@entity3264 receptors function as scaffolds for the regulation of b-amyloid and cellular XXXX signaling complexes.

@entity1 @entity3264 @entity10611 @entity73 @entity10092 @entity3669 @entity179 @entity195 @entity4495 @entity2359
@entity195 ( @entity195 ) is a progressive @entity179 that affects 36 million @entity1 worldwide, but currently has no effective treatment options. One of the original hallmarks of @entity195 are plaques comprised of beta amyloid (Ab) and neurofibrillary tangles comprised of phosphorylated Tau protein. However, it is soluble oligomeric Ab which is more closely correlated with @entity73 and is therefore considered to be the @entity2359 species. Oligomeric Ab has recently been shown to form complexes with the @entity4495 ( @entity10611 )-anchored membrane protein, cellular @entity3669 ( @entity3669 ), and these complexes are believed to play an important role in the progression of @entity195 pathogenesis. @entity3264 , the major excitatory neurotransmitter is responsible for mediating learning and memory under normal physiological conditions. However, the dysregulation of glutamatergic signaling has also been implicated in a number of @entity179 including @entity195 . @entity3264 acts via both ionotropic @entity3264 receptors (iGluR) and metabotropic @entity3264 receptors (mGluR), each of which have been implicated in @entity195 . There is now growing evidence to suggest that @entity10092 may contribute the @entity195 pathogenesis by acting as scaffolds for the @entity3669 /Ab oligomer complex, enabling the propagation of @entity2359 signaling in @entity195 . In addition, @entity3669 and Ab oligomer signaling via NMDARs may also contribute to @entity195 pathology. The current review overviews our current understanding of the role of @entity3669 and Ab oligomers in regulating @entity3264 receptor signaling, as well as highlights the importance of understanding these signaling complexes to develop more effective therapeutic strategies to treat @entity195 .
