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首页> 外文期刊>Protoplasma: An International Journal of Cell Biology >ACIDIFICATION OF THE YOUNG PHAGOSOMES OF PARAMECIUM IS MEDIATED BY PROTON PUMPS DERIVED FROM THE ACIDOSOMES
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ACIDIFICATION OF THE YOUNG PHAGOSOMES OF PARAMECIUM IS MEDIATED BY PROTON PUMPS DERIVED FROM THE ACIDOSOMES

机译：RAM的年轻磷酸化的酸化是由酸化体质子泵介导的

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Although it is generally accepted that phagosome acidification is induced through the activity of a vacuolar proton pump (V-ATPase) present on the phagosome membrane, exactly how these pumps are delivered to the phagosomes is not well understood. To study this question in Paramecium, it was necessary to first show that an authentic V-ATPase was present on their phagosomal membranes. Three antibodies raised against V-ATPases or their subunits were each found to label one or two large digestive vacuoles (DVs) in Paramecium multimicronucleatum when immunofluorescence microscopy was used. Using horseradish peroxidase immunocytochemistry to increase sensitivity, about 10 DVs were shown to contain a V-ATPase. In high magnification images and cryoultramicrotomy these proton pumps were found to be located on the acidosomes, suggesting the vacuolar proton pumps on the DVs originate from the acidosomes. The authenticity of the V-ATPase was further confirmed by its sensitivity to cold temperature and to the V-ATPase specific inhibitor, concanamycin B, which at 10 nM doubled the tin for vacuole acidification. Thus, we conclude that (1) acidosomes and some DVs of Paramecium have a bona-fide concanamycin B-sensitive and cold-sensitive V-ATPase, (2) the V-ATPase is delivered to the young DVs during acidosome fusion, and (3) the V-ATPase is involved in vacuole acidification. Finally, we have now determined that Paramecium has two immunologically related V-ATPases that are involved in two very different functions, (1) the acidification of phagosomes and (2) fluid segregation in the contractile vacuole complexes. [References: 36]
机译：尽管通常公认吞噬体酸化是通过吞噬体膜上存在的液泡质子泵（V-ATPase）的活性诱导的，但对于如何将这些泵递送至吞噬体的确切方式尚不清楚。为了在草履虫中研究这个问题，有必要首先证明其吞噬体膜上存在真实的V-ATPase。当使用免疫荧光显微镜检查时，发现三种针对V-ATPase或其亚基的抗体均标记了草履虫微核中的一个或两个大消化液泡（DV）。使用辣根过氧化物酶免疫细胞化学增加敏感性，显示约10个DV含有V-ATPase。在高放大倍数图像和超薄切片术中，发现这些质子泵位于酸体上，这表明DV上的液泡质子泵来自酸体。 V-ATPase对低温和对V-ATPase特异性抑制剂刀豆霉素B的敏感性进一步证实了它的真实性，后者在10 nM时使液泡酸化的锡增加了一倍。因此，我们得出以下结论：（1）草履虫的酸体和某些DV具有真正的伴刀豆球蛋白B敏感和冷敏感的V-ATPase;（2）在酸体融合过程中，V-ATPase被递送至年轻的DV，并且（ 3）V-ATP酶参与液泡酸化。最终，我们现在确定草履虫具有两种与免疫学相关的V-ATPase，它们参与两种非常不同的功能：（1）吞噬体的酸化和（2）收缩液泡复合物中的液体分离。 [参考：36]

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