We are analyzing https://link.springer.com/article/10.1186/2047-9158-1-2.

Title:
Macroautophagy in sporadic and the genetic form of Parkinson's disease with the A53T α-synuclein mutation | Translational Neurodegeneration
Description:
Background The A53T mutation in the α-synuclein gene causes autosomal-dominant Lewy body Parkinson
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28 years and 1 months (reg. 1997-05-29).

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Keywords {🔍}

αsynuclein, pubmed, article, macroautophagy, cells, google, scholar, cas, disease, mutant, autophagy, figure, alphasynuclein, sporadic, parkinsons, transfected, lewy, brain, patients, cases, markers, mutation, cell, compared, data, gene, atg, shsyy, neurons, usa, central, bodies, mutations, observed, controls, protein, aggregates, increased, cortical, kda, research, antihuman, diluted, authors, immunohistochemistry, human, table, increase, biol, access,

Topics {✒️}

mouse anti-human α-synuclein wt α-synuclein-gfp plasmid a53t α-synuclein-gfp plasmids wt α-synuclein-gfp plasmids α-synuclein-immunoreactive lewy neurites gfp-tagged α-synuclein detected larger α-synuclein-immunopositive aggregates α-synuclein-immunopositive lewy body rabbit anti-human atg8/lc3 expressing gfp-tagged wildtype open access article atg8/lc3-immunopositive cortical neurons α-synuclein-immunoreactive aggregates α-synuclein-immunopositive aggregates anti-rabbit igg conjugated transfected sh-sy5y cells sh-sy5y cells transfected rabbit anti-human atg8 rabbit anti-human atg6 gfp-tagged a53t mutant article download pdf mutated α-synuclein protein ubiquitin-dependent degradation system control sh-sy5y cells large α-synuclein aggregates cortical α-synuclein accumulation gene encoding alpha-synuclein alpha-synuclein gene identified alpha-synuclein gene duplication a53t mutant α-synuclein phosphatidyl ethanolamine-modified form rabbit anti-human atg5 alpha-synuclein impairs macroautophagy cytoplasmic α-synuclein pathologies insoluble intracellular α-synuclein α-synuclein aggregate disposal mutant a53t {alpha}-synuclein intracellular α-synuclein aggregation alpha-synuclein locus triplication a53t α-synuclein mutation α-synuclein transfected cells increased α-synuclein accumulation α-synuclein positive neurites α-synuclein-immunopositive dots ala53thr alpha-synuclein mutation wild type α-synuclein gfp-fused major band wt α-synuclein transfection wild-type alpha-synuclein wild type alpha-synuclein

Schema {🗺️}

WebPage:
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         headline:Macroautophagy in sporadic and the genetic form of Parkinson's disease with the A53T α-synuclein mutation
         description:The A53T mutation in the α-synuclein gene causes autosomal-dominant Lewy body Parkinson's disease (PD). Cultured cell models have linked this mutation to increased cell macroautophagy, although evidence of enhanced macroautophagy in patients with this mutation has not been assessed. To determine whether macroautophagy is increased by the A53T α-synuclein gene mutation in PD patients and cell models. Formalin-fixed paraffin-embedded 10 μm-thick tissue sections from the substantia nigra and anterior cingulate cortex of two PD patients with the A53T α-synuclein gene mutation were compared with four sporadic PD cases and four controls obtained from the Sydney Brain Bank. Lewy bodies were isolated from frontal cortex of a case with late stage PD (recruited from South Australian Brain Bank). Immunohistochemistry was performed for α-synuclein and the macroautophagy markers autophagy-specific gene (ATG) 5, ATG6/Beclin1 and ATG8/LC3. SH-SY5Y cells were transfected with wild type or A53T mutant α-synuclein plasmids and observable changes in macroautophagy marker protein levels assessed using Western blotting. α-Synuclein immunoreactive neurites and dots were more numerous in patients with A53T mutations compared with late stage sporadic PD patients, and perinuclear cytoplasmic α-synuclein aggregates were observed in the α-synuclein A53T gene transfected SH-SY5Y cells compared to wild type transfections. All PD patients (with or without A53T mutations) had increased immunohistochemical evidence for macroautophagy compared with controls, and the levels of the ATG5 complex were equally increased in wild type and A53T α-synuclein gene transfected cells compared to controls. Despite increased α-synuclein accumulation with A53T mutations, macroautophagy is not increased above that observed in sporadic patients with PD or in cells transfected with wild type α-synuclein, suggesting that mutated α-synuclein protein is not removed by macroautophagy.
         datePublished:2012-01-13T00:00:00Z
         dateModified:2012-01-13T00:00:00Z
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      headline:Macroautophagy in sporadic and the genetic form of Parkinson's disease with the A53T α-synuclein mutation
      description:The A53T mutation in the α-synuclein gene causes autosomal-dominant Lewy body Parkinson's disease (PD). Cultured cell models have linked this mutation to increased cell macroautophagy, although evidence of enhanced macroautophagy in patients with this mutation has not been assessed. To determine whether macroautophagy is increased by the A53T α-synuclein gene mutation in PD patients and cell models. Formalin-fixed paraffin-embedded 10 μm-thick tissue sections from the substantia nigra and anterior cingulate cortex of two PD patients with the A53T α-synuclein gene mutation were compared with four sporadic PD cases and four controls obtained from the Sydney Brain Bank. Lewy bodies were isolated from frontal cortex of a case with late stage PD (recruited from South Australian Brain Bank). Immunohistochemistry was performed for α-synuclein and the macroautophagy markers autophagy-specific gene (ATG) 5, ATG6/Beclin1 and ATG8/LC3. SH-SY5Y cells were transfected with wild type or A53T mutant α-synuclein plasmids and observable changes in macroautophagy marker protein levels assessed using Western blotting. α-Synuclein immunoreactive neurites and dots were more numerous in patients with A53T mutations compared with late stage sporadic PD patients, and perinuclear cytoplasmic α-synuclein aggregates were observed in the α-synuclein A53T gene transfected SH-SY5Y cells compared to wild type transfections. All PD patients (with or without A53T mutations) had increased immunohistochemical evidence for macroautophagy compared with controls, and the levels of the ATG5 complex were equally increased in wild type and A53T α-synuclein gene transfected cells compared to controls. Despite increased α-synuclein accumulation with A53T mutations, macroautophagy is not increased above that observed in sporadic patients with PD or in cells transfected with wild type α-synuclein, suggesting that mutated α-synuclein protein is not removed by macroautophagy.
      datePublished:2012-01-13T00:00:00Z
      dateModified:2012-01-13T00:00:00Z
      pageStart:1
      pageEnd:7
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      keywords:
         α-synuclein
         macroautophagy
         Parkinson's disease
         Neurosciences
         Neurology
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      affiliation:
            name:University of New South Wales
            address:
               name:Neuroscience Research Australia, University of New South Wales, Sydney, Australia
               type:PostalAddress
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      name:Karen Murphy
      affiliation:
            name:University of New South Wales
            address:
               name:Neuroscience Research Australia, University of New South Wales, Sydney, Australia
               type:PostalAddress
            type:Organization
      name:Weiping Gai
      affiliation:
            name:Flinders University School of Medicine
            address:
               name:Department of Human Physiology and the Centre for Neuroscience, Flinders University School of Medicine, Bedford Park, Australia
               type:PostalAddress
            type:Organization
      name:Glenda M Halliday
      affiliation:
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      name:Neuroscience Research Australia, University of New South Wales, Sydney, Australia
      name:Neuroscience Research Australia, University of New South Wales, Sydney, Australia
      name:Department of Human Physiology and the Centre for Neuroscience, Flinders University School of Medicine, Bedford Park, Australia
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