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@ARTICLE{Lerche:163488,
      author       = {Lerche, Stefanie and Sjödin, Simon and Brinkmalm, Ann and
                      Blennow, Kaj and Wurster, Isabel and Roeben, Benjamin and
                      Zimmermann, Milan and Hauser, Ann-Kathrin and
                      Liepelt-Scarfone, Inga and Waniek, Katharina and Lachmann,
                      Ingolf and Gasser, Thomas and Zetterberg, Henrik and
                      Brockmann, Kathrin},
      title        = {{CSF} {P}rotein {L}evel of {N}eurotransmitter {S}ecretion,
                      {S}ynaptic {P}lasticity, and {A}utophagy in {PD} and {DLB}.},
      journal      = {Movement disorders},
      volume       = {36},
      number       = {11},
      issn         = {1531-8257},
      address      = {New York, NY},
      publisher    = {Wiley},
      reportid     = {DZNE-2022-00248},
      pages        = {2595 - 2604},
      year         = {2021},
      abstract     = {Molecular pathways associated with α-synuclein
                      proteostasis have been detected in genetic studies and in
                      cell models and include autophagy, ubiquitin-proteasome
                      system, mitochondrial homeostasis, and synaptic plasticity.
                      However, we lack biomarkers that are representative for
                      these pathways in human biofluids.The objective of this
                      study was to evaluate CSF protein profiles of pathways
                      related to α-synuclein proteostasis.We assessed CSF protein
                      profiles associated with neurotransmitter secretion, synapse
                      plasticity, and autophagy in 2 monocentric cohorts with
                      α-synucleinopathy (385 PD patients and 67 DLB patients). We
                      included 80 PD patients and 17 DLB patients with variants in
                      the glucocerebrosidase gene to serve as proxy for
                      accelerated α-synuclein pathology with pronounced clinical
                      trajectories.(1) Proteins associated with neurotransmitter
                      secretion, synaptic plasticity, and endolysosomal autophagy
                      were lower in PD and DLB patients compared with healthy
                      controls. (2) These patterns were more pronounced in DLB
                      than in PD patients, accentuated by GBA variant status in
                      both entities. (3) CSF levels of these proteins were
                      positively associated with CSF levels of total α-synuclein,
                      with lower levels of proteostasis proteins related to lower
                      levels of total α-synuclein. (4) These findings could be
                      confirmed longitudinally. PD patients with low CSF profiles
                      of proteostasis proteins showed lower CSF levels of
                      α-synuclein longitudinally compared with PD patients with a
                      normal proteostasis profile.CSF proteins associated with
                      neurotransmitter secretion, synaptic plasticity, and
                      endolysosomal autophagy might serve as biomarkers related to
                      α-synuclein proteostasis in PD and DLB. © 2021 The
                      Authors. Movement Disorders published by Wiley Periodicals
                      LLC on behalf of International Parkinson and Movement
                      Disorder Society.},
      keywords     = {Autophagy / Biomarkers / Glucosylceramidase / Humans / Lewy
                      Body Disease / Neuronal Plasticity / Neurotransmitter Agents
                      / Parkinson Disease: metabolism / alpha-Synuclein:
                      metabolism / CSF (Other) / GBA (Other) / PD (Other) /
                      lysosome (Other) / secretion (Other) / synaptic plasticity
                      (Other) / Biomarkers (NLM Chemicals) / Neurotransmitter
                      Agents (NLM Chemicals) / alpha-Synuclein (NLM Chemicals) /
                      Glucosylceramidase (NLM Chemicals)},
      cin          = {AG Gasser / Core ICRU},
      ddc          = {610},
      cid          = {I:(DE-2719)1210000 / I:(DE-2719)1240005},
      pnm          = {353 - Clinical and Health Care Research (POF4-353)},
      pid          = {G:(DE-HGF)POF4-353},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34180557},
      doi          = {10.1002/mds.28704},
      url          = {https://pub.dzne.de/record/163488},
}