Dreskin S C
University of Colorado Health Science Center, Denver 80262.
J Immunol Methods. 1995 Feb 13;179(1):87-93. doi: 10.1016/0022-1759(94)00276-3.
Monoclonal antibodies have been used extensively to study the roles of specific extracellular proteins in cellular activation. Due to the large size of these molecules, their use for the study of receptor-mediated activation of intracellular processes has been limited. This report describes a method to introduce whole IgG antibody molecules into large functional membrane vesicles (ghosts) derived from rat basophilic leukemia (RBL) cells. Furthermore, an IgG1 mouse monoclonal antibody (JRK) directed against the cytoplasmic portion of the beta subunit of the high affinity receptor for IgE (Fc epsilon RI) can partially inhibit Fc epsilon RI-mediated PI hydrolysis through modest effects on both basal and receptor-mediated activation of phospholipase C.
单克隆抗体已被广泛用于研究特定细胞外蛋白在细胞激活中的作用。由于这些分子体积较大，它们在受体介导的细胞内过程激活研究中的应用受到了限制。本报告描述了一种将完整IgG抗体分子引入源自大鼠嗜碱性白血病（RBL）细胞的大型功能性膜囊泡（血影）的方法。此外，一种针对IgE高亲和力受体（FcεRI）β亚基细胞质部分的IgG1小鼠单克隆抗体（JRK），可以通过对磷脂酶C的基础激活和受体介导的激活产生适度影响，部分抑制FcεRI介导的磷脂酰肌醇水解。
