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人类中性粒细胞中休眠的NADPH氧化酶和细胞色素b559的双颗粒定位

Dual granule localization of the dormant NADPH oxidase and cytochrome b559 in human neutrophils.

作者信息

Bjerrum O W, Borregaard N

机构信息

Department of Internal Medicine and Haematology C, University of Copenhagen, Gentofte Hospital, Hellerup, Denmark.

出版信息

Eur J Haematol. 1989 Jul;43(1):67-77. doi: 10.1111/j.1600-0609.1989.tb01254.x.

DOI:10.1111/j.1600-0609.1989.tb01254.x
PMID:2548892
Abstract

The subcellular localization of the microbicidal nicotinamide adenine dinucleotide phosphate (NADPH) oxidase and associated b-cytochrome was investigated in human neutrophils. In unperturbed neutrophils 85% of b-cytochrome and the major part of membrane-bound components of the NADPH oxidase co-sedimented with markers for specific granules and gelatinase. Using cytochrome b559 as a marker for membrane-bound components of the NADPH oxidase in quantitative studies we observed that, of the remaining 15%, the vast majority co-sedimented with latent alkaline phosphatase, a marker for a newly identified mobilizable intracellular compartment. Only a small fraction co-localized with the plasma membranes. Azurophil granules contained a protease activity which rapidly inactivated the NADPH oxidase components present in other membranes. Stimulation of the neutrophils with formyl-methionyl-leucyl-phenyl-alanine and leukotriene B4 which caused minimal degranulation of specific granules, resulted in translocation of b-cytochrome to the plasma membrane, concomitant with incorporation of alkaline phosphatase into the plasma membrane.

摘要

在人类中性粒细胞中研究了杀菌性烟酰胺腺嘌呤二核苷酸磷酸(NADPH)氧化酶及相关b型细胞色素的亚细胞定位。在未受干扰的中性粒细胞中,85%的b型细胞色素以及NADPH氧化酶的大部分膜结合成分与特异性颗粒和明胶酶的标志物共同沉降。在定量研究中,使用细胞色素b559作为NADPH氧化酶膜结合成分的标志物,我们观察到,在其余的15%中,绝大多数与潜在碱性磷酸酶共同沉降,潜在碱性磷酸酶是新发现的可动员细胞内区室的标志物。只有一小部分与质膜共定位。嗜天青颗粒含有一种蛋白酶活性,可迅速使存在于其他膜中的NADPH氧化酶成分失活。用甲酰甲硫氨酰亮氨酰苯丙氨酸和白三烯B4刺激中性粒细胞,导致特异性颗粒的脱颗粒最少,但会导致b型细胞色素转位到质膜,同时碱性磷酸酶掺入质膜。

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