Perez H D, Goldstein I M
J Rheumatol Suppl. 1987 Jun;14 Suppl 13:53-8.
Studies completed thus far indicate that normal human serum contains a specific anionic polypeptide (cochemotaxin) that permits low concentrations of C5a desarg to exhibit chemotactic activity for human polymorphonuclear leukocytes. Under conditions of limited complement activation in vivo, the cochemotaxin may play an important physiologic role by amplifying the chemotactic activity of C5a desarg. The "complex" of C5a desarg plus cochemotaxin probably accounts for most of the chemotactic activity that is generated in human serum after complement activation and also appears to be the target of the heat stable cationic protein inhibitor (Bb fragment of Factor B) that is present in serum from some patients with active systemic lupus erythematosus.
迄今为止完成的研究表明,正常人血清含有一种特定的阴离子多肽(协同趋化因子),它能使低浓度的C5a去精氨酸对人多形核白细胞表现出趋化活性。在体内补体激活受限的情况下,协同趋化因子可能通过放大C5a去精氨酸的趋化活性发挥重要的生理作用。C5a去精氨酸与协同趋化因子的“复合物”可能是补体激活后人血清中产生的大部分趋化活性的原因,并且似乎也是一些活动性系统性红斑狼疮患者血清中存在的热稳定阳离子蛋白抑制剂(B因子的Bb片段)的作用靶点。