Osteoclast recruiting activity in bone matrix

T. A. Hentunen, N. S. Cunningham, O. Vuolteenaho, A Hari Reddi, H. K. Vaananen

Research output: Contribution to journalArticlepeer-review

20 Scopus citations


An activity that recruits osteoclasts has been identified and partially characterized from bone matrix. Bone-derived osteoclast recruiting activity (BORA) was co-purified with osteogenin, a bone inductive protein. Osteogenin was extracted from bovine bone with 6 M urea and purified by chromatography on hydroxyapatite, heparin-Sepharose and Sephacryl S-200 gel filtration. The biologically active osteoclast formation-stimulating material was further purified by C18 reverse phase HPLC. BORA is obviously distinct from osteogenin and transforming growth factor β (TGF-β), since further purified osteogenin and pure TGF-β did not stimulate the formation of osteoclast-like cells. BORA (0.1-10 μg/ml) stimulated the formation of tartrate-resistant acid phosphatase (TRAP)-positive multinucleated cells (MNC) in a dose-dependent manner. These multinucleated cells resorbed bone when cultured on bovine bone slices. The effect of BORA is primarily directed to differentiate osteoclast precursors, since it did not stimulate osteoclast function in in vitro resorption assay where disaggregated rat osteoclasts were cultured on bovine bone slices. However, after 24 h preincubation with 50 nM PTH in the mouse calvaria assay, BORA at 10 μg/ml significantly stimulated bone resorption.

Original languageEnglish (US)
Pages (from-to)183-198
Number of pages16
JournalBone and Mineral
Issue number3
StatePublished - 1994
Externally publishedYes


  • Bone matrix
  • Osteoclast recruitment
  • Osteogenin
  • TGF-β

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Surgery


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