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dc.contributor.authorZhang, Yi-Fan
dc.contributor.authorKitano, Yoshikazu
dc.contributor.authorNogata, Yasuyuki
dc.contributor.authorZhang, Yu
dc.contributor.authorQian, Pei-Yuan
dc.date.accessioned2015-04-16T13:59:12Z
dc.date.available2015-04-16T13:59:12Z
dc.date.issued2012-09-18
dc.identifier.citationThe Mode of Action of Isocyanide in Three Aquatic Organisms, Balanus amphitrite, Bugula neritina and Danio rerio 2012, 7 (9):e45442 PLoS ONE
dc.identifier.issn1932-6203
dc.identifier.pmid23029013
dc.identifier.doi10.1371/journal.pone.0045442
dc.identifier.urihttp://hdl.handle.net/10754/550218
dc.description.abstractIsocyanide is a potential antifouling compound in marine environments. In this study, we investigated its mode of action in three aquatic organisms. Two of them, the bryozoan Bugula neritina and the barnacle Balanus amphitrite, are major marine fouling invertebrates, and the other organism is the non-target species zebrafish Danio rerio. In the swimming larvae of B. neritina, isocyanide did not affect the total attachment rate (≤50 µg ml^(−1)), but it did change the attachment site by increasing the percentage of attachment on the bottom of the container rather than on the wall or air-water inter-surface. Isocyanide binds several proteins in B. neritina as identified via SDS-PAGE-LC-MS/MS: 1) a 30 kD protein band containing two proteins similar to voltage dependent anion channels (VDAC), which control the direct coupling of the mitochondrial matrix to the energy maintenance of the cytosol and the release of apoptogenic factors from mitochondria of mammalian cells; and 2) an unknown 39 kD protein. In B. amphitrite cyprids, the isocyanide binding protein were 1) a protein similar to NADH-ubiquinone oxidoreductase, which is the “entry enzyme” of oxidative phosphorylation in mitochondria; and 2) cytochrome P450. In Danio rerio embryos, isocyanide caused “wavy” notochords, hydrocephalus, pericardial edema, poor blood circulation, and defects in pigmentation and hematopoiesis, which phenocopied copper deficiency. This is the first report on isocyanide binding proteins in fouling organisms, as well as the first description of its phenotype and potential toxicology in zebrafish.
dc.description.sponsorshipThis study was supported by a research grant (DY125-15-T-02) from China Ocean Mineral Resources Research and Development Association, an award from King Abdullah University of Science and Technology (SA-C0040/UK-C0016) and grants from the Research Grants Council of the Hong Kong Special Administrative Region (N_HKUST602/09 and AoE/P-04/04-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.
dc.publisherPublic Library of Science (PLoS)
dc.relation.urlhttp://dx.plos.org/10.1371/journal.pone.0045442
dc.rightsThis 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.
dc.titleThe Mode of Action of Isocyanide in Three Aquatic Organisms, Balanus amphitrite, Bugula neritina and Danio rerio
dc.typeArticle
dc.identifier.journalPLoS ONE
dc.identifier.pmcidPMC3445549
dc.eprint.versionPublisher's Version/PDF
dc.contributor.institutionDivision of Life Science, Hong Kong University of Science and Technology, Hong Kong SAR, China
dc.contributor.institutionLaboratory of Bio-organic Chemistry, Tokyo University of Agriculture and Technology, Tokyo, Japan
dc.contributor.institutionAbiko Research Laboratory, Central Research Institute of Electric Power Industry, Chiba, Japan
kaust.personZhang, Yi-Fan
kaust.personZhang, Yu
kaust.personQian, Pei-Yuan
kaust.grant.numberSA-C0040
kaust.grant.numberUK-C0016
kaust.grant.programKAUST Global Collaborative Research Program
refterms.dateFOA2018-06-13T16:53:08Z


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