Taya M, Rabinovich E, Haimovich J
Department of Human Microbiology, Sackler Faculty of Medicine, Tel-Aviv University, Israel.
Immunol Lett. 1992 Jul;33(2):173-7. doi: 10.1016/0165-2478(92)90044-o.
Characterization of a membrane-IgM-negative variant cell line derived from the murine B-cell line 38C-13 revealed the absence of light chains and the presence of polypeptides with an apparent molecular size of 18 kDa and 14 kDa, previously denoted omega and iota and characteristic of pre-B cells. These polypeptides assemble with the mu chains into complexes with apparent molecular sizes of about 100 kDa and 200 kDa. It has been previously shown that light-chain-deficient variants of the 38C cell line undergo 'secondary' light chain rearrangements. It is suggested, therefore, that complexes of mu and the 'surrogate' light chains omega and iota play a role in this process. As these complexes do not reach the cell surface we would like to propose that the mechanism of secondary rearrangement is intracellularly controlled.
对源自小鼠B细胞系38C - 13的膜IgM阴性变异细胞系的特性分析显示，该细胞系缺乏轻链，存在表观分子大小为18 kDa和14 kDa的多肽，此前分别称为ω和ι，是前B细胞的特征。这些多肽与μ链组装成表观分子大小约为100 kDa和200 kDa的复合物。此前已表明，38C细胞系的轻链缺陷变异体经历“二次”轻链重排。因此，有人提出，μ链与“替代”轻链ω和ι的复合物在这一过程中发挥作用。由于这些复合物未到达细胞表面，我们推测二次重排的机制是由细胞内控制的。
