Identification of proteins from human permanent erupted enamel

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dc.contributor.authorCastiblanco, Gina A.
dc.contributor.authorRutishauser, Dorothea
dc.contributor.authorIlag, Leopold L.
dc.contributor.authorMartignon, Stefania
dc.contributor.authorCastellanos, Jaime
dc.contributor.authorMejía, Wilson
dc.contributor.orcidCastellanos, Jaime [0000-0003-1596-8383]
dc.contributor.orcidMartignon, Stefania [0000-0002-6505-8356]
dc.date.accessioned2020-08-10T16:45:55Z
dc.date.available2020-08-10T16:45:55Z
dc.date.issued2015
dc.description.abstractenglishProteins 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 trypsin‐digestion 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.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1111/eos.12214
dc.identifier.instnameinstname:Universidad El Bosquespa
dc.identifier.issn1600-0722
dc.identifier.reponamereponame:Repositorio Institucional Universidad El Bosquespa
dc.identifier.repourlhttps://repositorio.unbosque.edu.co
dc.identifier.urihttps://hdl.handle.net/20.500.12495/3735
dc.language.isoeng
dc.publisherWileyspa
dc.publisher.journalEuropean Journal of Oral Sciencesspa
dc.relation.ispartofseriesEuropean Journal of Oral Sciences, 1600-0722, Vol. 123, Nro. 6, 2015, p. 390-395spa
dc.relation.urihttps://onlinelibrary.wiley.com/doi/abs/10.1111/eos.12214
dc.rights.accessrightshttps://purl.org/coar/access_right/c_abf2
dc.rights.accessrightsinfo:eu-repo/semantics/openAccess
dc.rights.accessrightsAcceso abierto
dc.rights.creativecommons2015-10-03
dc.rights.localAcceso abiertospa
dc.subject.keywordsAmelogeninspa
dc.subject.keywordsDental enamel proteinsspa
dc.subject.keywordsEnamelinspa
dc.subject.keywordsMass spectrometryspa
dc.titleIdentification of proteins from human permanent erupted enamelspa
dc.title.translatedIdentification of proteins from human permanent erupted enamelspa
dc.type.coarhttps://purl.org/coar/resource_type/c_6501
dc.type.driverinfo:eu-repo/semantics/article
dc.type.hasversioninfo:eu-repo/semantics/publishedVersion
dc.type.localArtículo de revista

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