Abstract

BackgroundGPR125 belongs to the family of Adhesion G protein-coupled receptors (GPCRs). A single copy of GPR125 was found in many vertebrate genomes. We also identified a Drosophila sequence, DmCG15744, which shares a common ancestor with the entire Group III of Adhesion GPCRs, and also contains Ig, LRR and HBD domains which were observed in mammalian GPR125.ResultsWe found specific expression of GPR125 in cells of the choroid plexus using in situ hybridization and protein-specific antibodies and combined in situ/immunohistochemistry co-localization using cytokeratin, a marker specific for epithelial cells. Induction of inflammation by LPS did not change GPR125 expression. However, GPR125 expression was transiently increased (almost 2-fold) at 4 h after traumatic brain injury (TBI) followed by a decrease (approximately 4-fold) from 2 days onwards in the choroid plexus as well as increased expression (2-fold) in the hippocampus that was delayed until 1 day after injury.ConclusionThese findings suggest that GPR125 plays a functional role in choroidal and hippocampal response to injury.

Highlights

  • GPR125 belongs to the family of Adhesion G protein-coupled receptors (GPCRs)

  • The GPCR proteolytic site (GPS) domain is conserved in all sequences except DmCG15744

  • Intron-exon boundaries were conserved between human, rat and mouse GPR125 and between the two teleost sequences but there was no conservation of boundaries between these and DmCG15744

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Summary

Introduction

GPR125 belongs to the family of Adhesion G protein-coupled receptors (GPCRs). A single copy of GPR125 was found in many vertebrate genomes. Gprotein-coupled receptors (GPCRs) form one of the largest gene families in the human genome and participate in a wide range of physiological and sensory functions Their ability to mediate specific signals over the cell membrane contributes to the fact that about 25% of the 100 top-selling pharmaceutical targets are GPCRs [1]. The N-termini of the Adhesion family, known as family B2 [3] or LNBTM7 [4], are very different from those of the other groups since these consist of long stretches rich in serine and threonine which produce a stalk-like formation projecting from the cell membrane This structure is probably very important for cell-to-cell interactions. The Adhesion GPCRs can be further subdivided into groups IVIII based on phylogeny (sequence similarity) and virtually all of them contain the GPCR proteolytic site (GPS) domain [6]

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