Biologically active synthetic peptides as probes of embryonic development: a competitive peptide inhibitor of fibronectin function inhibits gastrulation in amphibian embryos and neural crest cell migration in avian embryos.

Biologically active synthetic peptides as probes of embryonic development: a competitive peptide inhibitor of fibronectin function inhibits gastrulation in amphibian embryos and neural crest cell migration in avian embryos.
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生物活性合成肽作为胚胎发育的探针:纤连蛋白功能的竞争性肽抑制剂抑制两栖动物胚胎中的胃肠液和鸟类胚胎中神经rest细胞迁移。

DOI:
10.1083/jcb.99.5.1822
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发表时间:
1984-11
影响因子:
7.8
通讯作者:
Thiery, J P
Thiery, J P
中科院分区:
生物学1区
文献类型:
--
作者:
Boucaut, J C;Darribere, T;Poole, T J;Aoyama, H;Yamada, K M;Thiery, J P

文献摘要

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我们描述了一种新的方法来分析胚胎事件依赖于一个特定的肽识别信号。纤连蛋白中的一个短的特异性氨基酸序列被认为是纤连蛋白介导的相互作用中的识别位点。成纤维细胞与纤连蛋白的粘附被某些合成肽竞争性抑制,包括十肽Arg-Gly-Asp-Ser-Pro-Ala-Ser-Ser-Lys-Pro,其似乎含有细胞识别序列。我们发现,这种肽抑制两栖类原肠胚和鸟类神经嵴细胞迁移在体内,以及在体外的附着和迁移的神经嵴细胞。这些过程是以前认为涉及纤连蛋白的主要细胞迁移事件。阴性对照包括来自胶原结合区的另一种保守的纤连蛋白肽,其含有序列Cys-Gln-Asp-Ser-Glu-Thr-Arg-Thr-Phe-Tyr和另一种肽。我们的结果证明了使用针对细胞外蛋白识别位点的合成肽作为形态发生过程探针的可行性,并且它们为纤连蛋白参与原肠胚形成和神经嵴细胞迁移的假设提供了进一步的支持。
We describe a new method for analyzing embryonic events dependent on a specific peptide recognition signal. A short, specific amino acid sequence in fibronectin has been implicated as a recognition site in fibronectin-mediated interactions. Fibroblast adhesion to fibronectin is competitively inhibited by certain synthetic peptides, including the decapeptide Arg-Gly-Asp-Ser-Pro-Ala-Ser-Ser-Lys-Pro, which appears to contain the cell recognition sequence. We found that this peptide inhibited both amphibian gastrulation and avian neural crest cell migration in vivo, as well as the attachment and migration of neural crest cells in vitro. These processes are major cell migratory events previously suggested to involve fibronectin. Negative controls included another conserved fibronectin peptide from the collagen-binding region containing the sequence Cys-Gln-Asp-Ser-Glu-Thr-Arg-Thr-Phe-Tyr and another peptide. Our results demonstrate the feasibility of using synthetic peptides directed at recognition sites in extracellular proteins as probes of morphogenetic processes, and they provide further support for the hypothesis that fibronectin is involved in gastrulation and neural crest cell migration.