Biologically active BMP-2 in early Xenopus laevis embryos.
In this study, we attempted to purify the dimeric BMP-2 from extracts of Xenopus embryos in order to show the presence of BMP-2 activity in the embryos. Immunoreactive BMP-2 protein was found to be a homodimer of an 18 kDa BMP-2 polypeptide linked through disulfide bridge(s). Biological activities of the partially purified dimeric BMP-2 were examined in vitro. The Xenopus BMP-2 induced alkaline phosphatase in a dose-dependent manner in cultured osteoblastic cells, MC3T3-E1. The inducing activity was synergistically enhanced by the presence of retinoic acid. The results showed that the dimeric form of Xenopus BMP-2 has an indistinguishable biological activity from that of mammalian BMP-2.
Shoda
A
A
Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
Murakami
K
K
Ueno
N
N
D000469:Alkaline Phosphatase / Q000096:biosynthesis; D000818:Animals; D019485:Bone Morphogenetic Proteins; D002417:Cattle; D002460:Cell Line; D002478:Cells, Cultured; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004305:Dose-Response Relationship, Drug; D004591:Electrophoresis, Polyacrylamide Gel; D004625:Embryo, Nonmammalian / Q000378:metabolism*; D004790:Enzyme Induction / Q000187:drug effects; D006031:Glycosylation; D006133:Growth Substances / Q000096:biosynthesis* / Q000494:pharmacology; D007700:Kinetics; D046911:Macromolecular Substances; D010006:Osteoblasts / Q000187:drug effects / Q000201:enzymology; D014176:Protein Biosynthesis; D011506:Proteins / Q000302:isolation & purification / Q000494:pharmacology; D014982:Xenopus laevis
D019485:Bone Morphogenetic Proteins; D006133:Growth Substances; D046911:Macromolecular Substances; D011506:Proteins; D000469:Alkaline Phosphatase