Expression profile of the entire family of AdhesionG protein-coupled receptors in mouse and rat

Haitina, Tatjana; Olsson, Fredrik; Stephansson, Olga; Alsiö, Johan; Roman, Erika; Ebendal, Ted; Schiöth, Helgi B.; Fredriksson, Robert

doi:10.1186/1471-2202-9-43

Cited by 57 publications

(45 citation statements)

References 42 publications

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“…The high affinity of this binding (K D = 1-20 nM), along with the nature of C1ql proteins as small secreted proteins and of BAI3 as a membrane-bound GPCR, suggest that BAI3 is a genuine receptor for C1ql proteins in the brain. Both C1ql and BAI3 proteins are expressed in adult animals almost exclusively in the brain and appear to be enriched in neurons (11,12,31). Strikingly, the addition of the recombinant gC1q domains of C1ql proteins to the medium of cultured hippocampal neurons caused significant decreases in synapse density without affecting other measured morphological parameters (Figs.…”

Section: Discussionmentioning

confidence: 95%

“…The extracellular sequences of BAI proteins are composed of an N-terminal CUB domain, five (BAI1) or four (BAI2 and BAI3) thrombospondin type 1 repeats, a hormonebinding domain, and the GPS (10,11). RNA quantification and in situ hybridization have indicated that in adult mice, BAI proteins are expressed primarily in the brain, with low-level expression in other tissues (12)(13)(14)(15). The BAI1 gene, originally identified in a screen for p53-inducible genes, is thought to inhibit neovascularization, a process required for tumor growth (10,13,(16)(17)(18)(19).…”

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confidence: 99%

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The cell-adhesion G protein-coupled receptor BAI3 is a high-affinity receptor for C1q-like proteins

Bolliger¹,

Martinelli²,

Südhof

2011

Proc. Natl. Acad. Sci. U.S.A.

159

168

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C1q-like genes (C1ql1-C1ql4) encode small, secreted proteins that are expressed in differential patterns in the brain but whose receptors and functions remain unknown. BAI3 protein, in contrast, is a member of the cell-adhesion class of G protein-coupled receptors that are expressed at high levels in the brain but whose ligands have thus far escaped identification. Using a biochemical approach, we show that all four C1ql proteins bind to the extracellular thrombospondin-repeat domain of BAI3 with high affinity, and that this binding is mediated by the globular C1q domains of the C1ql proteins. Moreover, we demonstrate that addition of submicromolar concentrations of C1ql proteins to cultured neurons causes a significant decrease in synapse density, and that this decrease was prevented by simultaneous addition of the thrombospondin-repeat fragment of BAI3, which binds to C1ql proteins. Our data suggest that C1ql proteins are secreted signaling molecules that bind to BAI3 and act, at least in part, to regulate synapse formation and/or maintenance.

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Section: Discussionmentioning

confidence: 95%

mentioning

confidence: 99%

The cell-adhesion G protein-coupled receptor BAI3 is a high-affinity receptor for C1q-like proteins

Bolliger¹,

Martinelli²,

Südhof

2011

Proc. Natl. Acad. Sci. U.S.A.

159

168

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“…AY140958). They have been classified as novel aGPCR in human and encode putative aGPCR in the mouse genome (Fredriksson et al, 2002;Bjarnadottir et al, 2007;Haitina et al, 2008;Lum et al, 2010). Gpr116 was initially named Ig-Hepta because of its two immunoglobulin and 7TM spanning domains (Abe et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Characterization and functional study of a cluster of four highly conserved orphan adhesion‐GPCR in mouse

Prömel

Waller-Evans

Dixon

et al. 2012

Developmental Dynamics

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Background: Adhesion G protein-coupled receptors (aGPCR) constitute a structurally and functionally diverse class of seven-transmembrane receptor proteins. Although for some of the members important roles in immunology, neurology, as well as developmental biology have been suggested, most receptors have been poorly characterized. Results: We have studied evolution, expression, and function of an entire receptor group containing four uncharacterized aGPCR: Gpr110, Gpr111, Gpr115, and Gpr116. We show that the genomic loci of these four receptors are clustered tightly together in mouse and human genomes and that this cluster likely derives from a single common ancestor gene. Using transcriptional profiling on wild-type and knockout/LacZ reporter knockin mice strains, we have obtained detailed expression maps that show ubiquitous expression of Gpr116, co-expression of Gpr111 and Gpr115 in developing skin, and expression of Gpr110 in adult kidney. Loss of Gpr110, Gpr111, or Gpr115 function did not result in detectable defects, indicating that genes of this aGPCR group might function redundantly. Conclusions: The aGPCR cluster Gpr110, Gpr111, Gpr115, and Gpr116 developed from one common ancestor in vertebrates. Expression suggests a role in epithelia, and one can speculate about a possible redundant function of GPR111 and GPR115. Developmental Dynamics 241:1591-1602, 2012.V C 2012 Wiley Periodicals, Inc.

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“…Nervous System and Behavior. Most Adhesion GPCRs are present in nervous tissues, and some are especially highly expressed in the brain (Haitina et al, 2008;Regard et al, 2008). While not critical for the survival of individual neurons per se, these Adhesion GPCRs seem to jointly control various high-level functions that are characteristic of the brain as an organ.…”

Section: Skeletal Muscle and Bonementioning

confidence: 99%

International Union of Basic and Clinical Pharmacology. XCIV. Adhesion G Protein–Coupled Receptors

et al. 2015

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Expression profile of the entire family of AdhesionG protein-coupled receptors in mouse and rat

Cited by 57 publications

References 42 publications

The cell-adhesion G protein-coupled receptor BAI3 is a high-affinity receptor for C1q-like proteins

The cell-adhesion G protein-coupled receptor BAI3 is a high-affinity receptor for C1q-like proteins

Characterization and functional study of a cluster of four highly conserved orphan adhesion‐GPCR in mouse

International Union of Basic and Clinical Pharmacology. XCIV. Adhesion G Protein–Coupled Receptors

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