PMID- 25869610
OWN - NLM
STAT- MEDLINE
DCOM- 20160314
LR  - 20181113
IS  - 1559-1166 (Electronic)
IS  - 0895-8696 (Linking)
VI  - 56
IP  - 2
DP  - 2015 Jun
TI  - Amyloid-beta Activates Microglia and Regulates Protein Expression in a Manner 
      Similar to Prions.
PG  - 509-18
LID - 10.1007/s12031-015-0553-2 [doi]
AB  - Prions are the only convincingly demonstrated proteinaceous infectious particle, 
      yet recent studies find that amyloid-beta peptide (Abeta) aggregates are capable of 
      self-propagation, which induces amyloidosis pathology in Alzheimer's disease (AD) 
      model mice that is similar to the self-propagation phenomenon of prions in 
      neurons. Gliosis is a common hallmark of AD and prion diseases, in which 
      activated microglia accumulate around abnormal protein deposits. Analyses of the 
      characteristics of activated microglia induced by Abeta in comparison with those 
      induced by prions will provide new insight into the pathogenesis of AD. 
      Therefore, we compared the characteristics of BV-2 cells (model microglia) 
      activated by Abeta fibrillar peptides (Abeta1-42) and prions (PrP106-126). Abeta1-42 and 
      PrP106-126, as well as the supernatants of the media collected from BV-2 cells 
      cocultured with Abeta1-42 and PrP106-126, were potent activators of BV-2 microglial 
      activity, but the chemotaxis index (CI) induced by Abeta1-42 was significantly 
      higher than that induced by PrP106-126 at each concentration. Abeta1-42 and 
      PrP106-126 increased the proliferation index (PI) and upregulated monocyte 
      chemoattractant protein-1 (MCP-1) and transforming growth factor beta 1 (TGF-beta1) 
      expression after 12 h of exposure. Our results show that Abeta activates microglia 
      and regulates microglial protein expression in a manner similar to prions and, 
      thus, provide new insight into the pathogenesis of AD.
FAU - Tu, Jian
AU  - Tu J
AD  - State Key Laboratories for Agrobiotechnology, National Animal Transmissible 
      Spongiform Encephalopathy Laboratory, College of Veterinary Medicine, China 
      Agricultural University, 100193, Beijing, China, tujian1980@126.com.
FAU - Chen, Baian
AU  - Chen B
FAU - Yang, Lifeng
AU  - Yang L
FAU - Qi, Kezong
AU  - Qi K
FAU - Lu, Jing
AU  - Lu J
FAU - Zhao, Deming
AU  - Zhao D
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20150414
PL  - United States
TA  - J Mol Neurosci
JT  - Journal of molecular neuroscience : MN
JID - 9002991
RN  - 0 (Amyloid beta-Peptides)
RN  - 0 (Ccl2 protein, mouse)
RN  - 0 (Chemokine CCL2)
RN  - 0 (Peptide Fragments)
RN  - 0 (Prions)
RN  - 0 (Transforming Growth Factor beta1)
RN  - 0 (amyloid beta-protein (1-42))
RN  - 0 (prion protein (106-126))
SB  - IM
MH  - Amyloid beta-Peptides/*toxicity
MH  - Animals
MH  - Cell Line
MH  - Chemokine CCL2/genetics/*metabolism
MH  - Mice
MH  - Microglia/drug effects/*metabolism
MH  - Peptide Fragments/*toxicity
MH  - Prions/*toxicity
MH  - Transforming Growth Factor beta1/genetics/*metabolism
MH  - *Up-Regulation
EDAT- 2015/04/15 06:00
MHDA- 2016/03/15 06:00
CRDT- 2015/04/15 06:00
PHST- 2015/01/21 00:00 [received]
PHST- 2015/03/24 00:00 [accepted]
PHST- 2015/04/15 06:00 [entrez]
PHST- 2015/04/15 06:00 [pubmed]
PHST- 2016/03/15 06:00 [medline]
AID - 10.1007/s12031-015-0553-2 [doi]
PST - ppublish
SO  - J Mol Neurosci. 2015 Jun;56(2):509-18. doi: 10.1007/s12031-015-0553-2. Epub 2015 
      Apr 14.