Lymphocyte alpha-actinin. Relationship to cell membrane and co-capping with surface receptors.
Lymphocyte alpha-actinin. Relationship to cell membrane and co-capping with surface receptors.
复制标题
DOI：
10.1083/jcb.84.2.305
复制
发表时间：
1980-02
期刊：
影响因子：
--
通讯作者：
Gabbiani G
中科院分区：
文献类型：
--
作者：
Hoessli D;Rungger-Brändle E;Jockusch BM;Gabbiani G
小鼠脾淋巴细胞在双向凝胶电泳中合成一种与骨骼肌α-肌动蛋白融合的蛋白质，并由针对骨骼肌α-肌动蛋白的抗体免疫沉淀。小鼠淋巴细胞α-肌动蛋白存在于膜组分中，并由针对这些纯化的膜的抗血清从淋巴细胞洗涤剂裂解物中免疫沉淀而来。该抗血清与固定完整的淋巴细胞孵育后，其抗α-肌动蛋白活性不被吸附。淋巴细胞α-肌动蛋白不与刀豆蛋白A结合，也不能被乳过氧化物酶催化的表面碘化。双重免疫荧光显示，α-肌动蛋白与重新分布的表面免疫球蛋白和Thy-1抗原同时沿细胞膜运动，并与这些受体的表面聚集体结合长达30分钟。我们的结果表明，淋巴细胞α-肌动蛋白，根据分子质量和与肌肉蛋白抗体的交叉反应定义，(A)与细胞膜有关，(B)不在细胞表面表达，(C)参与表面受体的运动。
Mouse spleen lymphocytes synthesize a protein which comigrates with skeletal muscle alpha-actinin on two-dimensional gel electrophoresis and is immunoprecipitated by an antibody directed against skeletal muscle alpha-actinin. Mouse lymphocyte alpha-actinin is present in membrane fractions, and is immunoprecipitated from lymphocyte detergent lysates by an antiserum made against these purified membranes. The anti- alpha-actinin activity of this antiserum is not adsorbed after incubation with fixed intact lymphocytes. Lymphocyte alpha-actinin does not bind concanavalin A and it is inaccessible to lactoperoxidase- catalyzed surface iodination. Double immunofluorescence shows that alpha-actinin moves concurrently along the cell membrane with redistributed surface immunoglobulins and Thy-1 antigen, and remains associated up to 30 min with surface aggregates of these receptors. Our results suggest that lymphocyte alpha-actinin, as defined by molecular weight and cross reactivity with the antibody against the muscle protein, (a) is associated with the cell membrane, (b) is not expressed at the cell surface, and (c) participates in the movement of surface receptors.