Altered zinc homeostasis in a primary cell culture model of the retinal pigment epithelium

The retinal pigment epithelium (RPE) is progressively degenerated during age-related macular degeneration (AMD), one of the leading causes of irreversible blindness, which clinical hallmark is the buildup of sub-RPE extracellular material. Clinical observations indicate that Zn dyshomeostasis can in...

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Autores: Álvarez-Barrios, Ana, Álvarez, Lydia, Artime, Enol, García, Montserrat, Lengyel, Imre, Pereiro, Rosario, González-Iglesias, Héctor
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2023
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/339030
Acceso en línea:http://hdl.handle.net/10261/339030
Access Level:acceso abierto
Palabra clave:Retinal pigment epithelium
Cell culture
Sub-RPE deposits
AMD in vitro model
Zinc dyshomeostasis
Physical barrier
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spelling Altered zinc homeostasis in a primary cell culture model of the retinal pigment epitheliumÁlvarez-Barrios, AnaÁlvarez, LydiaArtime, EnolGarcía, MontserratLengyel, ImrePereiro, RosarioGonzález-Iglesias, HéctorRetinal pigment epitheliumCell cultureSub-RPE depositsAMD in vitro modelZinc dyshomeostasisPhysical barrierThe retinal pigment epithelium (RPE) is progressively degenerated during age-related macular degeneration (AMD), one of the leading causes of irreversible blindness, which clinical hallmark is the buildup of sub-RPE extracellular material. Clinical observations indicate that Zn dyshomeostasis can initiate detrimental intracellular events in the RPE. In this study, we used a primary human fetal RPE cell culture model producing sub-RPE deposits accumulation that recapitulates features of early AMD to study Zn homeostasis and metalloproteins changes. RPE cell derived samples were collected at 10, 21 and 59 days in culture and processed for RNA sequencing, elemental mass spectrometry and the abundance and cellular localization of specific proteins. RPE cells developed processes normal to RPE, including intercellular unions formation and expression of RPE proteins. Punctate deposition of apolipoprotein E, marker of sub-RPE material accumulation, was observed from 3 weeks with profusion after 2 months in culture. Zn cytoplasmic concentrations significantly decreased 0.2 times at 59 days, from 0.264 ± 0.119 ng·μg at 10 days to 0.062 ± 0.043 ng·μg at 59 days (p < 0.05). Conversely, increased levels of Cu (1.5-fold in cytoplasm, 5.0-fold in cell nuclei and membranes), Na (3.5-fold in cytoplasm, 14.0-fold in cell nuclei and membranes) and K (6.8-fold in cytoplasm) were detected after 59-days long culture. The Zn-regulating proteins metallothioneins showed significant changes in gene expression over time, with a potent down-regulation at RNA and protein level of the most abundant isoform in primary RPE cells, from 0.141 ± 0.016 ng·mL at 10 days to 0.056 ± 0.023 ng·mL at 59 days (0.4-fold change, p < 0.05). Zn influx and efflux transporters were also deregulated, along with an increase in oxidative stress and alterations in the expression of antioxidant enzymes, including superoxide dismutase, catalase and glutathione peroxidase. The RPE cell model producing early accumulation of extracellular deposits provided evidences on an altered Zn homeostasis, exacerbated by changes in cytosolic Zn-binding proteins and Zn transporters, along with variations in other metals and metalloproteins, suggesting a potential role of altered Zn homeostasis during AMD development.The Instituto Oftalmológico Fernández-Vega and Fundación de Investigación Oftalmológica acknowledge financial support from the Fundación Rafael del Pino (http://www.frdelpino.es), through the “Cátedra Rafael del Pino.” This work was partially financed through project (PID2019-107838RB-I00/Agencia Estatal de Investigación (AEI)/10.13039/501100011033). AÁ-B acknowledges the FPU grant (Ref. FPU20/00608, Ministry of Universities of Spain).Frontiers MediaFundación de Investigación Oftalmológica Fernández-VegaFundación Rafael del PinoAgencia Estatal de Investigación (España)Ministerio de Ciencia, Innovación y Universidades (España)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2023202320232023info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://hdl.handle.net/10261/339030reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PID2019-107838RB-I00The underlying dataset has been published as supplementary material of the article in the publisher platform at http://dx.doi.org/10.3389/fnut.2023.1124987http://dx.doi.org/10.3389/fnut.2023.1124987Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3390302026-05-22T06:33:51Z
dc.title.none.fl_str_mv Altered zinc homeostasis in a primary cell culture model of the retinal pigment epithelium
title Altered zinc homeostasis in a primary cell culture model of the retinal pigment epithelium
spellingShingle Altered zinc homeostasis in a primary cell culture model of the retinal pigment epithelium
Álvarez-Barrios, Ana
Retinal pigment epithelium
Cell culture
Sub-RPE deposits
AMD in vitro model
Zinc dyshomeostasis
Physical barrier
title_short Altered zinc homeostasis in a primary cell culture model of the retinal pigment epithelium
title_full Altered zinc homeostasis in a primary cell culture model of the retinal pigment epithelium
title_fullStr Altered zinc homeostasis in a primary cell culture model of the retinal pigment epithelium
title_full_unstemmed Altered zinc homeostasis in a primary cell culture model of the retinal pigment epithelium
title_sort Altered zinc homeostasis in a primary cell culture model of the retinal pigment epithelium
dc.creator.none.fl_str_mv Álvarez-Barrios, Ana
Álvarez, Lydia
Artime, Enol
García, Montserrat
Lengyel, Imre
Pereiro, Rosario
González-Iglesias, Héctor
author Álvarez-Barrios, Ana
author_facet Álvarez-Barrios, Ana
Álvarez, Lydia
Artime, Enol
García, Montserrat
Lengyel, Imre
Pereiro, Rosario
González-Iglesias, Héctor
author_role author
author2 Álvarez, Lydia
Artime, Enol
García, Montserrat
Lengyel, Imre
Pereiro, Rosario
González-Iglesias, Héctor
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Fundación de Investigación Oftalmológica Fernández-Vega
Fundación Rafael del Pino
Agencia Estatal de Investigación (España)
Ministerio de Ciencia, Innovación y Universidades (España)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Retinal pigment epithelium
Cell culture
Sub-RPE deposits
AMD in vitro model
Zinc dyshomeostasis
Physical barrier
topic Retinal pigment epithelium
Cell culture
Sub-RPE deposits
AMD in vitro model
Zinc dyshomeostasis
Physical barrier
description The retinal pigment epithelium (RPE) is progressively degenerated during age-related macular degeneration (AMD), one of the leading causes of irreversible blindness, which clinical hallmark is the buildup of sub-RPE extracellular material. Clinical observations indicate that Zn dyshomeostasis can initiate detrimental intracellular events in the RPE. In this study, we used a primary human fetal RPE cell culture model producing sub-RPE deposits accumulation that recapitulates features of early AMD to study Zn homeostasis and metalloproteins changes. RPE cell derived samples were collected at 10, 21 and 59 days in culture and processed for RNA sequencing, elemental mass spectrometry and the abundance and cellular localization of specific proteins. RPE cells developed processes normal to RPE, including intercellular unions formation and expression of RPE proteins. Punctate deposition of apolipoprotein E, marker of sub-RPE material accumulation, was observed from 3 weeks with profusion after 2 months in culture. Zn cytoplasmic concentrations significantly decreased 0.2 times at 59 days, from 0.264 ± 0.119 ng·μg at 10 days to 0.062 ± 0.043 ng·μg at 59 days (p < 0.05). Conversely, increased levels of Cu (1.5-fold in cytoplasm, 5.0-fold in cell nuclei and membranes), Na (3.5-fold in cytoplasm, 14.0-fold in cell nuclei and membranes) and K (6.8-fold in cytoplasm) were detected after 59-days long culture. The Zn-regulating proteins metallothioneins showed significant changes in gene expression over time, with a potent down-regulation at RNA and protein level of the most abundant isoform in primary RPE cells, from 0.141 ± 0.016 ng·mL at 10 days to 0.056 ± 0.023 ng·mL at 59 days (0.4-fold change, p < 0.05). Zn influx and efflux transporters were also deregulated, along with an increase in oxidative stress and alterations in the expression of antioxidant enzymes, including superoxide dismutase, catalase and glutathione peroxidase. The RPE cell model producing early accumulation of extracellular deposits provided evidences on an altered Zn homeostasis, exacerbated by changes in cytosolic Zn-binding proteins and Zn transporters, along with variations in other metals and metalloproteins, suggesting a potential role of altered Zn homeostasis during AMD development.
publishDate 2023
dc.date.none.fl_str_mv 2023
2023
2023
2023
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/339030
url http://hdl.handle.net/10261/339030
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PID2019-107838RB-I00
The underlying dataset has been published as supplementary material of the article in the publisher platform at http://dx.doi.org/10.3389/fnut.2023.1124987
http://dx.doi.org/10.3389/fnut.2023.1124987

dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Frontiers Media
publisher.none.fl_str_mv Frontiers Media
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
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