Age-dependent cognitive decline and amygdala pathology in α-synuclein transgenic mice

Freichel, Christian; Neumann, Manuela; Ballard, Theresa M.; Müller, Veronika; Woolley, Marie L.; Ozmen, Laurence; Borroni, Edilio; Kretzschmar, Hans A.; Haass, Christian; Spooren, Will; Kahle, Philipp J.

doi:10.1016/j.neurobiolaging.2006.06.013

Cited by 162 publications

(160 citation statements)

References 53 publications

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“…The effects of phosphorylation on ␣Syn-induced toxicity are complex with reports supporting negative as well as positive impacts on cells (23,24,(51)(52)(53)(54). Therefore, we next investigated the interplay between ␣Syn sumoylation and phosphorylation by examining how changes in sumoylation affect ␣Syn phosphorylation and whether this impacted ␣Syn toxicity.…”

Section: Protective Function Of Sumo Requires Direct Modification Ofmentioning

confidence: 99%

Interplay between Sumoylation and Phosphorylation for Protection against α-Synuclein Inclusions

Shahpasandzadeh

Popova

Kleinknecht

et al. 2014

Journal of Biological Chemistry

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Background: Phosphorylation and sumoylation are post-translational modifications of the Parkinson disease protein ␣-synuclein. Results: ␣-Synuclein inclusion clearance is impaired in yeast when sumoylation is inhibited; phosphorylation of ␣-synuclein can compensate SUMO impairment. Conclusion: Sumoylation stimulates autophagy clearance of ␣-synuclein inclusions, whereas phosphorylation promotes autophagy and proteasome degradation. Significance: A complex molecular post-translational cross-talk is required in yeast to clear toxic inclusions.

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Section: Protective Function Of Sumo Requires Direct Modification Ofmentioning

confidence: 99%

Interplay between Sumoylation and Phosphorylation for Protection against α-Synuclein Inclusions

Shahpasandzadeh

Popova

Kleinknecht

et al. 2014

Journal of Biological Chemistry

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“…The Thy-1-human (A30P)αSyn transgenic mouse model has been previously described [22], by introducing the neuron specific Thy1 promoter for overexpression of human mutant αSyn(A30P). Mice were sacrificed by cervical dislocation, and brains harvested and divided into forebrain left (FB/L)/ Intens.…”

Section: Preparation Of Mouse Brain Homogenatementioning

confidence: 99%

“…The Aß-epitopes recognized by the antibodies were identified in previous studies by proteolytic excision-mass spectrometry [17,25] (Table 1). The mass spectrometric analysis of the epitope specificity revealed that the aggregation-inhibiting antibody (4G8) binds to a central-to C-terminal epitope, Aß (17)(18)(19)(20)(21)(22)(23)(24) [19,25]. In contrast, an N-terminal epitope, Aß(4-10) is recognized by a plaque-disaggregating antibody (6E10) [17].…”

Section: Characterization Of Interactions Of Aß-polypeptides and Antimentioning

confidence: 99%

Identification and Affinity-Quantification of ß-Amyloid and α-Synuclein Polypeptides Using On-Line SAW-Biosensor-Mass Spectrometry

Slamnoiu

Vlad

Stumbaum

et al. 2014

J. Am. Soc. Mass Spectrom.

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Abstract. Bioaffinity analysis using a variety of biosensors has become an established tool for detection and quantification of biomolecular interactions.Biosensors, however, are generally limited by the lack of chemical structure information of affinity-bound ligands. On-line bioaffinity-mass spectrometry using a surface-acoustic wave biosensor (SAW-MS) is a new combination providing the simultaneous affinity detection, quantification, and mass spectrometric structural ({"' characterization of ligands. We describe here an on-line SAW-MS combination for direct identification and affinity determination, using a new interface for MS of the affinity-isolated ligand eluate. Key element of the SAW-MS combination is a microfluidic interface that integrates affinity-isolation on a gold chip, in-situ sample concentration, and desalting with a microcolumn forMS of the ligand eluate from the biosensor. Suitable MSacquisition software has been developed that provides coupling of the SAW-MS interface to a Bruker Daltonics ion trap-MS, FTICR-MS, and Waters Synapt-QTOF-MS systems. Applications are presented for mass spectrometric identifications and affinity (K 0 ) determinations of the neurodegenerative polypeptides, r..-amyloid (AI1), and pathophysiological and physiological synucleins (a-and r..-synucleins), two key polypeptide systems for Alzheimer's disease and Parkinson's disease, respectively. Moreover, first in vivo applications of aSyn polypeptides from brain homogenate show the feasibility of on-line affinity-MS to the direct analysis of biological material. These results demonstrate on-line SAW-bioaffinity-MS as a powerful tool for structural and quantitative analysis of biopolymer interactions.

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“…Freichel et al [76] used a transgenic mouse model to assess the behavioral and structural implications of mutant α-synuclein (αSYN) expression, a neuronal protein. αSYN inclusions constitute the hallmark lesions of a number of neurodegenerative diseases, including PD and dementia with Lewy bodies.…”

Section: Neurodegenerative Diseasesmentioning

confidence: 99%

Amygdalar Models of Neurological and Neuropsychiatric Disorders

Gilbert¹

2012

The Amygdala - A Discrete Multitasking Manager

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Age-dependent cognitive decline and amygdala pathology in α-synuclein transgenic mice

Cited by 162 publications

References 53 publications

Interplay between Sumoylation and Phosphorylation for Protection against α-Synuclein Inclusions

Interplay between Sumoylation and Phosphorylation for Protection against α-Synuclein Inclusions

Identification and Affinity-Quantification of ß-Amyloid and α-Synuclein Polypeptides Using On-Line SAW-Biosensor-Mass Spectrometry

Amygdalar Models of Neurological and Neuropsychiatric Disorders

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