Takemura R, Stenberg P E, Bainton D F, Werb Z
J Cell Biol. 1986 Jan;102(1):55-69. doi: 10.1083/jcb.102.1.55.
We have observed increases in assembled clathrin on the plasma membrane during "frustrated phagocytosis," the spreading of macrophages on immobilized immune complexes. Resident macrophages freshly harvested from the peritoneal cavity of mice and attached to bovine serum albumin (BSA)-anti-BSA-coated surfaces at 4 degrees C had almost no clathrin basketworks on their adherent plasma membrane (less than 0.01 coated patch/micron 2), as observed by immunofluorescence, immunoperoxidase, and platinum-carbon replica techniques, although abundant assembled clathrin was observed in the perinuclear Golgi region. When the cells were warmed to 37 degrees C they started to spread by 4 min and reached their maximum extent by 20 min. Spreading preceded clathrin assembly at the plasma membrane. Clathrin-coated patches were first observed on the adherent plasma membrane at 6 min. Between 12 and 20 min assembled clathrin coats appeared on both adherent and nonadherent plasma membranes with a concomitant decrease in identifiable clathrin in the perinuclear region. A new steady state emerged by 2 h, as perinuclear clathrin began to reappear. At 20 min at 37 degrees C the adherent plasma membranes of macrophages spreading on BSA alone had 0.9 coated patch/micron 2, whereas in cells spread on immune complex-coated surfaces, the clathrin patches increased, dependent on ligand concentration, to a maximum of 2.1 coated patches/micron 2. Because frustrated phagocytosis of immune complex-coated surfaces at 37 degrees C increased the area of adherent plasma membrane, the total area coated by clathrin basket-works increased 5-fold (28 micron 2/cell) as compared with cells plated on BSA alone (5.6 micron 2/cell) and 200-fold as compared with cells adhering to immune complexes at 4 degrees C. We then determined that macrophages cultured on BSA-coated coverslips for 24 h already have abundant surface clathrin. When immune complexes were formed by the addition of anti-BSA IgG to already spread macrophages cultured on BSA-coated coverslips for 24 h, clathrin assembled at the sites of ligand-receptor interaction even at 4 degrees C, before spreading, and a 2.6-fold increase in assembled clathrin was observed on the adherent plasma membrane of cells on immune complexes as compared with cells on BSA alone. Clathrin was reversibly redistributed to the Golgi region, returning to the steady state by 2 h.(ABSTRACT TRUNCATED AT 400 WORDS)
我们观察到,在“受挫吞噬作用”(即巨噬细胞在固定的免疫复合物上铺展)过程中,质膜上组装的网格蛋白增多。从小鼠腹腔新收获的驻留巨噬细胞,在4℃附着于牛血清白蛋白(BSA)-抗BSA包被的表面时,其黏附质膜上几乎没有网格蛋白篮状结构(每平方微米少于0.01个包被斑),通过免疫荧光、免疫过氧化物酶和铂-碳复型技术观察均是如此,尽管在核周高尔基体区域观察到大量组装的网格蛋白。当细胞升温至37℃时,它们在4分钟时开始铺展,并在20分钟时达到最大铺展程度。铺展先于质膜上的网格蛋白组装。在6分钟时首次在黏附质膜上观察到网格蛋白包被斑。在12至20分钟之间,组装的网格蛋白衣出现在黏附质膜和非黏附质膜上,同时核周区域中可识别的网格蛋白减少。2小时后出现新的稳态,此时核周网格蛋白开始重新出现。在37℃ 20分钟时,仅在BSA上铺展的巨噬细胞的黏附质膜有每平方微米0.9个包被斑,而在免疫复合物包被表面上铺展的细胞中,网格蛋白斑增多,取决于配体浓度,最多可达每平方微米2.1个包被斑。由于在37℃对免疫复合物包被表面的受挫吞噬作用增加了黏附质膜的面积,与仅接种在BSA上的细胞(每细胞5.6平方微米)相比,网格蛋白篮状结构包被的总面积增加了5倍(每细胞28平方微米),与在4℃黏附于免疫复合物的细胞相比增加了200倍。然后我们确定,在BSA包被的盖玻片上培养24小时的巨噬细胞已经有大量表面网格蛋白。当向在BSA包被的盖玻片上培养24小时且已经铺展的巨噬细胞中加入抗BSA IgG形成免疫复合物时,即使在4℃,在铺展之前,网格蛋白也会在配体-受体相互作用位点组装,与仅在BSA上的细胞相比,免疫复合物上细胞的黏附质膜上组装的网格蛋白增加了2.6倍。网格蛋白可逆地重新分布到高尔基体区域,2小时后恢复到稳态。(摘要截取自400字)