title: Coordination of BMP-3b and cerberus is required for head formation of Xenopus embryos.
abstract: Bone morphogenetic proteins (BMPs) and their antagonists are involved in the axial patterning of vertebrate embryos. We report that both BMP-3b and BMP-3 dorsalize Xenopus embryos, but act as dissimilar antagonists within the BMP family. BMP-3b injected into Xenopus embryos triggered secondary head formation in an autonomous manner, whereas BMP-3 induced aberrant tail formation. At the molecular level, BMP-3b antagonized nodal-like proteins and ventralizing BMPs, whereas BMP-3 antagonized only the latter. These differences are due to divergence of their pro-domains. Less BMP-3b than BMP-3 precursor is proteolytically processed in embryos. BMP-3b protein associated with a monomeric form of Xnrl, a nodal-like protein, whereas BMP-3 did not. These molecular features are consistent with their expression profiles during Xenopus development. XBMP-3b is expressed in the prechordal plate, while xBMP-3 is expressed in the notochord. Using antisense morpholino oligonucleotides, we found that the depletion of both xBMP-3b and cerberus, a head inducer, caused headless Xenopus embryos, whereas the depletion of both xBMP-3 and cerberus affected the size of the somite. These results revealed that xBMP-3b and cerberus are essential for head formation regulated by the Spemann organizer, and that xBMP-3b and perhaps xBMP-3 are involved in the axial patterning of Xenopus embryos.
authors.affiliation: Department of Biochemistry, National Cardiovascular Center Research Institute, Suita, Osaka 565-8565, Japan.
authors.forename: Jun
authors.initials: J
authors.lastname: Hino
authors.forename: Shin-ichiro
authors.initials: S
authors.lastname: Nishimatsu
authors.forename: Takeharu
authors.initials: T
authors.lastname: Nagai
authors.forename: Hisayuki
authors.initials: H
authors.lastname: Matsuo
authors.forename: Kenji
authors.initials: K
authors.lastname: Kangawa
authors.forename: Tsutomu
authors.initials: T
authors.lastname: Nohno
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D019521:Body Patterning / Q000187:drug effects; D055396:Bone Morphogenetic Protein 2; D055398:Bone Morphogenetic Protein 3; D019485:Bone Morphogenetic Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D016466:CHO Cells; D002678:Chimera / Q000378:metabolism; D017124:Conserved Sequence; D006224:Cricetinae; D004625:Embryo, Nonmammalian; D004627:Embryonic Induction; D018507:Gene Expression Regulation, Developmental; D006133:Growth Substances / Q000235:genetics / Q000378:metabolism; D006257:Head / Q000196:embryology*; D036341:Intercellular Signaling Peptides and Proteins; D008969:Molecular Sequence Data; D016376:Oligonucleotides, Antisense / Q000494:pharmacology; D011506:Proteins / Q000235:genetics / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D016212:Transforming Growth Factor beta; D014981:Xenopus / Q000196:embryology*; D029867:Xenopus Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D055396:Bone Morphogenetic Protein 2; D055398:Bone Morphogenetic Protein 3; D019485:Bone Morphogenetic Proteins; D006133:Growth Substances; D036341:Intercellular Signaling Peptides and Proteins; D016376:Oligonucleotides, Antisense; D011506:Proteins; D016212:Transforming Growth Factor beta; D029867:Xenopus Proteins; C100866:cer1 protein, Xenopus