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A novel proteotoxic stress associated mechanism for macular corneal dystrophy

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dc.contributor.authorKaarniranta, Kai
dc.contributor.authorSzalai, Eszter
dc.contributor.authorSmedowski, Adrian
dc.contributor.authorHegy, Zoltán
dc.contributor.authorKivinen, Niko
dc.contributor.authorViiri, Johanna
dc.contributor.authorWowra, Bogumil
dc.contributor.authorDobrowolski, Dariusz
dc.contributor.authorMódis Jr, László
dc.contributor.authorBerta, András
dc.contributor.authorWylegala, Edgar
dc.contributor.authorFelszeghy, Szabolcs
dc.date.accessioned2020-09-21T16:52:13Z
dc.date.available2020-09-21T16:52:13Z
dc.date.issued2015
dc.description.abstractMacular corneal dystrophy is a rare autosomal recessive eye disease affecting primarily the corneal stroma. Abnormal accumulation of proteoglycan aggregates has been observed intra- and extracellularly in the stromal layer. In addition to the stromal keratocytes and corneal lamellae, deposits are also present in the basal epithelial cells, endothelial cells and Descemet's membrane. Misfolding of proteins has a tendency to gather into aggregating deposits. We studied interaction of molecular chaperones and proteasomal clearance in macular dystrophy human samples and in human corneal HCE-2 epithelial cells. Seven cases of macular corneal dystrophy and four normal corneal buttons collected during corneal transplantation were examined for their expression patterns of heat shock protein 70, ubiquitin protein conjugates and SQSTM1/p62. In response to proteasome inhibition the same proteins were analyzed by western blotting. Slitlamp examination, in vivo confocal cornea microscopy and transmission electron microscopy were used for morphological analyses. Heat shock protein 70, ubiquitin protein conjugates and SQSTM1/p62 were upregulated in both the basal corneal epithelial cells and the stromal keratocytes in macular corneal dystrophy samples that coincided with an increased expression of the same molecules under proteasome inhibition in the HCE-2 cells in vitro. We propose a novel regulatory mechanism that connects the molecular chaperone and proteasomal clearance system in the pathogenesis of macular corneal dystrophy.es
dc.formatapplication/pdfes
dc.format.extent10es
dc.identifier.citationHistology and histopathology, Vol. 30, nº 8 (2015)
dc.identifier.doihttps://doi.org/10.14670/HH-11-588
dc.identifier.issn1699-5848
dc.identifier.urihttp://hdl.handle.net/10201/96265
dc.languageenges
dc.publisherF. Hernández y Juan F. Madrid. Universidad de Murcia: Departamento de Biología Celular e Histologíaes
dc.relationSin financiación externa a la Universidades
dc.rightsinfo:eu-repo/semantics/openAccesses
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectHeat shock proteinses
dc.subjectMacular corneal dystrophyes
dc.subjectMisfoldinges
dc.subjectProtein aggregationes
dc.subjectUbiquitin/ proteasome pathwayes
dc.subject.otherCDU::5 - Ciencias puras y naturales::57 - Biología::576 - Biología celular y subcelular. Citologíaes
dc.titleA novel proteotoxic stress associated mechanism for macular corneal dystrophyes
dc.typeinfo:eu-repo/semantics/articlees
dspace.entity.typePublicationes
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Histology and histopathology Vol.30, nº8 (2015)