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Alpha-Synuclein Aggregates Associated with Mitochondria in Tunnelling Nanotubes

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F20%3A00533119" target="_blank" >RIV/86652036:_____/20:00533119 - isvavai.cz</a>

  • Result on the web

    <a href="https://link.springer.com/article/10.1007/s12640-020-00285-y" target="_blank" >https://link.springer.com/article/10.1007/s12640-020-00285-y</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1007/s12640-020-00285-y" target="_blank" >10.1007/s12640-020-00285-y</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Alpha-Synuclein Aggregates Associated with Mitochondria in Tunnelling Nanotubes

  • Original language description

    The interaction of alpha-synuclein with mitochondria in both typical and atypical Parkinson's disease is a critical component of degeneration. The mechanism of cell-to-cell propagation of pathological alpha-synuclein in synucleinopathies is unclear. Intercellular exchange of mitochondria along tunnelling nanotubes has been described in other diseases, such as cancer, however, its role in synucleinopathies is unknown. Pathological alpha-synuclein species have been demonstrated previously to move from cell to cell via tunnelling nanotubes. This process was further explored using co-culture and monoculture systems to determine if alpha-synuclein binds to migrating mitochondria within tunnelling nanotubes. Super-resolution analysis via stimulated emission depletion microscopy showed interaction between alpha-synuclein with the mitochondrial outer membrane and the presence of alpha-synuclein associated with mitochondria in tunnelling nanotubes between 1321N1, differentiated THP-1 and SH-SY5Y cell types. siRNA knockdown of Miro1, a critical protein-bridging mitochondria to the motor adaptor complex, had no effect on mitochondrial density or alpha-synuclein association with mitochondria in tunnelling nanotubes. The results show that alpha-synuclein aggregates associate with mitochondria in intercellular tunnelling nanotubes, suggesting that mitochondria-mediated alpha-synuclein transfer between cells may contribute to cell-to-cell spread of alpha-synuclein aggregates and disease propagation.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    30103 - Neurosciences (including psychophysiology)

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2020

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Neurotoxicity Research

  • ISSN

    1029-8428

  • e-ISSN

  • Volume of the periodical

    SEP 2020

  • Issue of the periodical within the volume

    SEP 2020

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    15

  • Pages from-to

  • UT code for WoS article

    000569293100002

  • EID of the result in the Scopus database

    2-s2.0-85091009949