Identification and characterization of cellular binding proteins (receptors) for recombinant human bone morphogenetic protein 2B, an initiator of bone differentiation cascade
- National Inst. of Health, Bethesda, MD (United States)
- Genentech, Inc., San Francisco, CA (United States)
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 the authors have examined BMP 2B-responsive cells for the presence of specific cellular binding proteins. Using {sup 125}I-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, epidermal growth factor, and transforming growth factor {beta} 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. These data demonstrate specific, high-affinity cell-surface binding proteins for BMP 2B.
- OSTI ID:
- 6055802
- Journal Information:
- Proceedings of the National Academy of Sciences of the United States of America; (United States), Vol. 88:8; ISSN 0027-8424
- Country of Publication:
- United States
- Language:
- English
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550601* - Medicine- Unsealed Radionuclides in Diagnostics