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首页> 美国卫生研究院文献>The Journal of Biological Chemistry >Insights into the Effects of Complement Factor H on the Assembly and Decay of the Alternative Pathway C3 Proconvertase and C3 Convertase
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Insights into the Effects of Complement Factor H on the Assembly and Decay of the Alternative Pathway C3 Proconvertase and C3 Convertase

机译：洞察补体因子H对另类途径C3转化酶和C3转化酶的组装和衰减的影响

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The activated fragment of C3 (C3b) and factor B form the C3 proconvertase (C3bB), which is cleaved by factor D to C3 convertase (C3bBb). Older studies (Conrad, D. H., Carlo, J. R., and Ruddy, S. (1978) J. Exp. Med. 147, 1792–1805; Pangburn, M. K., and Müller-Eberhard, H. J. (1978) Proc. Natl. Acad. Sci. U.S.A. 75, 2416–2420; Kazatchkine, M. D., Fearon, D. T., and Austen, K. F. (1979) J. Immunol. 122, 75–81) indicated that the complement alternative pathway regulator factor H (FH) competes with factor B for C3b binding; however, the capability of FH to prevent C3bB assembly has not been formally investigated. Moreover, in the few published studies FH did not favor C3bB dissociation. Whether FH may affect C3bBb formation from C3bB is unknown. We set up user-friendly assays based on combined microplate/Western blotting techniques that specifically detect either C3bB or C3bBb, with the aim of investigating the effect of FH on C3bB assembly and decay and C3bBb formation and decay. We document that FH does not affect C3bB assembly, indicating that FH does not efficiently compete with factor B for C3b binding. We also found that FH does not dissociate C3bB. FH showed a strong C3bBb decay-accelerating activity, as reported previously, and also exerted an apparent inhibitory effect on C3bBb formation. The latter effect was not fully attributable to a rapid FH-mediated dissociation of C3bBb complexes, because blocking decay with properdin and C3 nephritic factor did not restore C3bBb formation. FH almost completely prevented release of the smaller cleavage subunit of FB (Ba), without modifying the amount of C3bB complexes, suggesting that FH inhibits the conversion of C3bB to C3bBb. Thus, the inhibitory effect of FH on C3bBb formation is likely the sum of inhibition of C3bB conversion to C3bBb and of C3bBb decay acceleration. Further studies are required to confirm these findings in physiological cell-based settings.
机译：C3（C3b）和因子B的活化片段形成C3前转化酶（C3bB），其被因子D切割为C3转化酶（C3bBb）。较早的研究（Conrad，DH，Carlo，JR和Ruddy，S.（1978）J. Exp。Med。147，1792–1805; Pangburn，MK和Müller-Eberhard，HJ（1978）Proc。Natl。Acad。美国科学75，2416-2420; Kazatchkine，MD，Fearon，DT和Austen，KF（1979）J.Immunol.122，75-81）指出补体替代途径调节因子H（FH）与B竞争用于C3b结合；但是，尚未正式研究FH防止C3bB组装的能力。此外，在少数已发表的研究中，FH不赞成C3bB的解离。 FH是否会影响从C3bB形成C3bBb尚不清楚。我们基于微孔板/ Western印迹技术相结合的方法建立了用户友好的检测方法，可特异性检测C3bB或C3bBb，目的是研究FH对C3bB组装和衰减以及C3bBb形成和衰减的影响。我们记录FH不会影响C3bB大会，表明FH不能有效地与因子B竞争C3b绑定。我们还发现FH不会解离C3bB。如先前报道，FH显示出强大的C3bBb衰变加速活性，并且对C3bBb的形成也具有明显的抑制作用。后一种作用不能完全归因于FH介导的C3bBb复合物的快速解离，因为用备解素和C3肾病因子阻断衰变不能恢复C3bBb的形成。 FH几乎完全阻止了FB（Ba）较小切割亚基的释放，而没有改变C3bB复合物的量，这表明FH抑制了C3bB向C3bBb的转化。因此，FH对C3bBb形成的抑制作用可能是抑制C3bB转化为C3bBb和抑制C3bBb衰减的总和。需要进一步的研究以证实在基于生理细胞的环境中的这些发现。

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