Chang L Y, Slot J W, Geuze H J, Crapo J D
Department of Medicine, Duke University, Durham, North Carolina 27710.
J Cell Biol. 1988 Dec;107(6 Pt 1):2169-79. doi: 10.1083/jcb.107.6.2169.
The distribution of CuZn superoxide dismutase (SOD) molecules in subcellular organelles in rat liver hepatocytes was studied using integrated biochemical, stereological, and quantitative immunocytochemical techniques. A known concentration of purified CuZn SOD in 10% gelatin was embedded alongside the liver tissue for the calculation of CuZn SOD concentrations in hepatocyte organelles and total CuZn SOD in the rat liver. Most of the CuZn SOD was located in the cytoplasmic matrix (73.1%) and in the nucleus (11.9%) with concentrations of 1.36 and 0.71 mg/cm3, respectively. Lysosomes contained the highest concentration (5.81 mg/cm3). Only low concentrations were measured in mitochondria (0.21 mg/cm3). Membrane-bound spaces of rough endoplasmic reticulum (ER), smooth ER, and the Golgi system did not contain significant concentrations of the enzyme. By adding up the concentrations in all subcellular compartments, a total liver content of CuZn SOD was established from the immunocytochemical measurements (0.386 +/- 0.028 mg/gm liver) that agreed closely with those obtained by biochemical assays (0.380 +/- 0.058 mg/gm liver). The average distances between two CuZn SOD molecules can be calculated from enzyme concentrations. It was determined that CuZn SOD molecules in the cytoplasmic matrix and nucleus were 34 and 42 nm apart, respectively. In peroxisomes and mitochondria, average intermolecular distance increased to approximately 60 nm and increased to 136 nm in smooth ER. CuZn SOD is a relatively abundant protein in the cytosol of hepatocytes and its distribution overlaps with major sites of O2- production. The efficiency of protection CuZn SOD can provide to cytosolic proteins from attacks by superoxide anion depends on the rate of O2- production, distribution of CuZn SOD relative to cytosolic proteins, and the relative reaction rates between O2- with both cytosolic proteins and CuZn SOD. Future studies of these substrate-enzyme relationships in vivo can lead to a greater understanding of how cells handle oxidant stress.
运用综合生化、体视学和定量免疫细胞化学技术,研究了大鼠肝脏肝细胞亚细胞器中铜锌超氧化物歧化酶(SOD)分子的分布。将已知浓度的纯化铜锌SOD溶于10%明胶中,与肝组织一同包埋,用于计算肝细胞细胞器中铜锌SOD的浓度以及大鼠肝脏中总铜锌SOD的含量。大部分铜锌SOD位于细胞质基质(73.1%)和细胞核(11.9%)中,浓度分别为1.36和0.71mg/cm³。溶酶体中铜锌SOD浓度最高(5.81mg/cm³)。线粒体中仅检测到低浓度(0.21mg/cm³)。粗面内质网(ER)、滑面内质网和高尔基体系统的膜结合空间中该酶浓度不高。通过将所有亚细胞区室中的浓度相加,从免疫细胞化学测量中得出肝脏中铜锌SOD的总含量为(0.386±0.028mg/g肝脏),这与生化分析所得结果(0.380±0.058mg/g肝脏)非常接近。可根据酶浓度计算两个铜锌SOD分子之间的平均距离。经测定,细胞质基质和细胞核中铜锌SOD分子的间距分别为34和42nm。在过氧化物酶体和线粒体中,分子间平均距离增加到约60nm,在滑面内质网中则增加到136nm。铜锌SOD是肝细胞胞质溶胶中相对丰富的蛋白质,其分布与超氧阴离子产生的主要部位重叠。铜锌SOD为胞质溶胶蛋白抵御超氧阴离子攻击提供保护的效率,取决于超氧阴离子的产生速率、铜锌SOD相对于胞质溶胶蛋白的分布,以及超氧阴离子与胞质溶胶蛋白和铜锌SOD之间的相对反应速率。未来对体内这些底物 - 酶关系的研究,可能会使人们更深入地了解细胞如何应对氧化应激。