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Biologically active synthetic fragments of epidermal growth factor: localization of a major receptor-binding region.

机译:表皮生长因子的生物活性合成片段:主要受体结合区的定位。

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摘要

A primary receptor-binding region of mouse epidermal growth factor (EGF) was identified by comparing the relative affinities of selected synthetic fragments with overlapping sequences in the EGF receptor-binding assay, using human foreskin fibroblasts. Only synthetic peptides containing the amino acid residues 20-31 in the mouse EGF sequence showed the ability to compete with 125I-labeled EGF in binding to EGF receptors. The affinities of the cyclic EGF fragment [Ala20]EGF-(14-31) and the linear [(S-acetamidomethyl)-Cys20,31]-EGF-(20-31) were approximately 1/10(4) of the affinity of EGF. Despite their reduced receptor affinities, these two peptides exhibited the in vitro biological activities of native EGF, while fragments from other regions of the EGF molecule were devoid of these biological properties. The peptides induced DNA synthesis in human foreskin fibroblasts as measured by [3H]thymidine incorporation into DNA. They also induced EGF receptor clustering and activated the EGF-sensitive kinase, enhancing the autophosphorylation of EGF receptors in a dose-related manner. Moreover, a major antigenic determinant of EGF for rabbit anti-EGF antibodies was identified within this same localized region of the EGF molecule by competition experiments utilizing the synthetic EGF fragments. The predominant EGF antigenic determinant(s) was also found within the fragment [(S-acetamidomethyl)Cys20,31]-EGF-(20-31). The accessibility of the residues in positions 20-31 for antibody recognition is consistent with the conclusion that these residues constitute or contain a major receptor-binding region for EGF.
机译:使用人包皮成纤维细胞,通过在EGF受体结合试验中比较所选合成片段与重叠序列的相对亲和力,从而确定了小鼠表皮生长因子(EGF)的主要受体结合区。只有在小鼠EGF序列中含有氨基酸残基20-31的合成肽才具有与125I标记的EGF竞争结合EGF受体的能力。环状EGF片段[Ala20] EGF-(14-31)和线性[(S-乙酰氨基甲基)-Cys20,31] -EGF-(20-31)的亲和力约为亲和力的1/10(4) EGF。尽管它们的受体亲和力降低,但这两种肽仍表现出天然EGF的体外生物学活性,而来自EGF分子其他区域的片段却缺乏这些生物学特性。通过将[3H]胸苷掺入DNA,可测定该肽在人包皮成纤维细胞中诱导DNA合成。他们还诱导了EGF受体聚集并激活了EGF敏感激酶,以剂量相关的方式增强了EGF受体的自磷酸化。此外,通过利用合成的EGF片段的竞争实验,在EGF分子的该相同局部区域内鉴定了EGF对于兔抗EGF抗体的主要抗原决定簇。在片段[(S-乙酰氨基甲基)Cys20,31] -EGF-(20-31)中也发现了主要的EGF抗原决定簇。 20-31位残基可用于抗体识别的结论与这些残基构成或包含EGF的主要受体结合区的结论是一致的。

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