Repository logo
 
Publication

2-D difference gel electrophoresis approach to assess protein expression profiles in Bathymodiolus azoricus from Mid-Atlantic Ridge hydrothermal vents

dc.contributor.authorCompany, Rui
dc.contributor.authorAntĂșnez, Oreto
dc.contributor.authorBebianno, Maria JoĂŁo
dc.contributor.authorCajaraville, Miren P.
dc.contributor.authorTorreblanca, Amparo
dc.date.accessioned2020-04-27T13:27:33Z
dc.date.available2020-04-27T13:27:33Z
dc.date.issued2011
dc.description.abstractHydrothermal vent mussels Bathymodiolus azoricus are naturally exposed to toxic chemical species originated directly from vent chimneys. The amount of toxic elements varies significantly among vent sites along the Mid-Atlantic Ridge and B. azoricus must be able to adapt to changes in hydrothermal fluid composition, temperature and pressure. The aim of this work was to study changes in the proteome in the "gill-bacteria complex" of mussels B. azoricus from three hydrothermal vent sites with distinct environmental characteristics using 2-D Fluorescence Difference Gel Electrophoresis (2-D DIGE). Results showed that 31 proteins had different expression profiles among vent sites and both cluster and principal component analysis confirm a clear separation of mussels between sites. This suggests the existence of specific parameters grouping individuals from the same hydrothermal site. Protein spots of the more abundant differentially expressed proteins were excised, digested with trypsin and identified by mass spectrometry. All identified proteins (actin, ubiquinone, S-adenosylhomocysteine hydrolase, cysteine peptidases, chaperonin and catalase) have been related previously with oxidative stress conditions and are known to be affected by ROS inducing stressors, including metals. Results point out to specific adaptations at the proteome level of B. azoricus depending on the level of toxicants present in their environment.pt_PT
dc.description.sponsorship5th PCRD Ventox project (EVK3CT1999-00003)pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.doihttps://doi.org/10.1016/j.jprot.2011.07.012pt_PT
dc.identifier.issn1874-3919
dc.identifier.urihttp://hdl.handle.net/10400.1/13791
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherElsevierpt_PT
dc.relationA PROTEOMIC APPROACH TO THE INVESTIGATION OF MOLECULAR MECHANISMS INVOLVED IN OXIDATIVE STRESS RESISTANCE IN HYDROTHERMAL AND COASTAL MARINE ORGANISMS
dc.relation.publisherversionhttps://www.sciencedirect.com/science/article/pii/S1874391911003319?via%3Dihubpt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectAdaptationpt_PT
dc.subjectAnimalspt_PT
dc.subjectElectrophoresispt_PT
dc.subjectGene expression profilingpt_PT
dc.subjectGene expression Regulationpt_PT
dc.subjectHydrothermal ventspt_PT
dc.subjectMytilidaept_PT
dc.subjectProteomept_PT
dc.subjectBathymodiolus azoricuspt_PT
dc.subject2-D DIGEpt_PT
dc.title2-D difference gel electrophoresis approach to assess protein expression profiles in Bathymodiolus azoricus from Mid-Atlantic Ridge hydrothermal ventspt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleA PROTEOMIC APPROACH TO THE INVESTIGATION OF MOLECULAR MECHANISMS INVOLVED IN OXIDATIVE STRESS RESISTANCE IN HYDROTHERMAL AND COASTAL MARINE ORGANISMS
oaire.awardURIinfo:eu-repo/grantAgreement/FCT//SFRH%2FBPD%2F26399%2F2006/PT
oaire.citation.endPage2919pt_PT
oaire.citation.issue12pt_PT
oaire.citation.startPage2909pt_PT
oaire.citation.titleJournal of Proteomicspt_PT
oaire.citation.volume74pt_PT
person.familyNameBebianno
person.givenNameMaria
person.identifier.ciencia-id2B11-46AC-B94B
person.identifier.orcid0000-0003-1492-8566
person.identifier.scopus-author-id7004152715
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a CiĂȘncia e a Tecnologia
rcaap.rightsrestrictedAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublication2e00a26d-1dd3-4c22-a6bf-ac7943ae0d32
relation.isAuthorOfPublication.latestForDiscovery2e00a26d-1dd3-4c22-a6bf-ac7943ae0d32
relation.isProjectOfPublication3793dcb2-53f7-464c-bdb8-3fcdd7fc2e6e
relation.isProjectOfPublication.latestForDiscovery3793dcb2-53f7-464c-bdb8-3fcdd7fc2e6e

Files

Original bundle
Now showing 1 - 1 of 1
No Thumbnail Available
Name:
Company et al J Proteomics in press.pdf
Size:
833.19 KB
Format:
Adobe Portable Document Format