Biologically active human bone morphogenetic protein 4 fused to collagen-binding domain produced in silkworm-baculovirus expression system

抄録

Human bone morphogenetic protein 4 (BMP4) fused to the collagen-binding domain (CBD) of fibronectin was constructed and expressed in a silkworm-baculovirus expression system. When recombinant BmNPV was injected into the silkworm larvae and harvested after approximately 4 days, 0.22mg/ml (0.1mg/larva) of recombinant CBD-BMP4 was secreted into the silkworm haemolymph. Interestingly, cultured silkworm cells infected with the same recombinant virus could not secrete the recombinant CBD-BMP4 into culture media. The purified rCBD-BMP4 showed Smad- and MAPK-stimulating activities in human UET-13 cells.