125I标记显示人补体成分Cl的亚基Clq、Clr和Cls构象变化

Johann Bauer, Guenter Valet
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引用次数: 11

摘要

用125I标记C1s、C1r前酶和C1s、C1r、C1q酶。125I标签在C1s的H链和l链之间的分布仅轻微依赖于C1s的激活状态,并且约为。90%的标签位于h链上。在Clr原酶分子中,50%的标签被纳入h链。当C1r活化为C1r时,C1r h链标记减少到10%,而l链标记增加到总标记的90%。在标记过程中,C1s、C1q或C1qs的存在降低了C1r的h链标记,尽管C1r仍以酶原形式存在。在Ca2+或EDTA培养基中,C1s或C1rs的存在增强了C1q对125I的摄取。这是出乎意料的,因为人们会预料到由于C1r和C1s的结合而导致C1q标签的减少,类似于C1rs复合物和C1s二聚体形成过程中C1s的h链标签的减少。结果表明,C1r和C1q在活化过程中经过它们的构象并形成C1配合物。
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Conformational changes of the subunits Clq, Clr and Cls of human complement component Cl demonstrated by 125I labeling

C1s and C1r proenzymes and enzymes (C1s, C1r) and C1q were labeled with 125I. The distribution of the 125I label between H- and L-chain of C1s was only slightly dependent on the state of activation of C1s, and approx. 90% of the label was found in the H-chain. In the Clr proenzyme molecules 50% of the label was incorporated into the H-chain. The C1r H-chain label was reduced to 10% on activation of C1r to C1r, while the L-chain label increased to 90% of the total label. The presence of either C1s, C1q or C1qs during labeling reduced the C1r H-chain label, although C1r remained in the proenzyme form. The presence of C1s or C1rs enhanced the 125I uptake of C1q in Ca2+ or EDTA medium. This was unexpected because one would have anticipated a diminution of the C1q label due to the apposition of C1r and C1s, similarly as it occurs during C1rs complex and C1s dimer formation for the H-chain label of C1s. The results show that C1r and C1q after their conformation during activation and C1 complex formation.

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