RANKL–RANK signaling regulates expression of xenotropic and polytropic virus receptor (XPR1) in osteoclasts

► XPR1 is a receptor for xenotropic and polytropic viruses. ► XPR1 is expressed in monocyte precursors of osteoclasts. ► RANKL–RANK signaling differentiates osteoclast precursors into osteoclasts. ► RANKL–RANK signaling up-regulates XPR1 mRNA in differentiated osteoclasts. ► XPR1 protein is localize...

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Veröffentlicht in:Biochemical and biophysical research communications 2010-08, Vol.399 (2), p.129-132
Hauptverfasser: Sharma, Parul, Patntirapong, Somying, Hann, Steven, Hauschka, Peter V.
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Patntirapong, Somying
Hann, Steven
Hauschka, Peter V.
description ► XPR1 is a receptor for xenotropic and polytropic viruses. ► XPR1 is expressed in monocyte precursors of osteoclasts. ► RANKL–RANK signaling differentiates osteoclast precursors into osteoclasts. ► RANKL–RANK signaling up-regulates XPR1 mRNA in differentiated osteoclasts. ► XPR1 protein is localized to peripheral membranes in mature osteoclasts. Formation of multinucleated bone-resorbing osteoclasts results from activation of the receptor activated NF-κB ligand (RANKL)–receptor activated NF-κB (RANK) signaling pathway in primary bone marrow macrophages and a macrophage cell line (RAW 264.7). Osteoclasts, through bone remodeling, are key participants in the homeostatic regulation of calcium and phosphate levels within the body. Microarray analysis using Gene Expression Dynamic Inspector (GEDI) clustering software indicated that osteoclast differentiation is correlated with an increase in xenotropic and polytropic virus receptor 1 (XPR1) mRNA transcripts. XPR1 is a receptor of the xenotropic and polytropic murine leukemia virus and homolog of yeast Syg1 and plant Pi transporter PHO1. Quantitative PCR was used to validate the up-regulation of XPR1 message following RANKL stimulation in both primary bone marrow cells and a macrophage cell line. Immunostaining for the XPR1 protein showed that there is translocation of XPR1 to the membranes of the sealing zone in mature osteoclasts. This study is the first to demonstrate that the expression of retro-viral receptor, XPR1, is regulated by RANKL–RANK signaling.
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Formation of multinucleated bone-resorbing osteoclasts results from activation of the receptor activated NF-κB ligand (RANKL)–receptor activated NF-κB (RANK) signaling pathway in primary bone marrow macrophages and a macrophage cell line (RAW 264.7). Osteoclasts, through bone remodeling, are key participants in the homeostatic regulation of calcium and phosphate levels within the body. Microarray analysis using Gene Expression Dynamic Inspector (GEDI) clustering software indicated that osteoclast differentiation is correlated with an increase in xenotropic and polytropic virus receptor 1 (XPR1) mRNA transcripts. XPR1 is a receptor of the xenotropic and polytropic murine leukemia virus and homolog of yeast Syg1 and plant Pi transporter PHO1. Quantitative PCR was used to validate the up-regulation of XPR1 message following RANKL stimulation in both primary bone marrow cells and a macrophage cell line. Immunostaining for the XPR1 protein showed that there is translocation of XPR1 to the membranes of the sealing zone in mature osteoclasts. 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Formation of multinucleated bone-resorbing osteoclasts results from activation of the receptor activated NF-κB ligand (RANKL)–receptor activated NF-κB (RANK) signaling pathway in primary bone marrow macrophages and a macrophage cell line (RAW 264.7). Osteoclasts, through bone remodeling, are key participants in the homeostatic regulation of calcium and phosphate levels within the body. Microarray analysis using Gene Expression Dynamic Inspector (GEDI) clustering software indicated that osteoclast differentiation is correlated with an increase in xenotropic and polytropic virus receptor 1 (XPR1) mRNA transcripts. XPR1 is a receptor of the xenotropic and polytropic murine leukemia virus and homolog of yeast Syg1 and plant Pi transporter PHO1. Quantitative PCR was used to validate the up-regulation of XPR1 message following RANKL stimulation in both primary bone marrow cells and a macrophage cell line. Immunostaining for the XPR1 protein showed that there is translocation of XPR1 to the membranes of the sealing zone in mature osteoclasts. 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subjects Animals
Bone marrow
Cell Line
GEDI
Mice
Mice, Inbred C57BL
Mice, Transgenic
Microarray
Murine leukemia virus
Osteoclastogenesis
Osteoclasts - metabolism
RANK Ligand - metabolism
Receptor Activator of Nuclear Factor-kappa B - metabolism
Receptors, G-Protein-Coupled - biosynthesis
Receptors, G-Protein-Coupled - genetics
Receptors, Virus - biosynthesis
Receptors, Virus - genetics
Signal Transduction
Virus receptor
XPR1
title RANKL–RANK signaling regulates expression of xenotropic and polytropic virus receptor (XPR1) in osteoclasts
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