Lucy J A
Ciba Found Symp. 1984;103:28-44. doi: 10.1002/9780470720844.ch3.
Recent work is described on the fusion of human erythrocytes induced by chlorpromazine, which is accompanied by the endogenous proteolysis of integral and skeletal membrane proteins. This fusion reaction is of interest because it occurs at a high incidence in the presence of EGTA. It thus contrasts with the emphasis that has been placed on the role of Ca2+ in the fusion of lipid bilayers as a model for its behaviour in biomembrane fusion reactions. A survey of fusion in cells induced by chemicals and by Sendai virus, and of fusion in liposomes, in fact reveals numerous reported instances of fusion occurring in the absence of Ca2+. The finding that endogenous proteolysis of erythrocyte membrane proteins accompanies cell fusion induced by chlorpromazine leads to the suggestion that the products of proteolysis may in some cases be fusogenic, and that their formation may provide a general mechanism for the fusion of lipid bilayers in biomembrane fusion reactions, aspects of which are imitated by the fusogenic viruses.
本文描述了近期关于氯丙嗪诱导人红细胞融合的研究工作,该过程伴随着整合膜蛋白和骨架膜蛋白的内源性蛋白水解。这种融合反应备受关注,因为在乙二醇双四乙酸(EGTA)存在的情况下,其发生率很高。因此,这与一直以来强调Ca2+在脂质双层融合中作为生物膜融合反应行为模型的作用形成了对比。事实上,对化学物质和仙台病毒诱导的细胞融合以及脂质体融合的研究表明,有大量报道称融合反应在无Ca2+的情况下发生。氯丙嗪诱导红细胞融合时伴随红细胞膜蛋白的内源性蛋白水解这一发现表明,蛋白水解产物在某些情况下可能具有融合活性,其形成可能为生物膜融合反应中脂质双层的融合提供一种普遍机制,而融合病毒在一定程度上模仿了其中的某些方面。