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dc.contributor.authorWong, MB
dc.contributor.authorNoe, N
dc.contributor.authorRichter-Landsberg, C
dc.contributor.authorPountney, DL
dc.date.accessioned2017-05-03T15:03:40Z
dc.date.available2017-05-03T15:03:40Z
dc.date.issued2010
dc.date.modified2011-09-22T06:49:26Z
dc.identifier.issn0022-3042
dc.identifier.doi10.1111/j.1471-4159.2010.06943.x
dc.identifier.urihttp://hdl.handle.net/10072/40899
dc.description.abstractMany neurodegenerative diseases are characterised by microscopically- visible protein aggregates, or inclusion bodies, within neural cells. The ubiquitin homologue, SUMO-1, has been identified in sub-domains of pathological inclusion bodies in several neurodegenerative diseases. Inclusion bodies are believed to be formed actively in a defensive response to soluble cytotoxic protein aggregates. We hypothesised that SUMO-1 may become associated with lysosomes in this response. Protein aggregation was induced in 1321N1 glioma cells by proteasome inhibition with MG132 or transient transfection with Q74-EGFP. Fluorescence immunohistochemistry identified co-localisation of SUMO-1 and the lysosomal marker, cathepsin D, in both the transfected cells and MG132 treated cells, increasing over time at 24-96 h post-transfection/ treatment. SUMO-1-positive lysosomes were also detected following MG132-treatment of 1321N1 cells expressing SUMO-1-GFP and stained with Lysotracker dye. SUMO-1 did not mark lysosomes in untransfected or sham treated cells. To determine if SUMO-1 also marks lysosomes in disease, we examined 5 cases of progressive supranuclear palsy (PSP) and 5 cases of MSA. Punctate co-localisation of cathepsin D and SUMO-1 was consistently associated with both the tau-positive PSP inclusions and the a-synuclein-positive MSA inclusions. A similar pattern was also found with the OLN-t40 oligodendrocyte model. These findings suggest a role for SUMO-1 in the autophagy-lysosome pathway linked to the response to protein aggregates.
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherWiley
dc.publisher.placeUnited Kingdom
dc.relation.ispartofstudentpublicationY
dc.relation.ispartofconferencename10th Biennial Meeting of the Asia-Pacific Society of Neurochemistry
dc.relation.ispartofconferencetitleJOURNAL OF NEUROCHEMISTRY
dc.relation.ispartofdatefrom2010-10-18
dc.relation.ispartofdateto2010-10-18
dc.relation.ispartoflocationThailand
dc.relation.ispartofpagefrom44
dc.relation.ispartofpageto44
dc.relation.ispartofvolume115
dc.rights.retentionY
dc.subject.fieldofresearchBiochemistry and cell biology
dc.subject.fieldofresearchCell neurochemistry
dc.subject.fieldofresearchNeurosciences
dc.subject.fieldofresearchcode3101
dc.subject.fieldofresearchcode310104
dc.subject.fieldofresearchcode3209
dc.titleSUMO-1 Marks Lysosomes in Neurodegenerative Diseases and in the Cellular Response to Aggregated Proteins
dc.typeConference output
dc.type.descriptionE3 - Conferences (Extract Paper)
dc.type.codeE - Conference Publications
gro.date.issued2010
gro.hasfulltextNo Full Text
gro.griffith.authorPountney, Dean L.


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    Contains papers delivered by Griffith authors at national and international conferences.

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