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Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy.
It is found that wild-type alpha-synuclein was selectively translocated into lysosomes for degradation by the chaperone-mediated autophagy pathway, which may underlie the toxic gain-of-function by the pathogenic A53T and A30P mutants.
Impaired Degradation of Mutant α-Synuclein by Chaperone-Mediated Autophagy
It is found that wild-type α-synuclein was selectively translocated into lysosomes for degradation by the chaperone-mediated autophagy pathway, which may underlie the toxic gain-of-function by the A53T and A30P mutants.
Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)
There continues to be confusion regarding acceptable methods to measure autophagy, especially in multicellular eukaryotes, so it is important to update guidelines for monitoring autophagic activity in different organisms.
Wild Type α-Synuclein Is Degraded by Chaperone-mediated Autophagy and Macroautophagy in Neuronal Cells*
- Tereza Vogiatzi, M. Xilouri, K. Vekrellis, L. Stefanis
- BiologyJournal of Biological Chemistry
- 29 August 2008
It is shown that CMA and macroautophagy are important pathways for WT ASYN degradation in neurons and underline the importance of CMA as degradation machinery in the nervous system.
Cell-Produced α-Synuclein Is Secreted in a Calcium-Dependent Manner by Exosomes and Impacts Neuronal Survival
- Evangelia Emmanouilidou, Katerina Melachroinou, K. Vekrellis
- BiologyThe Journal of Neuroscience
- 19 May 2010
The results show for the first time that cell-produced α- Synuclein is secreted via an exosomal, calcium-dependent mechanism and suggest that α-synuclein secretion serves to amplify and propagate Parkinson's disease-related pathology.
Apoptosis in neurodegenerative disorders.
There is supportive, but not definitive, evidence for apoptosis in a number of neurodegenerative disorders, and tissue culture models, animal models and human pathological studies are discussed.
α-Synuclein in Parkinson's disease.
- L. Stefanis
- Biology, ChemistryCold Spring Harbor perspectives in medicine
- 1 February 2012
Targeting the toxic functions conferred by α-synuclein when it is dysregulated may lead to novel therapeutic strategies not only in PD, but also in other neurodegenerative conditions, termed synucleinopathies.
Expression of A53T Mutant But Not Wild-Type α-Synuclein in PC12 Cells Induces Alterations of the Ubiquitin-Dependent Degradation System, Loss of Dopamine Release, and Autophagic Cell Death
- L. Stefanis, K. E. Larsen, H. Rideout, D. Sulzer, L. Greene
- BiologyThe Journal of Neuroscience
- 15 December 2001
These cells may serve as a model to study the effects of aberrant α-synuclein on dopaminergic cell function and survival and raise the possibility that the primary abnormality in these cells may involve one or more deficits in the lysosomal and/or proteasomal degradation pathways, which in turn lead to loss of dopamine capacity and, ultimately, to death.
Abberant α-Synuclein Confers Toxicity to Neurons in Part through Inhibition of Chaperone-Mediated Autophagy
CMA dysfunction mediates aberrant ASYN toxicity, and may be a target for therapeutic intervention in PD and related disorders.
Caspase-Dependent and -Independent Death of Camptothecin-Treated Embryonic Cortical Neurons
- L. Stefanis, D. S. Park, W. Friedman, L. Greene
- Biology, ChemistryThe Journal of Neuroscience
- 1 August 1999
The findings shed light on the mechanisms by which DNA damage kills neurons and raise questions regarding the general utility of caspase inhibitors as neurotherapeutic agents.