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dc.contributor.authorPountney, DL
dc.contributor.authorDickson, TC
dc.contributor.authorPower, JHT
dc.contributor.authorVickers, JC
dc.contributor.authorWest, AJ
dc.contributor.authorGai, WP
dc.contributor.editorRichard M. Kostrzewa
dc.date.accessioned2017-05-03T15:03:38Z
dc.date.available2017-05-03T15:03:38Z
dc.date.issued2011
dc.date.modified2012-08-07T23:23:19Z
dc.identifier.issn1029-8428
dc.identifier.doi10.1007/s12640-009-9146-6
dc.identifier.urihttp://hdl.handle.net/10072/30344
dc.description.abstractMultiple system atrophy (MSA) is an adult onset neurodegenerative disease characterised by Parkinsonian and autonomic symptoms and by widespread intracytoplasmic inclusion bodies in oligodendrocytes. These glial cytoplasmic inclusions (GCIs) are comprised of 9-10 nm filaments rich in the protein alpha-synuclein, also found in neuronal inclusion bodies associated with Parkinson's disease. Metallothioneins (MTs) are a class of low-molecular weight (6-7 kDa), cysteine-rich metalbinding proteins the expression of which is induced by heavy metals, glucocorticoids, cytokines and oxidative stress. Recent studies have shown a role for the ubiquitously expressed MT-I/II isoforms in the brain following a variety of stresses, whereas, the function of the brain-specific MT isoform, MT-III, is less clear. MT-III and MT-I/II immunostaining of post-mortem tissue in MSA and normal control human brains showed that the number of MT-IIIpositive cells is significantly increased in MSA in visual cortex, whereas MT-I/II isoforms showed no significant difference in the distribution of immunopositive cells in MSA compared to normal tissue. GCIs were immunopositive for MT-III, but were immunonegative for the MT-I/II isoforms. Immunofluorescence double labelling showed the co-localisation of alpha-synuclein and MT-III in GCIs in MSA tissue. In isolated GCIs, transmission electron microscopy demonstrated MT-III immunogold labelling of the amorphous material surrounding alpha-synuclein filaments in GCIs. High-molecular weight MT-III species in addition to MT-III monomer were detected in GCIs by Western analysis of the detergent-solubilised proteins of purified GCIs. These results show that MT-III, but not MTI/ II, is a specific component of GCIs, present in abnormal aggregated forms external to the alpha-synuclein filaments.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherSpringer
dc.publisher.placeUnited States
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefrom115
dc.relation.ispartofpageto122
dc.relation.ispartofjournalNeurotoxicity Research
dc.relation.ispartofvolume19
dc.rights.retentionY
dc.subject.fieldofresearchBiochemistry and cell biology
dc.subject.fieldofresearchClinical sciences
dc.subject.fieldofresearchNeurosciences
dc.subject.fieldofresearchNeurology and neuromuscular diseases
dc.subject.fieldofresearchcode3101
dc.subject.fieldofresearchcode3202
dc.subject.fieldofresearchcode3209
dc.subject.fieldofresearchcode320905
dc.titleAssociation of Metallothionein-III with Oligodendroglial Cytoplasmic Inclusions in Multiple System Atrophy
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.facultyGriffith Health, School of Medical Science
gro.date.issued2011
gro.hasfulltextNo Full Text
gro.griffith.authorPountney, Dean L.


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