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Critical Reviews™ in Eukaryotic Gene Expression

Impact factor: 2.385

ISSN Print: 1045-4403
ISSN Online: 2162-6502

Critical Reviews™ in Eukaryotic Gene Expression

DOI: 10.1615/CritRevEukaryotGeneExpr.v13.i24.150
6 pages

P2 Receptors in Bone—Modulation of Osteoclast Formation and Activity via P2X7 Activation

Alison Gartland
University of Massachusetts Medical School, Department of Cell Biology, Worcester, MA 01655
Katherine A. Buckley
Human Bone Cell Research Group, Department of Human Anatomy and Cell Biology, The University of Liverpool, Liverpool, L69 3GE, UK
Robert A. Hipskind
Institut de Genetique Moleculaire de Montpellier, UMR 5535, Centre National de la Recherche Scientifique, 34293 Montpellier Cedex5, France
Wayne B. Bowler
Strakan Pharmaceuticals, Buckholm Mill Brae, Buckholm Mill, Galashiels, TD1 2HB, UK
James A. Gallagher
Human Bone Cell Research Group, Department of Human Anatomy and Cell Biology, The University of Liverpool, Liverpool, L69 3GE, UK

ABSTRACT

The concept that adenosine triphosphate (ATP) can act as an extracellular signaling molecule via interactions with specific purinergic receptors to mediate a wide variety of processes as diverse as neurotransmission (Edwards et al., 1992), inflammation (Perregaux et al., 1994), apoptosis (Chow et al., 1997), and bone remodelling (Jones et al., 1997; Morrison et al., 1998) is now widely accepted. Since the early work of Burnstock (Burnstock, 1972), the number of characterized P2 receptors responsive to extracellular nucleotides has increased dramatically. It is now known that both osteoblasts and osteoclasts express multiple P2 receptor subtypes, and the increasing number of nucleotide-induced effects reported to occur in bone serves to highlight the importance of these receptors in the bone microenvironment and the bone remodeling processes. In this article we will review work from our laboratory, and others, that has established nucleotides and P2 receptors as important signaling molecules in bone. In particular, we will focus on the expression of P2 receptors by osteoclasts and, more specifically, the P2X7 receptor and its paradoxical role in osteoclast function.