title: NG2 cells, a new trail for Alzheimer's disease mechanisms?
abstract: BACKGROUND
  Neuron Glial 2 (NG2) cells are glial cells known to serve as oligodendrocyte progenitors as well as modulators of the neuronal network. Altered NG2 cell morphology and up-regulation as well as increased shedding of the proteoglycan NG2 expressed on the cell surface have been described in rodent models of brain injury. Here we describe alterations in the human NG2 cell population in response to pathological changes characteristic of Alzheimer's disease (AD).
  
  
  RESULTS
  Immunohistological stainings of postmortem brain specimens from clinically diagnosed and postmortem verified AD patients and non-demented controls revealed reduced NG2 immunoreactivity as well as large numbers of NG2 positive astrocytes in individuals with high amyloid beta plaque load. Since fibrillar amyloid beta (Aβ)1-42 is the major component of AD-related senile plaques, we exposed human NG2 cells to oligomer- and fibril enriched preparations of Aβ1-42. We found that both oligomeric and fibrillar Aβ1-42 induced changes in NG2 cell morphology. Further, in vitro exposure to fibrillar Aβ1-42 decreased the NG2 concentrations in both cell lysates and supernatants. Interestingly, we also found significantly decreased levels of soluble NG2 in the cerebrospinal fluid (CSF) from clinically diagnosed AD patients compared to non-demented individuals. Additionally, the CSF NG2 levels were found to significantly correlate with the core AD biomarkers Aß1-42, T-tau and P-tau.
  
  
  CONCLUSIONS
  Our results demonstrate major alterations in the NG2 cell population in relation to AD pathology which highlights the NG2 cell population as a new attractive research target in the search for cellular mechanisms associated with AD pathogenesis.
authors.affiliation: Department of Clinical Sciences Malmö, Molecular Memory Research Unit, Lund University, The Wallenberg Laboratory 2nd floor, Inga Marie Nilssons gata, entrance 53, Skåne University Hospital, Malmö, 205 02, Sweden. malin.wennstrom@med.lu.se.
authors.forename: Henrietta M
authors.initials: HM
authors.lastname: Nielsen
authors.forename: Danyal
authors.initials: D
authors.lastname: Ek
authors.forename: Una
authors.initials: U
authors.lastname: Avdic
authors.forename: Camilla
authors.initials: C
authors.lastname: Orbjörn
authors.forename: Oskar
authors.initials: O
authors.lastname: Hansson
authors.forename: Robert
authors.initials: R
authors.lastname: Veerhuis
authors.forename: Annemieke Jm
authors.initials: AJ
authors.lastname: Rozemuller
authors.forename: Arne
authors.initials: A
authors.lastname: Brun
authors.forename: Lennart
authors.initials: L
authors.lastname: Minthon
authors.forename: Malin
authors.initials: M
authors.lastname: Wennström
mesh_terms: D000368:Aged; D000369:Aged, 80 and over; D000544:Alzheimer Disease / Q000473:pathology / Q000503:physiopathology*; D016229:Amyloid beta-Peptides / Q000378:metabolism*; D000941:Antigens / Q000378:metabolism*; D001253:Astrocytes / Q000473:pathology / Q000502:physiology; D015415:Biomarkers / Q000134:cerebrospinal fluid; D001921:Brain / Q000473:pathology / Q000503:physiopathology*; D002470:Cell Survival / Q000502:physiology; D002478:Cells, Cultured; D005260:Female; D006801:Humans; D008297:Male; D008875:Middle Aged; D009457:Neuroglia / Q000473:pathology / Q000502:physiology*; D010446:Peptide Fragments / Q000378:metabolism*; D010766:Phosphorylation; D058225:Plaque, Amyloid / Q000473:pathology / Q000503:physiopathology*; D011509:Proteoglycans / Q000378:metabolism*; D016875:tau Proteins / Q000134:cerebrospinal fluid; D000099216:Chondroitin Sulfate Proteoglycan 4
chemical_list: D016229:Amyloid beta-Peptides; D000941:Antigens; D015415:Biomarkers; D010446:Peptide Fragments; D011509:Proteoglycans; D016875:tau Proteins; D000099216:Chondroitin Sulfate Proteoglycan 4; C054369:MAPT protein, human; C075222:amyloid beta-protein (1-42)