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The effect of P2X7R-mediated Ca2+ signaling in OPG-induced osteoclasts adhesive structure damage

Yonggang Ma1, Hongyan Zhao1, Chung Chile1

  • 1College of Veterinary Medicine, Yangzhou University, Yangzhou, Jiangsu, 225009, PR China; Jiangsu Co-innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Yangzhou, Jiangsu, 225009, PR China; Joint International Research Laboratory of Agriculture and Agri-Product Safety of the Ministry of Education of China, Yangzhou University, Yangzhou, Jiangsu, 225009, PR China.

Experimental Cell Research
|August 16, 2019
PubMed

Insights

Osteoprotegerin impairs osteoclast adhesion by reducing P2X7R and calcium signaling. Restoring these pathways can reverse this damage, highlighting the P2X7R-Ca2+-NFATc1 pathway

Area of Science:

  • Cell Biology
  • Biochemistry
  • Bone Biology

Background:

  • Osteoclast adhesion is crucial for bone resorption, a process regulated by various signaling pathways.
  • Osteoprotegerin (OPG) inhibits osteoclast differentiation and bone resorption, partly through calcium (Ca2+) signaling.
  • Purinergic receptor P2X7 (P2X7R) influences osteoclastogenesis via nuclear factor of activated T cells 1 (NFATc1) activation, but its role in OPG-mediated effects on osteoclast adhesion is not fully understood.

Purpose of the Study:

  • To investigate the role of P2X7R in OPG-induced damage to osteoclast adhesion structure.
  • To elucidate the underlying molecular mechanisms involving Ca2+ signaling and downstream effectors.

Main Methods:

  • Assessed the effects of OPG on P2X7R expression, PYK2 and SRC phosphorylation, and intracellular Ca2+ levels in osteoclasts.
  • Utilized calcium chelators (BAPTA-AM/W-7) to examine their impact on OPG-induced osteoclast adhesion damage and signaling.
  • Employed P2X7R knockdown to evaluate its specific contribution to osteoclast differentiation, adhesion, and signaling.

Main Results:

  • OPG reduced P2X7R expression, PYK2/SRC phosphorylation, and Ca2+ concentration, impairing Ca2+-NFATc1 signaling and osteoclast adhesion.
  • BAPTA-AM/W-7 treatment partially or fully restored osteoclast adhesion structure, PYK2/SRC phosphorylation, cytoskeletal dynamics, and bone resorption activity by enhancing Ca2+-NFATc1 signaling.
  • P2X7R knockdown inhibited osteoclast differentiation and cytoskeletal organization but paradoxically exacerbated OPG-induced adhesion damage, indicating a protective role of P2X7R under OPG treatment.

Conclusions:

  • The P2X7R-Ca2+-NFATc1 signaling pathway is critically involved in mediating OPG-induced damage to osteoclast adhesion structure.
  • OPG-induced osteoclast dysfunction is linked to suppressed P2X7R and impaired Ca2+ signaling, affecting cytoskeletal integrity and bone resorption.
  • Targeting the P2X7R-Ca2+-NFATc1 pathway may offer therapeutic strategies for bone diseases characterized by abnormal bone resorption.
Keywords:
Adhesion structureCa(2+)OsteoclastOsteoprotegerinP2X7R

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