Infection, neurodegeneration, and other conditions associated with loss of brain
homeostasis, induce changes in microglial morphology, gene expression and function,
generally referred to as “activation”. Alzheimer’s disease (AD) is the most common
dementia and is characterized by neuroinfammatory changes, including alterations
in the morphology and distribution of microglia and astrocytes, and deposition of
complement and other infammatory mediators. Our previous observations show that
microglial cells challenged in vitro with amyloid peptides clustered and rounded up,
dramatically changing their morphology. Besides, in these cells we observed the early
acetylation and then the phosphorylation of STAT3 which is required for the expression
of the epsilon isoform of 14-3-3, a marker of Abeta-activated microglia (1, 2). We
applied afnity partitioning approach combined with high throughput mass spectrometric
analysis in order to identify variation of proteins on plasma membrane of BV2
immortalized microglia upon treatment with amyloid peptides. By this method several
proteins up- or down-regulated by amyloid treatment were identifed in microglial
plasma membrane. Among them annexins (5 and 7), IFITM3 and MARK3. These data
have been confrmed in primary microglial cultures.
In microglia, plasma membrane plays a relevant role in the cross-talking with the external neuronal
environment and in the resulting trophic or infammatory response of these sentinel cells. As such,
knowledge of the microglia responsiveness to beta amyloids in term of changes in its plasma
membrane proteome is imperative for unveiling the molecular landscape in which AD occurs
