Perez H D, Chenoweth D E, Goldstein I M
J Clin Invest. 1986 Dec;78(6):1589-95. doi: 10.1172/JCI112751.
The chemotactic activity of human C5a des Arg is enhanced significantly by an anionic polypeptide (cochemotaxin) in normal human serum and plasma. We have found that the cochemotaxin attaches to the oligosaccharide chain of native C5a des Arg to form a complex with potent chemotactic activity for human polymorphonuclear leukocytes. Although capable of enhancing the chemotactic activity of native C5a des Arg, the cochemotaxin had no effect on the chemotactic activity of either deglycosylated C5a des Arg, native C5a, or N-formyl-methionyl-leucyl-phenylalanine. Of the known components of the oligosaccharide chain, only sialic acid prevented enhancement by the cochemotaxin of the chemotactic activity exhibited by native C5a des Arg. Sialic acid also prevented the formation of C5a des Arg-cochemotaxin complexes, detected by acid polyacrylamide gel electrophoresis, molecular sieve chromatography on polyacrylamide gels, and sucrose density gradient ultracentrifugation.
人C5a去精氨酸在正常人血清和血浆中，其趋化活性会被一种阴离子多肽（共趋化因子）显著增强。我们发现，该共趋化因子附着于天然C5a去精氨酸的寡糖链上，形成一种对人多形核白细胞具有强大趋化活性的复合物。尽管共趋化因子能够增强天然C5a去精氨酸的趋化活性，但它对去糖基化的C5a去精氨酸、天然C5a或N-甲酰甲硫氨酰-亮氨酰-苯丙氨酸的趋化活性均无影响。在寡糖链的已知成分中，只有唾液酸可阻止共趋化因子增强天然C5a去精氨酸所表现出的趋化活性。唾液酸还能阻止通过酸性聚丙烯酰胺凝胶电泳、聚丙烯酰胺凝胶分子筛色谱法以及蔗糖密度梯度超速离心法检测到的C5a去精氨酸-共趋化因子复合物的形成。
