Publication:
Identification of proteins from human permanent erupted enamel

Simple item page
col.comunidadvinculadaComunidad odontológica colombianaes_CO
col.contrato0442-2012es_CO
col.date.proyecto2016-12
col.programa.colcienciasPrograma de Ciencia y Tecnología e Innovación en Saludes_CO
col.tipo.espArtículos de investigaciónes_CO
dc.audienceProfesoreses_CO
dc.audienceInvestigadoreses_CO
dc.coverage.spatialColombiaes_CO
dc.creatorCastiblanco Rubio, Gina Alejandra
dc.creatorRutishauser, Dorothea
dc.creatorIlag, Leopold L.
dc.creatorMartignon Biermann, Stefania
dc.creatorCastellanos, Jaime Eduardo
dc.creatorMejía, Wilson
dc.creator.corporativoUniversidad El Bosque - UNICA, Caries Research Unites_CO
dc.creator.corporativoIndiana University School of Dentistry, IUSDes_CO
dc.creator.mailmartignonstefania@unbosque.edu.coes_CO
dc.date.accessioned2019-03-26T15:01:29Z
dc.date.available2019-03-26T15:01:29Z
dc.date.embargoEndinfo:eu-repo/date/embargoEnd/2024-01-31es_CO
dc.date.issued2015-09
dc.description.abstractProteins from the extracellular matrix of enamel are highly specific and necessary for proper enamel formation. Most proteins are removed from the matrix by enamel proteases before complete mineralization is achieved; however, some residual protein fragments persist in the mineralized matrix of erupted enamel. So far, only amelogenin peptides obtained by traditional bottom-up proteomics have been recovered and identified in human permanent erupted enamel. In this study, we hypothesize that other enamel-specific proteins are also found in human permanent enamel, by analysing human erupted third molars. Pulverized enamel was used to extract proteins, and the protein extract was subjected directly to liquid-chromatography coupled to tandem mass spectrometry (LC-MS/MS) without a previous trypsindigestion step. Amelogenin and non-amelogenin proteins (ameloblastin and enamelin) were succesfully identified. The sequences of the naturally occurring peptides of these proteins are reported, finding in particular that most of the peptides from the amelogenin X-isoform come from the tyrosine-rich amelogenin peptide (TRAP) and that some were identified in all specimens. In conclusion, our LC-MS/MS method without trypsin digestion increased the coverage of identification of the enamel proteome from a few amelogenin peptides to a higher number of peptides from three enamel-specific proteins.es_CO
dc.description.isprojectnoes_CO
dc.description.projectid1308-569-34427es_CO
dc.description.projectnameModelo de caracterización ambiental, epidemológica, clínico-histológica e inorgánica de la fluorosis dental en niñoses_CO
dc.description.sponsorshipDepartamento Administrativo de Ciencia, Tecnología e Innovación [CO] Colcienciases_CO
dc.formatpdfes_CO
dc.format.extent6 páginases_CO
dc.identifier.bibliographicCitationContiene 34 referencias bibliográficas. Véase el documento adjuntoes_CO
dc.identifier.doi10.1111/eos.12214
dc.identifier.urihttp://repositorio.colciencias.gov.co/handle/11146/34142
dc.language.isoenges_CO
dc.relation.ispartofModelo de caracterización ambiental, epidemiológica, clínico-histológica e inorgánica de la fluorosis dental en niños. La publicación completa está disponible en : <a href="http://repositorio.colciencias.gov.co:80/handle/11146/34140" target="blank">http://repositorio.colciencias.gov.co:80/handle/11146/34140</a>es_CO
dc.rightsinfo:eu-repo/semantics/embargoedAccesses_CO
dc.sourceEuropean Journal Oral Science 2015; 1-6es_CO
dc.subject.lembEsmaltees_CO
dc.subject.lembAmelogenines_CO
dc.subject.lembDental enameles_CO
dc.subject.lembFluoridees_CO
dc.subject.spinesCaries dentales_CO
dc.subject.spinesFlour -- Investigacioneses_CO
dc.titleIdentification of proteins from human permanent erupted enameles_CO
dc.typeArtículo científicoes_CO
dc.type.driverinfo:eu-repo/semantics/articlees_CO
dc.type.hasversioninfo:eu-repo/semantics/publishedVersiones_CO
dspace.entity.typePublication

Files

Collections

Informes Finales