Lgr8 transcripts were also detected in frontal and motor cortices. The comparative distribution of LGR8 (receptor protein) was examined by autoradiography of [(125)I]-human INSL3 binding sites, with high densities detected in the thalamus, especially in Pf, and in the entire striatum-the caudate putamen (CP mu), islands of Calleja,

olfactory tubercle, nucleus accumbens-with lower levels in distinct layers of cerebral cortex. Notably, these areas also receive dopaminergic projections. These findings demonstrate the existence of LGR8 in neuronal soma in the thalamus and axons/terminals in thalamic target areas such as the striatum and frontal cortex. LGR8 was also detected throughout the medial habenula-fasciculus retroflexus-interpeduncular nucleus pathway, further indicating this website that the Selleckchem NVP-BGJ398 receptor is transported from mRNA-expressing soma to remote axonal/terminal sites. These findings suggest the existence of a broadly distributed LGR8 signaling system in the rat involved in sensorimotor, limbic and cognitive functions. Further studies are now required to elucidate the

precise function of LGR8, under normal and pathological conditions, as importantly, several of the equivalent receptor-positive areas in human brain are part of the pathology of neurodegenerative conditions including Parkinson’s disease. (C) 2008 IBRO. Published by Elsevier Ltd. All rights reserved.”
“Cytoplasmic inclusions in respiratory syncytial

virus-infected cells comprising viral nucleocapsid proteins (L, N, P, and M2-1) and the viral genome are sites of viral transcription. Although not believed to be necessary for transcription, Epothilone B (EPO906, Patupilone) the matrix (M) protein is also present in these inclusions, and we have previously shown that M inhibits viral transcription. In this study, we have investigated the mechanisms for the association of the M protein with cytoplasmic inclusions. Our data demonstrate for the first time that the M protein associates with cytoplasmic inclusions via an interaction with the M2-1 protein. The M protein colocalizes with M2-1 in the cytoplasm of cells expressing only the M and M2-1 proteins and directly interacts with M2-1 in a cell-free binding assay. Using a cotransfection system, we confirmed that the N and P proteins are sufficient to form cytoplasmic inclusions and that M2-1 localizes to these inclusions; additionally, we show that M associates with cytoplasmic inclusions only in the presence of the M24 protein. Using truncated mutants, we show that the N-terminal 110 amino acids of M mediate the interaction with M24 and the subsequent association with nucleocapsids. The interaction or M2-1 with M and, in particular, the N-terminal region or m may represent a target for novel antivirals that block the association of M with nucleocapsids, thereby inhibiting virus assembly.