Comparación del contenido proteico del esmalte de dientes permanentes sanos y con fluorosis

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dc.contributor.advisorMejía Naranjo, Wilson Alfonso
dc.contributor.advisorCastellanos Parra, Jaime Eduardo
dc.contributor.advisorMartignon, Stefania
dc.contributor.authorCastiblanco Rubio, Gina Alejandra
dc.date.accessioned2021-09-10T16:50:22Z
dc.date.available2021-09-10T16:50:22Z
dc.date.issued2014
dc.description.abstractEl esmalte con fluorosis es menos mineralizado y más poroso que el esmalte sano y durante el desarrollo retiene mayor contenido proteico. La evidencia en esmalte fluorótico erupcionado es contradictoria y no se conoce (en comparación al esmalte sano) si tiene mayor abundancia de péptidos, sus características, ni las proteínas de las que provienen. Identificar y comparar el material proteico del esmalte dental erupcionado sano y con fluorosis moderada usando Cromatografía Líquida acoplada a Espectrometría de Masas en Tándem (LC-MS/MS). Se estandarizó el protocolo de extracción de proteínas con TCA. Se obtuvo el extracto proteico del esmalte de 8 molares sanos (n=4) y con fluorosis dental moderada (n=4). Sin digestión previa con tripsina, se analizaron con LC-MS/MS y se utilizó la base de datos de SwissProt usando Mascot 2.3. Se consideraron identificaciones con puntaje ≥24 y se elaboró un listado con los péptidos de AMELX comunes a todas las muestras (puntaje ≥10), se determinó su abundancia relativa y se comparó entre los grupos (sano/fluorosis) con la prueba t-Student. Los sitios naturales de corte se compararon con los reportados en la literatura. Se predijo la estructura terciaria de la amelogenina con el servidor I-Tasser y la cuaternaria con Z-DOCK. Las imágenes se editaron en Pymol. Se identificaron tres proteínas específicas del esmalte: AMELX/Y, AMBN y ENAM, estas dos últimas se reportan por primera vez en esmalte erupcionado. Mientras que AMEL se identificó en todas las muestras, ENAM se encontró solo en el 50% de los dientes fluoróticos. Se obtuvieron las secuencias de 19 péptidos de AMELX comunes a los dos tipos de esmalte que mostraron sitios de clivaje previamente reportados para MMP-20 y KLK-4; tienen de 8 a 18 residuos, masas moleculares menores a 2 kDa, provienen en su mayoría de la región N-terminal y se ubican internamente en nuestra predicción de la estructura terciaria y cuaternaria de AMELX. No encontramos diferencias significativas en la abundancia relativa de los péptidos de los dos tipos de esmalte. Con estos resultados sugerimos un posible papel de ENAM en la patogénesis de la fluorosis dental y soportamos la hipótesis de que en la fluorosis se presenta retraso en el corte de amelogenina y no retención permanente de sus péptidos en el esmalte erupcionado.spa
dc.description.abstractenglishFluorosed enamel is less mineralized and more porous than sound enamel and during its development, retains more protein content. There is contradictory evidence in erupted human teeth: no reports are available on its protein identities, nor the characteristics and relative abundance of the peptides from erupted sound and fluorosed enamel. To identify and compare the proteins from human erupted sound and moderately fluorosed enamel by Liquid Chromatography coupled with Tandem Mass Spectrometry (LC-MS/MS). Permanent human erupted third molars were collected (TFI-0/TFI-3). Protein extraction was performed with TCA as previously reported. The extract from 8 erupted permanent sound (n=4) and mildly-fluorosed (n=4) erupted molars was processed for LCMS/MS without prior trypsin digestion. The chromatographic separation was achieved with acetonitrile/water solvent system containing 0.2% formic acid. The MS acquisition method was comprised of one survey scan ranging from m/z 300 to m/z 1650 with R=70,000 at m/z 400, followed by 10 data-dependent MS/MS scans from the top 10 precursor ions with a charge status ≥ 2. The data was searched against SwissProt protein database using Mascot 2.3. Peptides common to all samples with scores ≥ 10 were selected for quantification of relative abundance. Comparisons between peptide abundances were made with student’s t test. Amelogenin structure was predicted with I-Tasser server and molecular interactions with Z-DOCK.. Images were edited in Pymol. Four enamel-specific proteins were identified: AMEL isoforms X/Y, ENAM, and AMBN. While we found AMEL in 100% of samples, ENAM was only in 50% of fluorosed teeth. We found 19 peptide sequences common for both types of enamel, displaying natural cleavage sites previously reported for MMP-20 and KLK-4: they had 8-18 residues and molecular masses less than 2 kDa. Most of them belong to the AMEL N-terminal region and localize in the inner part of our amelogenin predicted structure. We didn’t find significant differences between relative abundances of the peptides. We suggest a possible role for ENAM in dental fluorosis and support the hypothesis that in fluorosis there are delays in amelogenin removal rather than permanent retention of its peptides.eng
dc.description.degreelevelMaestríaspa
dc.description.degreenameMagíster en Ciencias Básicas Biomédicasspa
dc.format.mimetypeapplication/pdf
dc.identifier.instnameinstname:Universidad El Bosquespa
dc.identifier.reponamereponame:Repositorio Institucional Universidad El Bosquespa
dc.identifier.repourlrepourl:https://repositorio.unbosque.edu.co
dc.identifier.urihttps://hdl.handle.net/20.500.12495/6048
dc.language.isospa
dc.publisher.facultyFacultad de Medicinaspa
dc.publisher.grantorUniversidad El Bosquespa
dc.publisher.programMaestría en Ciencias Básicas Biomédicasspa
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dc.rightsAttribution-NonCommercial-ShareAlike 4.0 International*
dc.rights.accessrightsinfo:eu-repo/semantics/openAccess
dc.rights.accessrightshttps://purl.org/coar/access_right/c_abf2
dc.rights.creativecommons2014
dc.rights.localAcceso abiertospa
dc.rights.urihttps://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subjectEsmalte dentalspa
dc.subjectProteínas del esmalte dentalspa
dc.subjectFluorosis dentalspa
dc.subject.decsEsmalte dentalspa
dc.subject.decsFluorosis dentalspa
dc.subject.decsProteínas del esmalte dentalspa
dc.subject.keywordsDental enamelspa
dc.subject.keywordsDental enamel proteinsspa
dc.subject.keywordsDental fluorosisspa
dc.subject.keywordsAmelogeninspa
dc.subject.nlmW 50
dc.titleComparación del contenido proteico del esmalte de dientes permanentes sanos y con fluorosisspa
dc.title.translatedComparison between protein content from permanent sound and fluorosed teethspa
dc.type.coarhttps://purl.org/coar/resource_type/c_bdcc
dc.type.coarversionhttps://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.driverinfo:eu-repo/semantics/masterThesis
dc.type.hasversioninfo:eu-repo/semantics/acceptedVersion
dc.type.localTesis/Trabajo de grado - Monografía - Maestríaspa

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Maestría en Ciencias Básicas Biomédicas