Brix K, Reinecke A, Stockem W
Institute of Cytology, University of Bonn, Federal Republic of Germany.
Eur J Cell Biol. 1990 Apr;51(2):279-84.
Affinity-purified antibodies against actin, myosin, alpha-actinin and vinculin cross-reacted with corresponding proteins from Amoeba proteus in immunoblotting experiments. Antibody staining of cells fixed during locomotion revealed different distribution patterns with a local concentration of anti-actin in the intermediate and of anti-myosin in the uroid region. Anti-alpha-actinin labeled a thin layer at the internal face of the plasma membrane, whereas anti-vinculin was distinctly concentrated at the base of advancing pseudopodia. Microinjection of different control solutions or antibodies against actin, myosin and alpha-actinin neither influenced the normal morphology and motile activity of amoebae nor changed the cellular distribution pattern of complementary antigens. However, antibodies against vinculin disorganized controlled locomotion and altered the spatial morphology of the microfilament system as well as the localization of the vinculin antigen thus pointing to a function of this protein in adhesion and locomotion of A. proteus. The results of the present paper show similarities to observations on mammalian tissue culture cells.
在免疫印迹实验中，针对肌动蛋白、肌球蛋白、α-辅肌动蛋白和纽蛋白的亲和纯化抗体与变形虫中的相应蛋白质发生交叉反应。对运动过程中固定的细胞进行抗体染色，结果显示出不同的分布模式，肌动蛋白抗体在中间区域局部聚集，肌球蛋白抗体在尾状区局部聚集。抗α-辅肌动蛋白标记了质膜内表面的一层薄层，而抗纽蛋白则明显集中在前进伪足的基部。显微注射不同的对照溶液或针对肌动蛋白、肌球蛋白和α-辅肌动蛋白的抗体，既不影响变形虫的正常形态和运动活性，也不改变互补抗原的细胞分布模式。然而，抗纽蛋白抗体扰乱了受控运动，改变了微丝系统的空间形态以及纽蛋白抗原的定位，从而表明该蛋白在变形虫的黏附和运动中发挥作用。本文的结果与对哺乳动物组织培养细胞的观察结果相似。
