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Cited by 61Bone Metabolism and DiseasesBone and Dental Protein StudiesOsteomyelitis and Bone Disorders Research

Osteoprotegerin ligand regulates osteoclast adherence to the bone surface in mouse calvaria.

O'Brien, E.A., Williams, J.H.H., Marshall, M.J.·2000·Biochemical and Biophysical Research Communications
DOI 10.1006/bbrc.2000.3129
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Abstract

The stimulators of bone resorption, prostaglandin E(2) (PGE(2)) and 1,25-dihydroxyvitamin D(3) (1,25D(3)), act through osteoblast-like cells to activate osteoclasts. One candidate for the intermediary produced by osteoblasts that subsequently stimulates the osteoclast is osteoprotegerin ligand (OPGL). OPGL has been shown to stimulate osteoclast differentiation and activation. The aim of the work reported here was to determine if soluble recombinant extracellular domain of human OPGL would bring about the change in osteoclast adhesion from the periosteum of mouse calvaria to the adjacent bone surface that occurs with the above-mentioned stimulators of resorption. This change in adherence or translocation of osteoclasts onto the bone surface required the expression and functioning of the integrin subunit, beta 3. We show that this soluble OPGL, like PGE(2) and 1,25D(3), stimulated the release of osteoclasts from the periosteum and their adherence to the bone surface accompanied by an increase in staining for immunolocalized integrin subunit beta 3. Recombinant human osteoprotegerin (OPG), which binds strongly to OPGL, inhibited this translocation of osteoclasts that occurred with PGE(2) and 1,25D(3), leaving integrin beta-3-negative osteoclasts on the periosteum. PGE(2) and 1,25D(3) increased the expression of messenger RNA for OPGL compared with indomethacin-treated controls after 6 h exposure. Evidence is presented that the change in the adhesion of osteoclasts from the periosteum to the bone surface, resulting in osteoclast activation, is mediated by OPGL.

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Crossref · 10.1006/bbrc.2000.3129

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  • RANKL is involved in osteoclast precursor fusion, differentiation into mature osteoclasts, attachment to bone, activation to resorb bone, and survival by avoiding apoptosis.

    “RANKL was implicated in the fusion of osteoclast precursors into multinucleated cells (39), their differentiation into mature osteoclasts (39), their attachment to bone surfaces (12), their activation to resorb bone (9,39), and their continued survival by avoiding apoptosis (11).”

    From Receptor Activator of Nuclear Factor κB Ligand and Osteoprotegerin Regulation of Bone Remodeling in Health and Disease (2008) · cites this paper as [12]

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Authors
O'Brien, E. A., Williams, J. H. H., & Marshall, M. J.
Affiliations
  • University of Chester (GB)
  • Robert Jones and Agnes Hunt Orthopaedic Hospital (GB)
ORCID
Venue
Biochemical and Biophysical Research Communications
Publisher
Elsevier BV
Published
2000-08
Volume
274
Issue
2
Pages
281-290
ISSN
0006-291X (ISSN-L)
DOI
10.1006/bbrc.2000.3129
OpenAlex
W1995862119
Cited by
61
References
30
Citations by year
2025: 1 · 2022: 1 · 2020: 1 · 2019: 1 · 2018: 1 · 2016: 2 · 2013: 8 · 2012: 7
FWCI
1.20
Type
journal article
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Biochemical and Biophysical Research Communications (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bone Metabolism and Diseases
  • Health Sciences › Medicine › Rheumatology › Bone and Dental Protein Studies
  • Health Sciences › Medicine › Rheumatology › Osteomyelitis and Bone Disorders Research
Keywords
osteoprotegerin ligand, osteoclast adhesion, bone resorption, CD61, periosteum, prostaglandin E2, 1,25-dihydroxyvitamin D3, osteoprotegerin, osteoclast activation, calvaria, bone surface
MeSH terms
Tartrate-Resistant Acid Phosphatase, Acid Phosphatase, Animals, Bone Resorption, Calcitriol, Carrier Proteins, Cell Adhesion, Cell Count, Cells, Cultured, Dose-Response Relationship, Drug, Indomethacin, Isoenzymes, Membrane Glycoproteins, Mice, Inbred BALB C, Osteoclasts, Peptides, Periosteum, Platelet Membrane Glycoproteins, RNA, Messenger, Skull, Dinoprostone, Antigens, CD, Reverse Transcriptase Polymerase Chain Reaction, Intercellular Signaling Peptides and Proteins, Integrin beta3, Mice, RANK Ligand, Receptor Activator of Nuclear Factor-kappa B, In Vitro Techniques

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