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@ARTICLE{Scheiblich:272487,
      author       = {Scheiblich, Hannah and Eikens, Frederik and Wischhof, Lena
                      and Opitz, Sabine and Jüngling, Kay and Cserép, Csaba and
                      Schmidt, Susanne V and Lambertz, Jessica and Bellande, Tracy
                      and Pósfai, Balázs and Geck, Charlotte and Spitzer, Jasper
                      and Odainic, Alexandru and Castro-Gomez, Mario Sergio and
                      Schwartz, Stephanie and Boussaad, Ibrahim and Krüger, Rejko
                      and Glaab, Enrico and Di Monte, Donato A and Bano, Daniele
                      and Dénes, Ádám and Latz, Eicke and Melki, Ronald and
                      Pape, Hans-Christian and Heneka, Michael T},
      title        = {{M}icroglia rescue neurons from aggregate-induced neuronal
                      dysfunction and death through tunneling nanotubes.},
      journal      = {Neuron},
      volume       = {112},
      number       = {18},
      issn         = {0896-6273},
      address      = {New York, NY},
      publisher    = {Elsevier},
      reportid     = {DZNE-2024-01168},
      pages        = {3106 - 3125.e8},
      year         = {2024},
      abstract     = {Microglia are crucial for maintaining brain health and
                      neuron function. Here, we report that microglia establish
                      connections with neurons using tunneling nanotubes (TNTs) in
                      both physiological and pathological conditions. These TNTs
                      facilitate the rapid exchange of organelles, vesicles, and
                      proteins. In neurodegenerative diseases like Parkinson's and
                      Alzheimer's disease, toxic aggregates of alpha-synuclein
                      (α-syn) and tau accumulate within neurons. Our research
                      demonstrates that microglia use TNTs to extract neurons from
                      these aggregates, restoring neuronal health. Additionally,
                      microglia share their healthy mitochondria with burdened
                      neurons, reducing oxidative stress and normalizing gene
                      expression. Disrupting mitochondrial function with antimycin
                      A before TNT formation eliminates this neuroprotection.
                      Moreover, co-culturing neurons with microglia and promoting
                      TNT formation rescues suppressed neuronal activity caused by
                      α-syn or tau aggregates. Notably, TNT-mediated aggregate
                      transfer is compromised in microglia carrying
                      Lrrk22(Gly2019Ser) or Trem2(T66M) and (R47H) mutations,
                      suggesting a role in the pathology of these gene variants in
                      neurodegenerative diseases.},
      keywords     = {Microglia: metabolism / Microglia: drug effects / Animals /
                      Neurons: metabolism / Neurons: drug effects / tau Proteins:
                      metabolism / tau Proteins: genetics / alpha-Synuclein:
                      metabolism / alpha-Synuclein: genetics / Coculture
                      Techniques / Mice / Mitochondria: metabolism / Mitochondria:
                      drug effects / Humans / Leucine-Rich Repeat Serine-Threonine
                      Protein Kinase-2: genetics / Leucine-Rich Repeat
                      Serine-Threonine Protein Kinase-2: metabolism / Cell Death:
                      drug effects / Cell Death: physiology / Nanotubes / Cells,
                      Cultured / Cell Communication: physiology / Cell
                      Communication: drug effects / Oxidative Stress: drug effects
                      / Oxidative Stress: physiology / Cell Membrane Structures /
                      Lrrk2 G2019S (Other) / Trem2 (Other) / alpha-synuclein
                      (Other) / intercellular transfer (Other) / microglia (Other)
                      / mitochondria (Other) / neurons (Other) / oxidative stress
                      (Other) / tau (Other) / tunneling nanotubes (Other) / tau
                      Proteins (NLM Chemicals) / Tunneling Nanotubes (NLM
                      Chemicals) / alpha-Synuclein (NLM Chemicals) / Leucine-Rich
                      Repeat Serine-Threonine Protein Kinase-2 (NLM Chemicals)},
      cin          = {AG Heneka / AG Bano / AG Di Monte / AG Latz},
      ddc          = {610},
      cid          = {I:(DE-2719)1011303 / I:(DE-2719)1013003 /
                      I:(DE-2719)1013008 / I:(DE-2719)1013024},
      pnm          = {353 - Clinical and Health Care Research (POF4-353) / 351 -
                      Brain Function (POF4-351) / 352 - Disease Mechanisms
                      (POF4-352)},
      pid          = {G:(DE-HGF)POF4-353 / G:(DE-HGF)POF4-351 /
                      G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:39059388},
      doi          = {10.1016/j.neuron.2024.06.029},
      url          = {https://pub.dzne.de/record/272487},
}