Direct binding of follistatin to a complex of bone-morphogenetic protein and its receptor inhibits ventral and epidermal cell fates in early Xenopus embryo
Direct binding of follistatin to a complex of bone-morphogenetic protein and its receptor inhibits ventral and epidermal cell fates in early Xenopus embryo
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DOI：
10.1073/pnas.95.16.9337
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发表时间：
1998-08-04
影响因子：
11.1
通讯作者：
Ueno, N
中科院分区：
文献类型：
--
作者：
Iemura, S;Yamamoto, TS;Ueno, N
在非洲爪蟾早期发育过程中，已知多肽生长因子的活性受其结合蛋白的负调控。在本研究中，卵泡抑素，最初被称为激活素结合蛋白，被证明在早期非洲爪蟾胚胎中抑制骨形态发生蛋白（BMP）活性的各个方面。此外，使用表面等离子体共振生物传感器，我们证明了卵泡抑素可以直接与多种骨形成蛋白在显着高亲和力。有趣的是，发现卵泡抑素与BMP受体的配体结合是非竞争性的，并且与BMP及其受体形成三聚体复合物。结果表明，卵泡抑素作为一个组织因子在早期两栖动物胚胎发生抑制BMP活性的不同机制所使用的chordin和noggin。
In early development of Xenopus laevis, it is known that activities of polypeptide growth factors are negatively regulated by their binding proteins, In this study, follistatin, originally known as an activin-binding protein, was shown to inhibit all aspects of bone morphogenetic protein (BMP) activity in early Xenopus embryos. Furthermore, using a surface plasmon resonance biosensor, we demonstrated that follistatin can directly interact with multiple BMPs at significantly high affinities. Interestingly, follistatin was found to be noncompetitive with the BMP receptor for ligand binding and to form a trimeric complex with BMP and its receptor. The results suggest that follistatin acts as an organizer factor in early amphibian embryogenesis by inhibiting BMP activities by a different mechanism from that used by chordin and noggin.