A novel Xenopus homologue of bone morphogenetic protein-7 (BMP-7).

We identified a Xenopus gene closely related to mammalian bone morphogenetic protein (BMP)-7 (also termed osteogenic protein-1 or OP-1). It resembles the mammalian gene in primary structure and expression pattern much more closely than does a previously described Xenopus homologue, originally termed XBMP-7 [Nishimatsu, Suzuki, Shoda, Murakami and Ueno (1992) Biochem. Biophys.

Frzb-1, an antagonist of Wnt-1 and Wnt-8, does not block signaling by Wnts -3A, -5A, or -11.

Frzb-1 is a secreted factor that was recently shown to inhibit signaling by Wnts 1 and 8. Frzb-1 contains an amino terminal domain that is homologous to the Drosophila polarity gene frizzled; several other secreted proteins that share this feature have now been identified. These findings raise the question of whether or not Frzb-1 is a general inhibitor of signaling by all Wnts.

Frzb, a secreted protein expressed in the Spemann organizer, binds and inhibits Wnt-8.

We isolated a Xenopus homolog of Frzb, a newly described protein containing an amino-terminal Frizzled motif. It dorsalized Xenopus embryos and was expressed in the Spemann organizer during early gastrulation. Unlike Frizzled proteins, endogenous Frzb was soluble.

Anti-dorsalizing morphogenetic protein is a novel TGF-beta homolog expressed in the Spemann organizer.

We have identified a novel growth factor in Xenopus, which is most closely related to human Bone Morphogenetic Protein-3. Its expression peaks during gastrulation, most prominently in the Spemann organizer, and persists in the posterior neural floor plate and prechordal plate during neurulation. Injection of the corresponding mRNA into dorsal blastomeres results in dose-dependent suppression of dorsal and anterior structures, even in the presence of lithium chloride.

Factors responsible for the Ca(2+)-dependent inactivation of calcineurin in brain.

The Ca(2+)-dependent protein phosphatase activity of crude rat brain extracts measured in the presence of okadaic acid, exhibits the characteristic properties of the calmodulin-stimulated protein phosphatase, calcineurin. It is stimulated more than 200-fold by Ca2+ and inhibited by the calmodulin-binding peptide, M13, and by the immunosuppressive drug, FK506. It is insensitive to rapamycin at concentrations up to 1 microM.