IDENTITY OF P36K PHOSPHORYLATED UPON ROUS-SARCOMA VIRUS TRANSFORMATION WITH A PROTEIN PURIFIED FROM BRUSH-BORDERS - CALCIUM-DEPENDENT BINDING TO NON-ERYTHROID SPECTRIN AND F-ACTIN
IDENTITY OF P36K PHOSPHORYLATED UPON ROUS-SARCOMA VIRUS TRANSFORMATION WITH A PROTEIN PURIFIED FROM BRUSH-BORDERS - CALCIUM-DEPENDENT BINDING TO NON-ERYTHROID SPECTRIN AND F-ACTIN
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DOI：
10.1002/j.1460-2075.1984.tb01789.x
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发表时间：
1984-01-01
期刊：
影响因子：
11.4
通讯作者：
WEBER, K
中科院分区：
文献类型：
--
作者：
GERKE, V;WEBER, K
源自猪肠上皮细胞顶端侧的膜囊泡在存在 Ca 的情况下脱膜后保留了 2 种主要蛋白质（I、II），这些蛋白质通过添加 Ca 螯合剂而释放。对这 2 种 Ca 结合蛋白进行了纯化和表征。蛋白质 I 的分子量为 85,000，包含 2 个 36-K [千道尔顿] 亚基副本和一个额外的 10-K 亚基。它以 Ca 依赖性方式与 F-肌动蛋白以及非红系血影蛋白结合。免疫荧光显微镜揭示了肠细胞末端网和各种组织培养细胞的膜下皮质层中存在与蛋白 I 相关的抗原。生化和免疫学结果证明，蛋白 I 的 36-K 亚基与细胞 p36K 相同，细胞 p36K 被认为是劳斯肉瘤病毒转化细胞中 sarc 基因激酶酪氨酸磷酸化的主要底物。蛋白质 I 的生化特性与其在免疫荧光显微镜和细胞分级分离中看到的位置一致，表明皮质层中的肌动蛋白-血影蛋白网络可能受到病毒转化的影响。
Membrane vesicles derived from the apical side of porcine intestinal epithelial cells retain, after demembranation in the presence of Ca, 2 major proteins, (I, II) which are released by the addition of Ca chelators. These 2 Ca-binding proteins were purified and characterized. Protein I has a MW of 85,000 and contains 2 copies of a 36-K [kilodalton] subunit and an additional 10-K subunit. It binds in a Ca-dependent manner to F-actin as well as to non-erythroid spectrin. Immunofluorescence microscopy reveals protein I-related antigens in the terminal web of the intestinal cell and in a submembraneous cortical layer in various tissue culture cells. Biochemical and immunological results document that the 36-K subunit of protein I is identical with the cellular p36K recognized as a major substrate for tyrosine phosphorylation by the sarc gene kinase in Rous sarcoma virus-transformed cells. The biochemical properties of protein I agree with its location seen in immunofluorescence microscopy and cell fractionation and suggest that the actin-spectrin network in the cortical layer may be affected by virus transformation.