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@ARTICLE{Leliveld:62865,
      author       = {Leliveld, S. R. and Bader, V. and Hendriks, P. and
                      Prikulis, I. and Sajnani, G. and Requena, J. R. and Korth,
                      C.},
      title        = {{I}nsolubility of disrupted-in-schizophrenia 1 disrupts
                      oligomer-dependent interactions with nuclear distribution
                      element 1 and is associated with sporadic mental disease},
      journal      = {The journal of neuroscience},
      volume       = {28},
      issn         = {0270-6474},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {PreJuSER-62865},
      pages        = {3839 - 3845},
      year         = {2008},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Disrupted-in-schizophrenia 1 (DISC1) and other genes have
                      been identified recently as potential molecular players in
                      chronic psychiatric diseases such as affective disorders and
                      schizophrenia. A molecular mechanism of how these genes may
                      be linked to the majority of sporadic cases of these
                      diseases remains unclear. The chronic nature and
                      irreversibility of clinical symptoms in a subgroup of these
                      diseases prompted us to investigate whether proteins
                      corresponding to candidate genes displayed subtle features
                      of protein aggregation. Here, we show that in postmortem
                      brain samples of a distinct group of patients with
                      phenotypes of affective disorders or schizophrenia, but not
                      healthy controls, significant fractions of DISC1 could be
                      identified as cold Sarkosyl-insoluble protein aggregates. A
                      loss-of-function phenotype could be demonstrated for
                      insoluble DISC1 through abolished binding to a key DISC1
                      ligand, nuclear distribution element 1 (NDEL1): in human
                      neuroblastoma cells, DISC1 formed expression-dependent,
                      detergent-resistant aggregates that failed to interact with
                      endogenous NDEL1. Recombinant (r) NDEL1 expressed in
                      Escherichia coli selectively bound an octamer of an rDISC1
                      fragment but not dimers or high molecular weight multimers,
                      suggesting an oligomerization optimum for molecular
                      interactions of DISC1 with NDEL1. For DISC1-related sporadic
                      psychiatric disease, we propose a mechanism whereby impaired
                      cellular control over self-association of DISC1 leads to
                      excessive multimerization and subsequent formation of
                      detergent-resistant aggregates, culminating in loss of
                      ligand binding, here exemplified by NDEL1. We conclude that
                      the absence of oligomer-dependent ligand interactions of
                      DISC1 can be associated with sporadic mental disease of
                      mixed phenotypes.},
      keywords     = {Animals / Brain Chemistry / Cadaver / Carrier Proteins:
                      metabolism / Cell Line, Tumor / Drug Interactions /
                      Escherichia coli: metabolism / Humans / Ligands / Mice /
                      Mice, Transgenic / Mood Disorders: genetics / Mood
                      Disorders: metabolism / Nerve Tissue Proteins: chemistry /
                      Nerve Tissue Proteins: metabolism / Phenotype / Proteome:
                      isolation $\&$ purification / Recombinant Proteins:
                      metabolism / Schizophrenia: genetics / Schizophrenia:
                      metabolism / Solubility / Carrier Proteins (NLM Chemicals) /
                      DISC1 protein, human (NLM Chemicals) / Ligands (NLM
                      Chemicals) / NDEL1 protein, human (NLM Chemicals) / Nerve
                      Tissue Proteins (NLM Chemicals) / Proteome (NLM Chemicals) /
                      Recombinant Proteins (NLM Chemicals) / J (WoSType)},
      cin          = {INB-2},
      ddc          = {590},
      cid          = {I:(DE-Juel1)VDB805},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Neurosciences},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:18400883},
      UT           = {WOS:000255012400003},
      doi          = {10.1523/JNEUROSCI.5389-07.2008},
      url          = {https://juser.fz-juelich.de/record/62865},
}