THE ROLE OF SERUM COMPLEMENT IN CHEMOTAXIS OF LEUKOCYTES IN VITRO
THE ROLE OF SERUM COMPLEMENT IN CHEMOTAXIS OF LEUKOCYTES IN VITRO
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血清补体在体外白细胞趋化作用中的作用
DOI：
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发表时间：
1965
影响因子：
15.3
通讯作者：
H. Müller
中科院分区：
文献类型：
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作者：
P. Ward;C. Cochrane;H. Müller
本文用含有两个隔室和一个插入的过滤器的小室，研究了多种固定血清补体（C '）的试剂对多形核白细胞（PMN's）的体外趋化性。抗原-抗体复合物、酵母聚糖和聚集的人丙种球蛋白，在新鲜兔、豚鼠或小鼠血清存在下，导致中性粒细胞迁移通过滤纸。胃蛋白酶降解的兔抗体或含有抗体的未改变的鸭血清在添加抗原后不表现出这种活性。在治疗前加热血清或EDTA的存在防止了趋化因子的产生。在C '基因缺陷兔的全血清中不能产生趋化因子。然而，该兔血清中的缺陷可以通过添加兔或人C '6来纠正。B_（10）·D_2小鼠溶血性C ′缺陷血清的趋化活性也较低。豚鼠C'的前四个反应组分的相互作用不导致显著的趋化活性，除非还存在具有热不稳定组分的豚鼠优球蛋白。在兔血清中，C '5和C' 6，当通过与前四种反应组分的相互作用而被“激活”时，表现出类似于蛋白质-蛋白质复合物的行为，并表现出显著的趋化活性。通过采用有利于复合物解离的条件，分离出各个组分，并显示出无化学活性。然而，在两种成分重组后，活性再次出现。使用另一种方法，完整地分离C '5-C' 6复合物，并且显示出具有化学活性，而不含这些组分的其它级分没有活性。推测C '5-C' 6复合物是加入C '-固定剂后在血清中产生的活性趋化因子。
By the use of chambers containing two compartments with an interposed micropore filter, chemotaxis of polymorphonuclear leukocytes (PMN's) in vitro was studied employing various agents that fixed serum complement (C'). Antigen-antibody complexes, zymosan, and aggregated human gamma globulin, in the presence of fresh rabbit, guinea pig, or mouse serum resulted in the migration of PMN's through the micropore filter. Pepsin-degraded rabbit antibody or unaltered duck serum containing antibody did not exhibit such activity after addition of antigen. Heating of the serum before treatment or the presence of EDTA prevented the generation of the chemotactic factor. The chemotactic factor could not be generated in whole serum from rabbits genetically deficient in C'. However, the defect in this rabbit serum could be corrected by addition of rabbit or human C'6. Serum of B10·D2 mice deficient in hemolytic C' also yielded poor chemotactic activity. Interaction of the first four reacting components of guinea pig C' did not result in significant chemotactic activity unless guinea pig euglobulin with heat labile components was also present. In rabbit serum, C'5 and C'6, when "activated" by interaction with the first four reacting components, behaved like a protein-protein complex and exhibited marked chemotactic activity. By employing conditions favoring dissociation of the complex, the individual components were isolated and shown to be chemotactically inactive. Upon recombination of the two components, however, activity reappeared. Using another approach, the C'5–C'6 complex was isolated intact, and shown to be chemotactically active while other fractions not containing these components were not active. It is postulated that the C'5–C'6 complex is the active chemotactic factor generated in serum after the addition of C'-fixing agents.