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Antibodies against ...
Antibodies against alpha-synuclein reduce oligomerization in living cells
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- Näsström, Thomas (författare)
- Uppsala universitet,Geriatrik,Lannfelt, Molekylär geriatrik/ Rudbecklaboratoriet
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- Goncalves, Susana (författare)
- Cell and Molecular Neuroscience Unit, Instituto de Medicina Molecular, Lisboa
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- Sahlin, Charlotte (författare)
- Uppsala universitet,Geriatrik
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- Nordström, Eva (författare)
- BioArctic Neuroscience AB
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- Screpanti Sundquist, Valentina (författare)
- BioArctic Neuroscience AB
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- Lannfelt, Lars (författare)
- Uppsala universitet,Geriatrik,Lannfelt, Molekylär geriatrik/ Rudbecklaboratoriet
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- Bergström, Joakim (författare)
- Uppsala universitet,Geriatrik,Lannfelt, Molekylär geriatrik/ Rudbecklaboratoriet
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- Outeiro, Tiago. F (författare)
- Cell and Molecular Neuroscience Unit, Instituto de Medicina Molecular, Lisboa. Instituto de Fisiologia, Faculdade de Medicina da Universidade de Lisboa, Lisboa. Department of NeuroDegeneration and Restaurative Research, Universitätsmedizin Göttingen, Göttingen
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- Ingelsson, Martin (författare)
- Uppsala universitet,Geriatrik,Lannfelt, Molekylär geriatrik/ Rudbecklaboratoriet
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(creator_code:org_t)
- 2011-10-31
- 2011
- Engelska.
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Ingår i: PLOS ONE. - : Public Library of Science (PLoS). - 1932-6203. ; 6:10, s. e27230-
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Abstract
Ämnesord
Stäng
- Recent research implicates soluble aggregated forms of α-synuclein as neurotoxic species with a central role in the pathogenesis of Parkinson’s disease and related disorders. The pathway by which α-synuclein aggregates is believed to follow a step-wise pattern, in which dimers and smaller oligomers are initially formed. Here, we used H4 neuroglioma cells expressing α-synuclein fused to hemi:GFP to study the effects of α-synuclein monoclonal antibodies on the early stages of aggregation, as quantified by Bimolecular Fluorescence Complementation assay. Widefield and confocal microscopy revealed that cells treated for 48 h with monoclonal antibodies internalized antibodies to various degrees. Oligomer-selective and C-terminal specific α-synuclein antibodies reduced the extent of α-synuclein dimerization/oligomerization, as indicated by decreased GFP fluorescence signal. Furthermore, ELISA measurements on lysates and conditioned media from antibody treated cells displayed lower α-synuclein levels compared to untreated cells, suggesting increased protein turnover. Taken together, our results propose that extracellular administration of monoclonal antibodies can modify or inhibit early steps in the aggregation process of α-synuclein, thus providing further support for passive immunization against diseases with α-synuclein pathology.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Neurovetenskaper (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Neurosciences (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Cell- och molekylärbiologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Cell and Molecular Biology (hsv//eng)
Nyckelord
- Alpha-synuclein; Parkinson’s disease; Lewy bodies; Aggregation; Bimolecular Fluorescence Complementation; Monoclonal antibodies; Immunotherapy
- Neuroscience
- Neurovetenskap
- Geriatrics
- Geriatrik
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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