Kim K M, Adachi T, Nielsen P J, Terashima M, Lamers M C, Köhler G, Reth M
Max-Planck-Institut für Immunbiologie, Freiburg, Germany.
EMBO J. 1994 Aug 15;13(16):3793-800. doi: 10.1002/j.1460-2075.1994.tb06690.x.
The IgM and IgD classes of antigen receptor can perform different functions on B cells. However, so far no class-specific components communicating with the cytoplasm have been found in the two antigen receptors. We have employed a new biotinylation protocol to search for intracellular membrane Ig-associated proteins. Here we describe two proteins of 29 and 31 kDa that are associated with membrane IgD and to some extent with membrane IgM. The membrane IgM molecule is associated specifically with three proteins of 32, 37 and 41 kDa. The purification and sequencing of the two mIgD-associated proteins revealed that they are novel proteins which are related to each other. These proteins may be the missing link between the antigen receptor and the cytoskeleton and may contribute to functional differences between membrane IgM and membrane IgD.
抗原受体的IgM和IgD类别在B细胞上可执行不同功能。然而,迄今为止在这两种抗原受体中尚未发现与细胞质进行通讯的类别特异性成分。我们采用了一种新的生物素化方案来寻找细胞内膜免疫球蛋白(membrane Ig)相关蛋白。在此,我们描述了两种分别为29 kDa和31 kDa的蛋白,它们与膜IgD相关,并且在一定程度上与膜IgM相关。膜IgM分子特异性地与三种分别为32 kDa、37 kDa和41 kDa的蛋白相关。对这两种与膜IgD相关蛋白的纯化和测序表明,它们是彼此相关的新型蛋白。这些蛋白可能是抗原受体与细胞骨架之间缺失的环节,并且可能导致膜IgM和膜IgD之间的功能差异。