dc.contributor.author |
Dieriks, Birger |
en |
dc.contributor.author |
Park, In |
en |
dc.contributor.author |
Fourie, Chantelle |
en |
dc.contributor.author |
Faull, Richard |
en |
dc.contributor.author |
Dragunow, Michael |
en |
dc.contributor.author |
Curtis, Maurice |
en |
dc.date.accessioned |
2018-10-19T01:08:40Z |
en |
dc.date.issued |
2017-02-23 |
en |
dc.identifier.citation |
Scientific Reports 7 Article number 42984 23 Feb 2017 |
en |
dc.identifier.issn |
2045-2322 |
en |
dc.identifier.uri |
http://hdl.handle.net/2292/42928 |
en |
dc.description.abstract |
Parkinson's disease (PD) is characterized by the presence of inclusions known as Lewy bodies, which mainly consist of α-synuclein (α-syn) aggregates. There is growing evidence that α-syn self-propagates in non-neuronal cells, thereby contributing to the progression and spread of PD pathology in the brain. Tunneling nanotubes (TNTs) are long, thin, F-actin-based membranous channels that connect cells and have been proposed to act as conduits for α-syn transfer between cells. SH-SY5Y cells and primary human brain pericytes, derived from postmortem PD brains, frequently form TNTs that allow α-syn transfer and long-distance electrical coupling between cells. Pericytes in situ contain α-syn precipitates like those seen in neurons. Exchange through TNTs was rapid, but dependent on the size of the protein. Proteins were able to spread throughout a network of cells connected by TNTs. Transfer through TNTs was not restricted to α-syn; fluorescent control proteins and labeled membrane were also exchanged through TNTs. Most importantly the formation of TNTs and transfer continued during mitosis. Together, our results provide a detailed description of TNTs in SH-SY5Y cells and human brain PD pericytes, demonstrating their role in α-syn transfer and further emphasize the importance that non-neuronal cells, such as pericytes play in disease progression. |
en |
dc.format.medium |
Electronic |
en |
dc.language |
eng |
en |
dc.relation.ispartofseries |
Scientific reports |
en |
dc.rights |
Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. |
en |
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
en |
dc.rights.uri |
https://creativecommons.org/licenses/by/4.0/ |
en |
dc.subject |
Pericytes |
en |
dc.subject |
Brain |
en |
dc.subject |
Neurons |
en |
dc.subject |
Lewy Bodies |
en |
dc.subject |
Cells, Cultured |
en |
dc.subject |
Cell Membrane |
en |
dc.subject |
Humans |
en |
dc.subject |
Parkinson Disease |
en |
dc.subject |
Microscopy, Confocal |
en |
dc.subject |
Microscopy, Electron, Scanning |
en |
dc.subject |
Coculture Techniques |
en |
dc.subject |
Mitosis |
en |
dc.subject |
Protein Transport |
en |
dc.subject |
Nanotubes |
en |
dc.subject |
alpha-Synuclein |
en |
dc.subject |
Time-Lapse Imaging |
en |
dc.title |
α-synuclein transfer through tunneling nanotubes occurs in SH-SY5Y cells and primary brain pericytes from Parkinson's disease patients. |
en |
dc.type |
Journal Article |
en |
dc.identifier.doi |
10.1038/srep42984 |
en |
pubs.begin-page |
42984 |
en |
pubs.volume |
7 |
en |
dc.rights.holder |
Copyright: The authors |
en |
dc.identifier.pmid |
28230073 |
en |
pubs.publication-status |
Published |
en |
dc.rights.accessrights |
http://purl.org/eprint/accessRights/OpenAccess |
en |
pubs.subtype |
Research Support, Non-U.S. Gov't |
en |
pubs.subtype |
research-article |
en |
pubs.subtype |
Journal Article |
en |
pubs.elements-id |
615668 |
en |
pubs.org-id |
Medical and Health Sciences |
en |
pubs.org-id |
Medical Sciences |
en |
pubs.org-id |
Anatomy and Medical Imaging |
en |
pubs.org-id |
Pharmacology |
en |
dc.identifier.eissn |
2045-2322 |
en |
pubs.record-created-at-source-date |
2017-02-24 |
en |
pubs.dimensions-id |
28230073 |
en |