@article{vandeKerkhofFekkesvanderHeijdenetal.2016,
  author    = {van de Kerkhof, Nora WA and Fekkes, Durk and van der Heijden, Frank MMA and Hoogendijk, Witte JG and St{\"o}ber, Gerald and Egger, Jos IM and Verhoeven, Willem MA},
  title     = {Cycloid psychoses in the psychosis spectrum: evidence for biochemical differences with schizophrenia},
  series = {Neuropsychiatric Disease and Treatment},
  volume    = {12},
  journal   = {Neuropsychiatric Disease and Treatment},
  doi       = {10.2147/NDT.S101317},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-166255},
  pages     = {1927-1933},
  year      = {2016},
  abstract  = {Cycloid psychoses (CP) differ from schizophrenia regarding symptom profile, course, and prognosis and over many decades they were thought to be a separate entity within the psychosis spectrum. As to schizophrenia, research into the pathophysiology has focused on dopamine, brain-derived neurotrophic factor, and glutamate signaling in which, concerning the latter, the N-methyl-d-aspartate receptor plays a crucial role. The present study aims to determine whether CP can biochemically be delineated from schizophrenia. Eighty patients referred for psychotic disorders were assessed with the Comprehensive Assessment of Symptoms and History, and (both at inclusion and after 6 weeks of antipsychotic treatment) with the Positive and Negative Syndrome Scale and Clinical Global Impression. From 58 completers, 33 patients were diagnosed with schizophrenia and ten with CP according to the Diagnostic and Statistical Manual of Mental Disorders, Fourth Edition, and Leonhard criteria, respectively. Fifteen patients were diagnosed with other disorders within the psychosis spectrum. At both time points, blood levels of the dopamine metabolite homovanillic acid, brain-derived neurotrophic factor, and amino acids related to glutamate neurotransmission were measured and compared with a matched control sample. Patients with CP showed a significantly better response to antipsychotic treatment as compared to patients with schizophrenia. In CP, glycine levels were elevated and tryptophan levels were lowered as compared to schizophrenia. Glutamate levels were increased in both patient groups as compared to controls. These results, showing marked differences in both treatment outcome and glutamate-related variable parameters, may point at better neuroplasticity in CP, necessitating demarcation of this subgroup within the psychosis spectrum.},
  language  = {en}
}
@article{TretterMukherjeeMaricetal.2012,
  author    = {Tretter, Verena and Mukherjee, Jayanta and Maric, Hans-Michael and Schindelin, Hermann and Sieghart, Werner and Moss, Stephen J.},
  title     = {Gephyrin, the enigmatic organizer at GABAergic synapses},
  series = {Frontiers in Cellular Neuroscience},
  volume    = {6},
  journal   = {Frontiers in Cellular Neuroscience},
  number    = {23},
  doi       = {10.3389/fncel.2012.00023},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-133356},
  year      = {2012},
  abstract  = {GABA(A) receptors are clustered at synaptic sites to achieve a high density of postsynaptic receptors opposite the input axonal terminals. This allows for an efficient propagation of GABA mediated signals, which mostly result in neuronal inhibition. A key organizer for inhibitory synaptic receptors is the 93 kDa protein gephyrin that forms oligomeric superstructures beneath the synaptic area. Gephyrin has long been known to be directly associated with glycine receptor beta subunits that mediate synaptic inhibition in the spinal cord. Recently, synaptic GABA(A) receptors have also been shown to directly interact with gephyrin and interaction sites have been identified and mapped within the intracellular loops of the GABA(A) receptor alpha 1, alpha 2, and alpha 3 subunits. Gephyrin-binding to GABA(A) receptors seems to be at least one order of magnitude weaker than to glycine receptors (GlyRs) and most probably is regulated by phosphorylation. Gephyrin not only has a structural function at synaptic sites, but also plays a crucial role in synaptic dynamics and is a platform for multiple protein-protein interactions, bringing receptors, cytoskeletal proteins and downstream signaling proteins into close spatial proximity.},
  language  = {en}
}