Zimmerli S, Majeed M, Gustavsson M, Stendahl O, Sanan D A, Ernst J D
Division of Infectious Diseases, San Francisco General Hospital, University of California at San Francisco 94143-0868, USA.
J Cell Biol. 1996 Jan;132(1-2):49-61. doi: 10.1083/jcb.132.1.49.
Phagosome-lysosome membrane fusion is a highly regulated event that is essential for intracellular killing of microorganisms. Functionally, it represents a form of polarized regulated secretion, which is classically dependent on increases in intracellular ionized calcium ([Ca2+]i). Indeed, increases in [Ca2+]i are essential for phagosome-granule (lysosome) fusion in neutrophils and for lysosomal fusion events that mediate host cell invasion by Trypanosoma cruzi trypomastigotes. Since several intracellular pathogens survive in macrophage phagosomes that do not fuse with lysosomes, we examined the regulation of phagosome-lysosome fusion in macrophages. Macrophages (M phi) were treated with 12.5 microM bis-(2-amino-S-methylphenoxy) ethane-N,N,N',N',-tetraacetic acid tetraacetoxymethyl ester (MAPT/AM), a cell-permeant calcium chelator which reduced resting cytoplasmic [Ca2+]; from 80 nM to < or = 20 nM and completely blocked increases in [Ca2+]i in response to multiple stimuli, even in the presence of extracellular calcium. Subsequently, M phi phagocytosed serum-opsonized zymosan, staphylococci, or Mycobacterium bovis. Microbes were enumerated by 4',6-diamidino-2-phenylindole, dihydrochloride (DAPI) staining, and phagosome-lysosome fusion was scored using both lysosome-associated membrane protein (LAMP-1) as a membrane marker and rhodamine dextran as a content marker for lysosomes. Confirmation of phagosome-lysosome fusion by electron microscopy validated the fluorescence microscopy findings. We found that phagosome-lysosome fusion in M phi occurs noramlly at very low [Ca2+]i (< or = 20 nM). Kinetic analysis showed that in M phi none of the steps leading from particle binding to eventual phagosome-lysosome fusion are regulated by [Ca2+]i in a rate-limiting way. Furthermore, confocal microscopy revealed no difference in the intensity of LAMP-1 immunofluorescence in phagolysosome membranes in calcium-buffered vs. control macrophages. We conclude that neither membrane recognition nor fusion events in the phagosomal pathway in macrophages are dependent on or regulated by calcium.
吞噬体-溶酶体膜融合是一个受到高度调控的过程,对于细胞内杀灭微生物至关重要。从功能上讲,它代表了一种极化调控分泌形式,传统上依赖于细胞内游离钙离子([Ca2+]i)浓度的升高。实际上,[Ca2+]i浓度的升高对于中性粒细胞中的吞噬体-颗粒(溶酶体)融合以及介导克氏锥虫锥鞭毛体入侵宿主细胞的溶酶体融合事件至关重要。由于几种细胞内病原体在不与溶酶体融合的巨噬细胞吞噬体中存活,我们研究了巨噬细胞中吞噬体-溶酶体融合的调控。用12.5微摩尔双-(2-氨基-5-甲基苯氧基)乙烷-N,N,N',N'-四乙酸四乙酰甲酯(MAPT/AM)处理巨噬细胞(M phi),这是一种可穿透细胞的钙螯合剂,可将静息细胞质[Ca2+]从80纳摩尔降低至≤20纳摩尔,并完全阻断对多种刺激的[Ca2+]i升高,即使在存在细胞外钙的情况下也是如此。随后,M phi吞噬血清调理的酵母聚糖、葡萄球菌或牛分枝杆菌。通过4',6-二脒基-2-苯基吲哚二盐酸盐(DAPI)染色对微生物进行计数,并使用溶酶体相关膜蛋白(LAMP-1)作为膜标记物以及罗丹明葡聚糖作为溶酶体的内容物标记物对吞噬体-溶酶体融合进行评分。通过电子显微镜对吞噬体-溶酶体融合的确认验证了荧光显微镜检查结果。我们发现M phi中的吞噬体-溶酶体融合在非常低的[Ca2+]i(≤20纳摩尔)时正常发生。动力学分析表明,在M phi中,从颗粒结合到最终吞噬体-溶酶体融合的所有步骤均不受[Ca2+]i以限速方式调控。此外,共聚焦显微镜检查显示,在钙缓冲的巨噬细胞与对照巨噬细胞中,吞噬溶酶体膜中LAMP-1免疫荧光强度没有差异。我们得出结论,巨噬细胞吞噬体途径中的膜识别和融合事件均不依赖于钙,也不受钙的调控。