PMID- 23267328
OWN - NLM
STAT- PubMed-not-MEDLINE
DCOM- 20121226
LR  - 20211021
IS  - 1664-042X (Electronic)
IS  - 1664-042X (Linking)
VI  - 3
DP  - 2012
TI  - Postsynaptic Receptors for Amyloid-beta Oligomers as Mediators of Neuronal Damage in 
      Alzheimer's Disease.
PG  - 464
LID - 10.3389/fphys.2012.00464 [doi]
LID - 464
AB  - The neurotoxic effect of amyloid-beta peptide (Abeta) over the central synapses has 
      been described and is reflected in the decrease of some postsynaptic excitatory 
      proteins, the alteration in the number and morphology of the dendritic spines, 
      and a decrease in long-term potentiation. Many studies has been carried out to 
      identify the putative Abeta receptors in neurons, and is still no clear why the Abeta 
      oligomers only affect the excitatory synapses. Abeta oligomers bind to neurite and 
      preferentially to the postsynaptic region, where the postsynaptic protein-95 
      (PSD-95) is present in the glutamatergic synapse, and interacts directly with the 
      N-methyl-D-aspartate receptor (NMDAR) and neuroligin (NL). NL is a postsynaptic 
      protein which binds to the presynaptic protein, neurexin to form a heterophilic 
      adhesion complex, the disruption of this interaction affects the integrity of the 
      synaptic contact. Structurally, NL has an extracellular domain homolog to 
      acetylcholinesterase, the first synaptic protein that was found to interact with 
      Abeta. In the present review we will document the interaction between Abeta and the 
      extracellular domain of NL-1 at the excitatory synapse, as well as the 
      interaction with other postsynaptic components, including the glutamatergic 
      receptors (NMDA and mGluR5), the prion protein, the neurotrophin receptor, and 
      the alpha7-nicotinic acetylcholine receptor. We conclude that several Abeta oligomers 
      receptors exist at the excitatory synapse, which could be the responsible for the 
      neurotoxic effect described for the Abeta oligomers. The characterization of the 
      interaction between Abeta receptors and Abeta oligomers could help to understand the 
      source of the neurologic damage observed in the brain of the Alzheimer's disease 
      patients.
FAU - Dinamarca, Margarita C
AU  - Dinamarca MC
AD  - Centro de Envejecimiento y Regeneracion, Departamento de Biologia Celular y 
      Molecular, Facultad de Ciencias Biologicas, Pontificia Universidad Catolica de 
      Chile Santiago, Chile.
FAU - Rios, Juvenal A
AU  - Rios JA
FAU - Inestrosa, Nibaldo C
AU  - Inestrosa NC
LA  - eng
PT  - Journal Article
DEP - 20121220
PL  - Switzerland
TA  - Front Physiol
JT  - Frontiers in physiology
JID - 101549006
PMC - PMC3526732
OTO - NOTNLM
OT  - Alzheimer's disease
OT  - Abeta oligomers
OT  - neuroligin-1
OT  - postsynaptic receptors
OT  - synaptotoxicity
EDAT- 2012/12/26 06:00
MHDA- 2012/12/26 06:01
PMCR- 2012/12/20
CRDT- 2012/12/26 06:00
PHST- 2012/08/20 00:00 [received]
PHST- 2012/11/22 00:00 [accepted]
PHST- 2012/12/26 06:00 [entrez]
PHST- 2012/12/26 06:00 [pubmed]
PHST- 2012/12/26 06:01 [medline]
PHST- 2012/12/20 00:00 [pmc-release]
AID - 10.3389/fphys.2012.00464 [doi]
PST - epublish
SO  - Front Physiol. 2012 Dec 20;3:464. doi: 10.3389/fphys.2012.00464. eCollection 
      2012.