Explore the words cloud of the NEUROTUNN project. It provides you a very rough idea of what is the project "NEUROTUNN" about.
The following table provides information about the project.
|Coordinator Country||France [FR]|
|Total cost||185˙076 €|
|EC max contribution||185˙076 € (100%)|
1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
|Duration (year-month-day)||from 2016-03-01 to 2018-02-28|
Take a look of project's partnership.
|1||INSTITUT PASTEUR||FR (PARIS CEDEX 15)||coordinator||185˙076.00|
A common feature of neurodegenerative diseases, including highly prevalent illnesses, is the presence of misfolded protein aggregates in affected regions of the nervous system. Aggregates result from the misfolding of one or more specific proteins, for example, amyloid-β in Alzheimer’s disease, α-synuclein in Parkinson’s disease, and the normal prion protein in transmissible spongiform encephalopathies (TSEs). Recently a series of exciting studies has suggested a prion-like mechanism underlying the pathological spreading of misfolded proteins (mainly tau, α-synuclein and huntingtin) involved in various neurodegenerative diseases. Particularly striking is the recovery of α-synuclein aggregates from engrafted embryonic neurons in post-mortem brains transplanted from Parkinson’s patients. Thus, while questioning the therapeutic use of transplants, the understanding of the molecular and cellular fundaments of cell-to-cell transmission of proteinaceous aggregates is clearly in the early stages of investigation and may represent a more readily accessible target for novel disease-modifying therapies, allowing the development of possible common therapeutic strategies. Tunneling nanotubes (TNTs) represent a novel mechanism of direct intercellular communication that has been shown to mediate both transfer of prions between neuronal cells and the passage of poliQ huntingtin between neurons. We hypothesize that TNT-mediated transfer of amyloidogenic protein aggregates represents one of the main pathways of communication between cells. Thus, molecules involved in TNT formation could represent valuable targets for the disease prevention. Here I will assess the underlying mechanism of cell-to cell transfer of α-synuclein, exploring whether its transport could be mediated by TNTs in physiologically relevant in vitro models, evaluating as well the possible contribution of non-cell autonomous processes, via neuron-glial interactions, to the pathological spreading of the protein.
|year||authors and title||journal||last update|
Frida Loria, Jessica Y. Vargas, Luc Bousset, Sylvie Syan, Audrey Salles, Ronald Melki, Chiara Zurzolo
Î±-Synuclein transfer between neurons and astrocytes indicates that astrocytes play a role in degradation rather than in spreading
published pages: 789-808, ISSN: 0001-6322, DOI: 10.1007/s00401-017-1746-2
|Acta Neuropathologica 134/5||2019-06-13|
SaÃ¯da Abounit, Luc Bousset, Frida Loria, Seng Zhu, Fabrice de Chaumont, Laura Pieri, Jeanâ€Christophe Olivoâ€Marin, Ronald Melki, Chiara Zurzolo
Tunneling nanotubes spread fibrillar Î±â€synuclein by intercellular trafficking of lysosomes
published pages: 2120-2138, ISSN: 0261-4189, DOI: 10.15252/embj.201593411
|The EMBO Journal 35/19||2019-06-13|
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