Dousset B, Straczek J, Maachi F, Nguyen D L, Jacob C, Capiaumont J, Nabet P, Belleville F
Laboratory of Biochemistry, Nancy Medical School, Henri Poincaré-Nancy I University, Vandoeuvre, France.
Biochem Biophys Res Commun. 1998 Jun 29;247(3):587-91. doi: 10.1006/bbrc.1998.8834.
The human plasma contains small peptide molecules known as low molecular weight growth factors synergistically increasing certain biological actions of insulin-like growth factors. In the present work we isolated and characterized a hexapeptide with HWESAS as structure. This purified peptide was absolutely necessary for the sulfation activity of insulin-like growth factor-I on chick embryo pelvic cartilages and improved the mitogenic activity of both insulin-like growth factors. The effects of this hexapeptide were confirmed by using the homologous synthetic peptide, that exhibited similar biological effects. Other synthetic peptides with structure derived from hexapeptide were shown to be active: the pentapeptide HWESA appeared more potent than the tripeptide HWE, which is about 170 to 200 times less active than the hexapeptide. The sequence of hexapeptide HWESAS is identified in only one human protein that is C3f, a fragment of C3 complement.
人血浆中含有被称为低分子量生长因子的小肽分子，这些因子能协同增强胰岛素样生长因子的某些生物学作用。在本研究中，我们分离并鉴定了一种结构为HWESAS的六肽。这种纯化的肽对于胰岛素样生长因子-I对鸡胚骨盆软骨的硫酸化活性是绝对必要的，并且提高了两种胰岛素样生长因子的促有丝分裂活性。使用同源合成肽证实了这种六肽的作用，该合成肽表现出相似的生物学效应。其他具有源自六肽结构的合成肽也显示出活性：五肽HWESA似乎比三肽HWE更有效，三肽HWE的活性比六肽低约170至200倍。六肽HWESAS的序列仅在一种人类蛋白质即C3补体的片段C3f中被鉴定出来。
