Human stem cell-derived monocytes and microglia-like cells reveal impaired amyloid plaque clearance upon heterozygous or homozygous loss of TREM2

Alzheimers Dement. 2019 Mar;15(3):453-464. doi: 10.1016/j.jalz.2018.09.006. Epub 2018 Nov 12.

Abstract

Introduction: Murine microglia expressing the Alzheimer's disease-linked TREM2R47H mutation display variable decrease in phagocytosis, while impaired phagocytosis is reported following loss of TREM2. However, no data exist on TREM2+/R47H human microglia. Therefore, we created human pluripotent stem cell (hPSC) monocytes and transdifferentiated microglia-like cells (tMGs) to examine the effect of the TREM2+/R47H mutation and loss of TREM2 on phagocytosis.

Methods: We generated isogenic TREM2+/R47H, TREM2+/-, and TREM2-/- hPSCs using CRISPR/Cas9. Following differentiation to monocytes and tMGs, we studied the uptake of Escherichia coli fragments and analyzed amyloid plaque clearance from cryosections of APP/PS1+/- mouse brains.

Results: We demonstrated that tMGs resemble cultured human microglia. TREM2+/- and TREM2-/- hPSC monocytes and tMGs phagocytosed significantly less E. coli fragments and cleared less amyloid plaques than wild-type hPSC progeny, with no difference for TREM2+/R47H progeny.

Discussion: In vitro phagocytosis of hPSC monocytes and tMGs was not affected by the TREM2+/R47H mutation but was significantly impaired in TREM2+/- and TREM2-/- progeny.

Keywords: Alzheimer's disease; Human amyloid plaques; Human pluripotent stem cells; Microglia; Monocytes; Phagocytosis; TREM2.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid beta-Protein Precursor / genetics
  • Amyloid beta-Protein Precursor / metabolism
  • Animals
  • Brain
  • CRISPR-Cas Systems
  • Cells, Cultured
  • Escherichia coli
  • Membrane Glycoproteins / deficiency*
  • Membrane Glycoproteins / genetics
  • Mice, Transgenic
  • Microglia / metabolism*
  • Monocytes / metabolism*
  • Phagocytosis
  • Plaque, Amyloid / metabolism*
  • Pluripotent Stem Cells
  • Presenilin-1 / genetics
  • Presenilin-1 / metabolism
  • Receptors, Immunologic / deficiency*
  • Receptors, Immunologic / genetics

Substances

  • APP protein, human
  • Amyloid beta-Protein Precursor
  • Membrane Glycoproteins
  • PSEN1 protein, human
  • Presenilin-1
  • Receptors, Immunologic
  • TREM2 protein, human