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J. Biochem, 1994, Vol. 115, No. 2 279-285
© 1994 Japanese Biochemical Society

research-article

Expression and Characterization of Human Bone Morphogenetic Protein-2 in Silkworm Larvae Infected with Recombinant Bombyx mori Nuclear Polyhedrosis Virus

Nobuhiro Ishida*,1, Masafumi Tsujimoto*, Toshimichi Kanaya**, Akio Shimamura***, Nobuo Tsuruoka*, Shiho Kodama*, Toyoko Katayama*, Shinzo Oikawa*, Masashi Matsui*, Toshihiro Nakanishi*, Jun Kobayashi****,2 and Hiroshi Nakazato*

*Suntory Institute for Biomedical Research Shimamoto, Mishima-gun, Osaka 618
**Research Institute of Biological Science, Katakura Industries Chuou, Matsumoto, Nagano 390
***Chuo-sanken Laboratory, Katakura Industries Shuno-okutomi, Sayama, Saitama 350-13
****Department of Insect Genetics and Breeding, National Institute of Sericultural and Entomological Science Ohwashi, Tsukuba, Ibaraki 305

1To whom correspondence should be addressed.

Recombinant human bone morphogenetic protein-2 (rhBMP-2) was expressed in silkworm larvae, and a milligram quantity of the protein was purified and characterized. The expressed rhBMP-2 was biologically active in terms of induction of alkaline phosphatase activity in MC3T3-E1 cells and ectopic bone formation in mice. On SDS-polyacrylamide gel electrophoretic analysis, the purified protein showed a 16 kDa band under reducing conditions and a 30 kDa band under non-reducing conditions. The silkworm-expressed rhBMP-2 was glycosylated and susceptible to endo-ß-N-acetylglucosaminidase F (endo F) and endo H, but resistant to endo D. Deglycosylated rhBMP-2 treated with endo F retained its biological activity. These results suggest that rhBMP-2 exists as a dimer and disulfide bond(s) are responsible for the dimerization. Moreover, sugar chains have no direct effect on the biological activity of the protein. The availability of a quite large amount of rhBMP-2 has allowed us to study the biological function of this interesting factor in detail.

2Present address, Faculty of Engineering, Mie University, Kamihamacho, Tsu, Mie 514.


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