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Differentiation Time Course Analysis of Gene Expression in Primary Osteoblasts from Wild Type and β-Arrestin 2 Knockout Mice

ABSTRACT: Gene expression analysis was performed on differentiating obsteoblasts isolated from calvaria of C57BL/6J wildtype or B-arrestin 2 knockout mice.

ORGANISM(S): Mus musculus

PROVIDER: GSE181459 | GEO | 2022/08/16

REPOSITORIES: GEO

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Differentiation Time Course Analysis of Gene Expression in Primary Osteoblasts from Wild Type and β-Arrestin 2 Knockout Mice

Project description:Differentiation Time Course Analysis of Gene Expression in Primary Osteoblasts from Wild Type and β-Arrestin 2 Knockout Mice

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Lung transcriptomes of wild type, β-arrestin 1 -/-, and β-arrestin 2 -/- mice exposed to normoxia or chronic hypoxia

Project description:We found that β-arrestin 1 -/- mice were more sensitive to hypoxia-induced pulmonary arterial hypertension with increased right ventricle hypertrophy and higher right ventricle systolic pressure, while β-arrestin 2 -/- mice developed right ventricle hypertrophy comparable to wild type mice. Moreover, β-arrestin 1 -/- mice had worse right ventricle function than wild type mice in response to chronic hypoxia, whereas β-arrestin 2 -/- mice relatively preserved right ventricle function compared to wild type mice. To investigate the molecular mechanisms responsible for the worse PAH in β-arrestin 1 -/- mice, we performed lung transcriptome analysis of wild type, β-arrestin 1 -/-, and β-arrestin 2 -/- mice using high-throughput RNA-seq.

2018-11-19 | GSE110131 | GEO

Parathyroid Hormone Treatment Effect on Gene Expression in Primary Calvarial Osteoblasts

Project description:The effect of parathyroid hormone (PTH) treatment was tested on osteoblasts prepared from calvaria of C57BL/6J mice 7-10 days old. Osteoblasts were treated with either human parathyroid hormone (1-34), bovine (D-Trp12,Tyr34) parathyroid hormone (7-34) amide or vehicle control for 4 hr. Gene expression effects were evaluated by DNA microarray.

2022-07-28 | GSE181284 | GEO

Delineation of a conserved arrestin-biased signaling repertoire in vivo

Project description:Biased G protein-coupled receptor agonists engender a restricted repertoire of downstream events from their cognate receptors, permitting them to produce mixed agonist-antagonist effects in vivo. While this opens the possibility of novel therapeutics, it complicates rational drug design, since the in vivo response to a biased agonist cannot be reliably predicted from its in vitro efficacy. We have employed novel informatic approaches to characterize the in vivo transcriptomic signature of the arrestin pathway-selective parathyroid hormone analog [D-Trp12, Tyr34]-bPTH(7-34) in six different murine tissues after chronic drug exposure. We find that [D-Trp12, Tyr34]-bPTH(7-34) elicits a distinctive arrestin-signaling focused transcriptomic response that is more coherently regulated across tissues than that of the pluripotent agonist, hPTH(1-34). This arrestin-focused network is closely associated with transcriptional control of cell growth and development. Our demonstration of a conserved arrestin-dependent transcriptomic signature suggests a framework within which the in vivo outcomes of arrestin-biased signaling may be generalized.

2015-03-05 | GSE64485 | GEO

β-arrestin 2 as an activator of cGAS-STING signaling and target of viral immune evasion

Project description:Virus infection may induce excessive interferon (IFN) responses that can lead to host tissue injury or even death. β-arrestin 2 regulates multiple cellular events through the G protein-coupled receptor (GPCR) signaling pathways. Here we demonstrate that β-arrestin 2 also promotes virus-induced production of IFN-β and clearance of viruses in macrophages. β-arrestin 2 interacts with cyclic GMP-AMP synthase (cGAS) and increases the binding of dsDNA to cGAS to enhance cyclic GMP-AMP (cGAMP) production and the downstreatm stimulator of interferon genes (STING) and innate immune responses. Mechanistically, deacetylation of β-arrestin 2 at Lys171 facilitates the activation of the cGAS–STING signaling and the production of IFN-β. In vitro, viral infection induces the degradation of β-arrestin 2 to facilitate immune evasion, while a β-blocker, carvedilol, rescues β-arrestin 2 expression to maintain the antiviral immune response. Our results thus identify a viral immune-evasion pathway via the degradation of β-arrestin 2, and also hint that carvedilol, approved for treating heart failure, can potentially be repurposed as an antiviral drug candidate.

2020-10-22 | GSE159735 | GEO

Micromass Time Course

Project description:Primary micromass cultures derived from 11.5 day old mouse embryo limb buds were cultured for 15 days in differentiating conditions (beta-glycerophosphate and ascorbic acid). Total RNA from differentiating chondrocytes was isolated every three days i.e. days 3,6,9,12 and 15 and hybridized to MOE430A chips. Objective: Gain a view of the temporal gene expression changes occuring during chondrocyte differentiation. Keywords = micromass culture Keywords = temporal gene expression Keywords = mouse Keywords = chondrocyte differentiation Keywords: time-course

2005-09-08 | GSE2154 | GEO

Exploring GPCR-arrestin interfaces with genetically encoded crosslinkers

Project description:-arrestins (arr1 and arr2) are ubiquitous regulators of G protein-coupled receptor (GPCR) signalling. Available data suggest that -arrestins dock to different receptors in different ways. However, the structural characterization of arrestin-GPCR complexes is challenging and alternative approaches to study arrestin-GPCR complexes are needed. Here, starting from the finger loop as a major site for the interaction of arrestins with GPCRs, we genetically incorporate non-canonical amino acids for photo- and chemical crosslinking into arr1 and arr2 and explore binding topologies to GPCRs forming either stable or transient complexes with arrestin: the vasopressin receptor 2 (rhodopsin-like), the corticotropin releasing factor receptor 1 and the parathyroid hormone receptor 1 (both secretin-like). We show that each receptor leaves a unique footprint on arrestin, whereas the two -arrestins yield quite similar crosslinking patterns. Furthermore, we show that the method allows defining the orientation of arrestin respect to the GPCR. Finally, we provide direct evidence for the formation of arrestin oligomers in the cell.

2020-09-21 | PXD020418 | Pride

Impact of beta-arrestin-2 deficiency on intestinal tumorigenesis in Apc-mutated mice

Project description:This SuperSeries is composed of the following subset Series: GSE24575: Beta-arrestin-2 deficiency effect on intestinal tumorigenesis in Apc-mutated mice GSE24576: Gene expression analysis of tumors from ApcD14/+ mice Refer to individual Series

2012-01-20 | E-GEOD-24577 | biostudies-arrayexpress

Time-course proteomic analysis of spontaneously differentiating human embryonic stem cells (hESCs)

Project description:Mass spectrometry analysis was carried out to investigate the protein expression landscape of RNA-binding proteins (RBPs) during a time-course of spontaneously differentiating human embryonic stem cells (hESCs). Mass spectrometry was performed on whole-cell extracts of differentiating TE03 (I3) hESCs at four time-points (days 0, 23, 39, and 54), each with two biological replicates.

2023-05-05 | PXD025274 | Pride

Molecular mechanism of β-arrestin-2 pre-activation by phosphatidylinositol 4,5-bisphosphate

Project description:Arrestins are a protein family that regulate G protein-coupled receptor (GPCR) signaling, with four distinct members in mammals (arrestin 1–4). Phosphorylated residues of G protein-coupled receptors bind to the N-domain of arrestin, resulting in C-terminus release. This induces further allosteric conformational changes, such as polar core disruption, alteration of interdomain loops, and domain rotation, which transform arrestins into the receptor-activated state. It is widely accepted that arrestin activation occurs by conformational changes propagated from the N- to the C-domain. However, recent studies have revealed that binding of phosphatidylinositol 4,5-bisphosphate (PIP2) to the C-domain transforms arrestins into an active state. In this study, we aimed to elucidate the mechanisms underlying PIP2-induced arrestin activation. We compared the conformational changes of β-arrestin-2 upon binding of PIP2 or phosphorylated C-tail peptide of vasopressin receptor type 2 (V2Rpp) using hydrogen/deuterium exchange mass spectrometry (HDX-MS). Introducing point mutations on the potential routes of the allosteric conformational changes and analyzing these mutant constructs with HDX-MS revealed that PIP2-binding at the C-domain affects the back loop, which destabilizes the gate loop and β-strand XX to transform β-arrestin-2 into the pre-active state.

2024-07-15 | PXD049391 | Pride

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