Hetero-oligomerization of XXXX A1 receptors with P2Y1 receptors in @entity35 brains.

@entity10298 @entity859 @entity35 @entity15094 @entity855
@entity859 and @entity855 modulate cellular and tissue functions via specific @entity10298 , respectively. Although, in general, @entity859 inhibits excitability and @entity855 functions as an excitatory transmitter in the central nervous system, little is known about the direct interaction between @entity10298 . We recently demonstrated that the G(i/o)-coupled @entity859 A1 receptor (A1R) and G(q/11)-coupled @entity15094 ( @entity15094 ) form a heteromeric complex with a unique pharmacology in cotransfected HEK293T cells using the coimmunoprecipitation of differentially epitope-tagged forms of the receptor [Yoshioka et al. (2001) Proc. Natl. Acad. Sci. USA 98, 7617-7622], although it remained to be determined whether this hetero-oligomerization occurs in vivo. In the present study, we first demonstrated a high degree of colocalization of A1R and @entity15094 by double immunofluorescence experiments with confocal laser microscopy in @entity35 cortex, hippocampus and cerebellum in addition to primary cultures of cortical neurons. Then, a direct association of A1R with @entity15094 was shown in coimmunoprecipitation studies using membrane extracts from these regions of @entity35 brain. Together, these results suggest the widespread colocalization of A1R and @entity15094 in @entity35 brain, and both receptors can exist in the same neuron, and therefore associate as hetero-oligomeric complexes in the @entity35 brain.
