.authorChen, Zhangfanen
kaust.authorMatsumura, Kiyotakaen
kaust.authorQian, Peiyuanen
kaust.grant.numberSA-C0040en
kaust.grant.numberUK-C0016en
kaust.grant.programKAUST Global Collaborative Research Programen

Related articles on PubMed

All Items in KAUST are protected by copyright, with all rights reserved, unless otherwise indicated.