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Osteoclast Derivation from Mouse Bone Marrow
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The ADP receptor P2RY12 regulates osteoclast function and pathologic bone remodeling.

Xinming Su1, Desiree H Floyd, Alun Hughes

  • 1Department of Medicine, Division of Oncology, Washington University in St. Louis School of Medicine, St. Louis, Missouri 63110, USA.

The Journal of Clinical Investigation
|September 22, 2012
PubMed
Summary

The P2RY12 receptor, crucial for platelet aggregation, also drives osteoclast activity. Inhibiting this receptor in mice reduced bone loss and osteolysis, suggesting P2RY12 inhibitors could treat bone diseases.

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Area of Science:

  • Bone Biology
  • Immunology
  • Pharmacology

Background:

  • The adenosine diphosphate (ADP) receptor P2RY12 is vital for platelet function.
  • Extracellular ADP influences osteoclast activity, but P2RY12's role in osteoclasts remains unclear.

Purpose of the Study:

  • To investigate the function of mouse P2RY12 in osteoclast biology and bone homeostasis.
  • To determine if P2RY12 inhibition can prevent pathological bone loss.

Main Methods:

  • Utilized P2ry12 knockout mice and wild-type littermates.
  • Assessed osteoclast differentiation, adhesion, and resorptive activity in vitro.
  • Administered clopidogrel, a P2RY12 inhibitor, to mice in models of bone loss.
  • Examined signaling pathways including RAP1 and integrin activation.

Main Results:

  • P2ry12 knockout mice exhibited reduced osteoclast activity and partial protection from age-related bone loss.
  • Extracellular ADP enhanced osteoclast adhesion and resorption in wild-type but not P2ry12 knockout cells.
  • P2RY12 signaling was essential for ADP-induced RAP1 and integrin activation in osteoclasts.
  • P2ry12 knockout mice and clopidogrel-treated mice were protected from various forms of pathological bone loss.

Conclusions:

  • P2RY12 is the principal ADP receptor mediating osteoclast function.
  • P2RY12 inhibition represents a promising therapeutic strategy for conditions characterized by excessive bone resorption and osteolysis.