Porous 50:50 poly(d,l lactide-co-glycolide) microspheres containing varying amounts of ''free'' recombinant human bone morphogenetic protein-2 (rhBMP-2) were evaluated for their ability to induce/enhance expression of osteoblastic characteristics by pluripotent mesenchymal cells in vitro. ''Free'' p
Biotinated bone morphogenetic protein-2: In vivo and in vitro activity
β Scribed by H. Uludag; J. Golden; R. Palmer; J. M. Wozney
- Publisher
- John Wiley and Sons
- Year
- 1999
- Tongue
- English
- Weight
- 98 KB
- Volume
- 65
- Category
- Article
- ISSN
- 0006-3592
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β¦ Synopsis
Recombinant human bone morphogenetic protein-2 (rhBMP-2) was biotinated, and the bioactivity of biotinated protein was assessed in vitro (alkaline phosphate induction in limb bud cells) and in vivo (osteoinduction in the rat ectopic assay). Amino-biotinated rhBMP-2 exhibited an increase in bioactivity whereas carboxy-biotinated rhBMP-2 did not exhibit any changes in bioactivity in vitro. Avidin inhibited the bioactivity of amino-biotinated but not carboxyl-biotinated rhBMP-2. Both amino-and carboxy-modified rhBMP-2 induced bone at an equivalent level to that of unmodified rhBMP-2 in vivo. The presence of avidin did not affect the osteoinductive activity of both types of biotinated rhBMP-2. The overall results indicated that binding to a large protein, avidin, might affect rhBMP-2 activity in vitro depending on the binding site; however, in vivo activity was unaffected by the avidin binding.
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