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Potent ectopic bone-inducing activity of bone morphogenetic protein-4/7 heterodimer.

Abstract：

:We have purified and characterized recombinant Xenopus bone morphogenetic proteins (xBMPs): homodimers of xBMP-4, 7 and heterodimers (xBMP-4/7) produced by a baculovirus expression system. Highly purified xBMPs had homogeneous NH2-termini predicted from a consensus motif, Arg-X-X-Arg, while they possessed diverse sugar chains. Implantation of xBMPs together with pure collagen carrier in rats induced new bone formation in a dose-dependent manner. The xBMP-4/7 heterodimer showed the strongest activity, with an effective dose of 1-30 micrograms, while more than 10 micrograms of xBMP-4 or 7 homodimer was required for a significant effect. Histological examination revealed that xBMP-4/7 implants showed intramembranous ossification without chondrogenesis. In primary cultures of rat bone marrow stromal cells, xBMP-4/7 induced alkaline phosphatase 3-fold more strongly than xBMP-7 and 20-fold more than xBMP-4. These results suggest that the heterodimeric form of BMP would generate the strongest signal triggering osteogenic differentiation of osteoprogenitor cells in adult tissues.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Aono A,Hazama M,Notoya K,Taketomi S,Yamasaki H,Tsukuda R,Sasaki S,Fujisawa Y

doi

10.1006/bbrc.1995.1712

subject

Has Abstract

pub_date

1995-05-25 00:00:00

pages

670-7

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(85)71712-3

journal_volume

210

pub_type

杂志文章

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