Identification of proteins from human permanent erupted enamel
Proteins 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 erup...
- Autores:
-
Castiblanco, Gina A.
Rutishauser, Dorothea
Ilag, Leopold L.
Martignon, Stefania
Castellanos, Jaime
Mejía, Wilson
- Tipo de recurso:
- Article of journal
- Fecha de publicación:
- 2015
- Institución:
- Universidad El Bosque
- Repositorio:
- Repositorio U. El Bosque
- Idioma:
- eng
- OAI Identifier:
- oai:repositorio.unbosque.edu.co:20.500.12495/3735
- Acceso en línea:
- http://hdl.handle.net/20.500.12495/3735
https://doi.org/10.1111/eos.12214
https://repositorio.unbosque.edu.co
- Palabra clave:
- Amelogenin
Dental enamel proteins
Enamelin
Mass spectrometry
- Rights
- openAccess
- License
- Acceso abierto
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Repositorio U. El Bosque |
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|
dc.title.spa.fl_str_mv |
Identification of proteins from human permanent erupted enamel |
dc.title.translated.spa.fl_str_mv |
Identification of proteins from human permanent erupted enamel |
title |
Identification of proteins from human permanent erupted enamel |
spellingShingle |
Identification of proteins from human permanent erupted enamel Amelogenin Dental enamel proteins Enamelin Mass spectrometry |
title_short |
Identification of proteins from human permanent erupted enamel |
title_full |
Identification of proteins from human permanent erupted enamel |
title_fullStr |
Identification of proteins from human permanent erupted enamel |
title_full_unstemmed |
Identification of proteins from human permanent erupted enamel |
title_sort |
Identification of proteins from human permanent erupted enamel |
dc.creator.fl_str_mv |
Castiblanco, Gina A. Rutishauser, Dorothea Ilag, Leopold L. Martignon, Stefania Castellanos, Jaime Mejía, Wilson |
dc.contributor.author.none.fl_str_mv |
Castiblanco, Gina A. Rutishauser, Dorothea Ilag, Leopold L. Martignon, Stefania Castellanos, Jaime Mejía, Wilson |
dc.contributor.orcid.none.fl_str_mv |
Castellanos, Jaime [0000-0003-1596-8383] Martignon, Stefania [0000-0002-6505-8356] |
dc.subject.keywords.spa.fl_str_mv |
Amelogenin Dental enamel proteins Enamelin Mass spectrometry |
topic |
Amelogenin Dental enamel proteins Enamelin Mass spectrometry |
description |
Proteins 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. |
publishDate |
2015 |
dc.date.issued.none.fl_str_mv |
2015 |
dc.date.accessioned.none.fl_str_mv |
2020-08-10T16:45:55Z |
dc.date.available.none.fl_str_mv |
2020-08-10T16:45:55Z |
dc.type.coar.fl_str_mv |
http://purl.org/coar/resource_type/c_2df8fbb1 |
dc.type.coarversion.fl_str_mv |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
dc.type.local.none.fl_str_mv |
Artículo de revista |
dc.type.coar.none.fl_str_mv |
http://purl.org/coar/resource_type/c_6501 |
dc.type.driver.none.fl_str_mv |
info:eu-repo/semantics/article |
format |
http://purl.org/coar/resource_type/c_6501 |
dc.identifier.issn.none.fl_str_mv |
1600-0722 |
dc.identifier.uri.none.fl_str_mv |
http://hdl.handle.net/20.500.12495/3735 |
dc.identifier.doi.none.fl_str_mv |
https://doi.org/10.1111/eos.12214 |
dc.identifier.instname.spa.fl_str_mv |
instname:Universidad El Bosque |
dc.identifier.reponame.spa.fl_str_mv |
reponame:Repositorio Institucional Universidad El Bosque |
dc.identifier.repourl.none.fl_str_mv |
https://repositorio.unbosque.edu.co |
identifier_str_mv |
1600-0722 instname:Universidad El Bosque reponame:Repositorio Institucional Universidad El Bosque |
url |
http://hdl.handle.net/20.500.12495/3735 https://doi.org/10.1111/eos.12214 https://repositorio.unbosque.edu.co |
dc.language.iso.none.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartofseries.spa.fl_str_mv |
European Journal of Oral Sciences, 1600-0722, Vol. 123, Nro. 6, 2015, p. 390-395 |
dc.relation.uri.none.fl_str_mv |
https://onlinelibrary.wiley.com/doi/abs/10.1111/eos.12214 |
dc.rights.local.spa.fl_str_mv |
Acceso abierto |
dc.rights.accessrights.none.fl_str_mv |
http://purl.org/coar/access_right/c_abf2 info:eu-repo/semantics/openAccess Acceso abierto |
dc.rights.creativecommons.none.fl_str_mv |
2015-10-03 |
rights_invalid_str_mv |
Acceso abierto http://purl.org/coar/access_right/c_abf2 2015-10-03 |
eu_rights_str_mv |
openAccess |
dc.format.mimetype.none.fl_str_mv |
application/pdf |
dc.publisher.spa.fl_str_mv |
Wiley |
dc.publisher.journal.spa.fl_str_mv |
European Journal of Oral Sciences |
institution |
Universidad El Bosque |
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Castiblanco, Gina A.Rutishauser, DorotheaIlag, Leopold L.Martignon, StefaniaCastellanos, JaimeMejía, WilsonCastellanos, Jaime [0000-0003-1596-8383]Martignon, Stefania [0000-0002-6505-8356]2020-08-10T16:45:55Z2020-08-10T16:45:55Z20151600-0722http://hdl.handle.net/20.500.12495/3735https://doi.org/10.1111/eos.12214instname:Universidad El Bosquereponame:Repositorio Institucional Universidad El Bosquehttps://repositorio.unbosque.edu.coapplication/pdfengWileyEuropean Journal of Oral SciencesEuropean Journal of Oral Sciences, 1600-0722, Vol. 123, Nro. 6, 2015, p. 390-395https://onlinelibrary.wiley.com/doi/abs/10.1111/eos.12214Identification of proteins from human permanent erupted enamelIdentification of proteins from human permanent erupted enamelArtículo de revistahttp://purl.org/coar/resource_type/c_6501http://purl.org/coar/resource_type/c_2df8fbb1info:eu-repo/semantics/articlehttp://purl.org/coar/version/c_970fb48d4fbd8a85AmelogeninDental enamel proteinsEnamelinMass spectrometryProteins 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.Acceso abiertohttp://purl.org/coar/access_right/c_abf2info:eu-repo/semantics/openAccessAcceso abierto2015-10-03ORIGINALCastiblanco, Gina A..pdfCastiblanco, Gina A..pdfapplication/pdf133105https://repositorio.unbosque.edu.co/bitstreams/35b47a6b-f71f-4126-a226-78439a10e798/download77bb7fe1beb18def1a35742c45a4950cMD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://repositorio.unbosque.edu.co/bitstreams/a1136cce-ff74-4fd3-942d-57ed6021a229/download8a4605be74aa9ea9d79846c1fba20a33MD52THUMBNAILCastiblanco, Gina A..pdf.jpgCastiblanco, Gina A..pdf.jpgimage/jpeg5775https://repositorio.unbosque.edu.co/bitstreams/5f22381e-5fe3-4cd7-abee-ecf8323c72c9/download7210a811635d1799e7c05fee5d259be7MD53TEXTCastiblanco, Gina A..pdf.txtCastiblanco, Gina A..pdf.txtExtracted texttext/plain29819https://repositorio.unbosque.edu.co/bitstreams/96b2196e-33fb-4e64-8698-0f364758ebb6/downloade56a56058e1426704900982e56edb48bMD5420.500.12495/3735oai:repositorio.unbosque.edu.co:20.500.12495/37352024-02-06 23:10:56.213restrictedhttps://repositorio.unbosque.edu.coRepositorio Institucional Universidad El Bosquebibliotecas@biteca.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 |