Contribución al estudio de la función de las elastasas en la degradación de elastina aislada de piel humana

ilustraciones, diagramas, fotografías

Autores:: García Manosalva, Leidy Carolina

Tipo de recurso:

Fecha de publicación:: 2024

Institución:: Universidad Nacional de Colombia

Repositorio:: Universidad Nacional de Colombia

Idioma:: spa

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network_acronym_str	UNACIONAL2
network_name_str	Universidad Nacional de Colombia
repository_id_str
dc.title.spa.fl_str_mv	Contribución al estudio de la función de las elastasas en la degradación de elastina aislada de piel humana
dc.title.translated.eng.fl_str_mv	Contribution to understanding the role of elastases in the degradation of elastin derived from human skin
title	Contribución al estudio de la función de las elastasas en la degradación de elastina aislada de piel humana
spellingShingle	Contribución al estudio de la función de las elastasas en la degradación de elastina aislada de piel humana 610 - Medicina y salud::615 - Farmacología y terapéutica Catepsina G Metaloproteinasas de la Matriz Ácidos Fíbricos Envejecimiento de la Piel Cathepsin G Matrix Metalloproteinases Fibric Acids Skin Aging Elastina Elastasas Integridad de fibra Potencia elastolítica Elastin Elastases Fibre integrity Elastolytic power
title_short	Contribución al estudio de la función de las elastasas en la degradación de elastina aislada de piel humana
title_full	Contribución al estudio de la función de las elastasas en la degradación de elastina aislada de piel humana
title_fullStr	Contribución al estudio de la función de las elastasas en la degradación de elastina aislada de piel humana
title_full_unstemmed	Contribución al estudio de la función de las elastasas en la degradación de elastina aislada de piel humana
title_sort	Contribución al estudio de la función de las elastasas en la degradación de elastina aislada de piel humana
dc.creator.fl_str_mv	García Manosalva, Leidy Carolina
dc.contributor.advisor.spa.fl_str_mv	Mora Huertas, Angela Cristina
dc.contributor.author.spa.fl_str_mv	García Manosalva, Leidy Carolina
dc.contributor.researchgroup.spa.fl_str_mv	Grupo de investigación en tecnologías analíticas farmacéuticas
dc.subject.ddc.spa.fl_str_mv	610 - Medicina y salud::615 - Farmacología y terapéutica
topic	610 - Medicina y salud::615 - Farmacología y terapéutica Catepsina G Metaloproteinasas de la Matriz Ácidos Fíbricos Envejecimiento de la Piel Cathepsin G Matrix Metalloproteinases Fibric Acids Skin Aging Elastina Elastasas Integridad de fibra Potencia elastolítica Elastin Elastases Fibre integrity Elastolytic power
dc.subject.decs.spa.fl_str_mv	Catepsina G Metaloproteinasas de la Matriz Ácidos Fíbricos Envejecimiento de la Piel
dc.subject.decs.eng.fl_str_mv	Cathepsin G Matrix Metalloproteinases Fibric Acids Skin Aging
dc.subject.proposal.spa.fl_str_mv	Elastina Elastasas Integridad de fibra Potencia elastolítica
dc.subject.proposal.eng.fl_str_mv	Elastin Elastases Fibre integrity Elastolytic power
description	ilustraciones, diagramas, fotografías
publishDate	2024
dc.date.accessioned.none.fl_str_mv	2024-07-16T19:43:25Z
dc.date.available.none.fl_str_mv	2024-07-16T19:43:25Z
dc.date.issued.none.fl_str_mv	2024
dc.type.spa.fl_str_mv	Trabajo de grado - Maestría
dc.type.driver.spa.fl_str_mv	info:eu-repo/semantics/masterThesis
dc.type.version.spa.fl_str_mv	info:eu-repo/semantics/acceptedVersion
dc.type.content.spa.fl_str_mv	Text
dc.type.redcol.spa.fl_str_mv	http://purl.org/redcol/resource_type/TM
status_str	acceptedVersion
dc.identifier.uri.none.fl_str_mv	https://repositorio.unal.edu.co/handle/unal/86475
dc.identifier.instname.spa.fl_str_mv	Universidad Nacional de Colombia
dc.identifier.reponame.spa.fl_str_mv	Repositorio Institucional Universidad Nacional de Colombia
dc.identifier.repourl.spa.fl_str_mv	https://repositorio.unal.edu.co/
url	https://repositorio.unal.edu.co/handle/unal/86475 https://repositorio.unal.edu.co/
identifier_str_mv	Universidad Nacional de Colombia Repositorio Institucional Universidad Nacional de Colombia
dc.language.iso.spa.fl_str_mv	spa
language	spa
dc.relation.indexed.spa.fl_str_mv	Bireme
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dc.publisher.spa.fl_str_mv	Universidad Nacional de Colombia
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dc.publisher.branch.spa.fl_str_mv	Universidad Nacional de Colombia - Sede Bogotá
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spelling	Atribución-NoComercial 4.0 Internacionalhttp://creativecommons.org/licenses/by-nc/4.0/info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2Mora Huertas, Angela Cristinaed4f68971b26575e5681f3321a6085adGarcía Manosalva, Leidy Carolinaa780b73801c24ec612b6946eaac4aff7Grupo de investigación en tecnologías analíticas farmacéuticas2024-07-16T19:43:25Z2024-07-16T19:43:25Z2024https://repositorio.unal.edu.co/handle/unal/86475Universidad Nacional de ColombiaRepositorio Institucional Universidad Nacional de Colombiahttps://repositorio.unal.edu.co/ilustraciones, diagramas, fotografíasLa elastina es una proteína de la matriz extracelular que provee elasticidad y resiliencia a los tejidos. Durante su tiempo de vida media (74 años), continuamente es degradada principalmente por enzimas denominadas elastasas, lo que se asocia con la aparición de signos del envejecimiento cutáneo, desarrollo de enfermedades como aneurismas y aterosclerosis, entre otras. Es necesario entender los factores que influyen en la proteólisis enzimática de las fibras de elastina para en un futuro, poder retrasar o controlar este proceso. Se han identificado en la piel doce elastasas pertenecientes a tres diferentes familias de proteasas: cistein, serin y metaloproteasas. El tejido de origen de la elastina y la integridad de la fibra pueden condicionar la acción de las enzimas; pocos reportes han evaluado el efecto de estos factores sobre la potencia elastolítica, y algunos han encontrado comportamientos disimiles entre ellos. Para contribuir a la comprensión del efecto de la integridad de la fibra de elastina sobre la actividad de las elastasas, en esta tesis inicialmente se implementaron un método de aislamiento de elastina y dos metodologías analíticas para hacer el seguimiento a la degradación inducida por Catepsina G y V, Metaloproteinasa de la matriz 9 y Elastasa Pancreática. Los resultados obtenidos permiten concluir que el daño previo de la fibra no influye igual en la actividad de todas las enzimas y es necesario continuar estudiando la interacción entre tipo de elastasa y grado de degradación de la fibra, con el objetivo de establecer las enzimas de mayor relevancia en el inicio de la degradación de la elastina. (Texto tomado de la fuente).Elastin is an extracellular matrix protein that provides elasticity and resilience to tissues. During its half-life (74 years), it is continuously degraded, mainly by enzymes called elastases. Elastin damage is associated with the appearance of signs of skin ageing and the development of diseases such as aneurysms and atherosclerosis, among others. Understanding the factors that influence the enzymatic proteolysis of elastin fibres is crucial for developing strategies to delay or control this process. Twelve elastases belonging to three different families of proteases have been identified in the skin: cysteine, serin and metalloproteases. The tissue of elastin's origin and the fibre's integrity can condition the enzymes' action. Only some researchers have evaluated the effect of these factors on elastolytic activity, and some have found dissimilar behaviours between them. To contribute to the understanding of the effect of the integrity of the elastin fibre on the activity of elastases, in this thesis, an elastin isolation method and two analytical methodologies were initially implemented to monitor the degradation induced by Cathepsin G and V, Matrix Metalloproteinase 9 and Pancreatic Elastase. The results allow us to conclude that previous damage to the fibre does not influence the activity of all enzymes in the same way, and it is necessary to continue studying the interaction between the type of elastase and the degree of fibre damage to establish the most relevant enzymes at the beginning of elastin degradation.MaestríaMagíster en Ciencias FarmacéuticasMétodos para la evaluación de actividad biológicaviii, 89 páginasapplication/pdfspaUniversidad Nacional de ColombiaBogotá - Ciencias - Maestría en Ciencias FarmacéuticasFacultad de CienciasBogotá, ColombiaUniversidad Nacional de Colombia - Sede Bogotá610 - Medicina y salud::615 - Farmacología y terapéuticaCatepsina GMetaloproteinasas de la MatrizÁcidos FíbricosEnvejecimiento de la PielCathepsin GMatrix MetalloproteinasesFibric AcidsSkin AgingElastinaElastasasIntegridad de fibraPotencia elastolíticaElastinElastasesFibre integrityElastolytic powerContribución al estudio de la función de las elastasas en la degradación de elastina aislada de piel humanaContribution to understanding the role of elastases in the degradation of elastin derived from human skinTrabajo de grado - Maestríainfo:eu-repo/semantics/masterThesisinfo:eu-repo/semantics/acceptedVersionTexthttp://purl.org/redcol/resource_type/TMBiremeShapiro S, Endicott S, Province M, Pierce J, Campbell E. 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DOI:10.1074/jbc.M113.510008.Determinación de nuevas dianas para la prevención y tratamiento cosmético del envejecimiento cutáneoUniversidad Nacional de ColombiaEstudiantesInvestigadoresMaestrosPúblico generalLICENSElicense.txtlicense.txttext/plain; charset=utf-85879https://repositorio.unal.edu.co/bitstream/unal/86475/1/license.txteb34b1cf90b7e1103fc9dfd26be24b4aMD51ORIGINAL1052379344.2024.pdf1052379344.2024.pdfTesis de Maestría en Ciencias Farmacéuticasapplication/pdf2448206https://repositorio.unal.edu.co/bitstream/unal/86475/2/1052379344.2024.pdf2715ba905a1f5c212c2ff528c36b5814MD52unal/86475oai:repositorio.unal.edu.co:unal/864752024-07-16 14:44:44.236Repositorio Institucional Universidad Nacional de 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Contribución al estudio de la función de las elastasas en la degradación de elastina aislada de piel humana

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