Identification and characterization of cellular binding proteins (receptors) for recombinant human bone morphogenetic protein 2B, an initiator of bone differentiation cascade

Vishwas M. Paralkar, R. Glenn Hammonds, A Hari Reddi

Research output: Contribution to journalArticle

51 Scopus citations

Abstract

Bone morphogenetic protein 2B (BMP 2B), is a heparin-binding bone differentiation factor that initiates endochondral bone formation in rats when implanted subcutaneously. The molecular mechanism of action of this differentiation factor is not known, and as a first step we have examined BMP 26-responsive cells for the presence of specific cellular binding proteins. Using 125I-labeled BMP 2B, specific high-affinity binding sites for recombinant human BMP 2B on MC3T3 E1 osteoblast-like cells as well as on NIH 3T3 fibroblasts were identified. Platelet-derived growth factor, insulin-like growth factor 1, basic fibroblast growth factor, epidermal growth factor, and transforming growth factor β did not compete for the binding of radiolabeled BMP 2B. The binding of BMP 2B is a time- and temperature-dependent process. Chemical crosslinking of radiolabeled BMP showed two components (apparent size, 200 and 70 kDa in MC3T3 El cells and 200 and 90 kDa in NIH 3T3 cells). A minor component at 60 kDa was also detected in both cell lines. Scatchard analysis of the binding data showed a high-affinity receptor with an apparent dissociation constant of 128 ± 40 pM in MC3T3 El cells. These data demonstrate specific, high-affinity cell-surface binding proteins for BMP 2B.

Original languageEnglish (US)
Pages (from-to)3397-3401
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume88
Issue number8
StatePublished - 1991
Externally publishedYes

Keywords

  • Bone cells
  • Cartilage
  • Development
  • Morphogenesis
  • Transforming growth factor β superfamily

ASJC Scopus subject areas

  • General
  • Genetics

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