Chung J B, Baumeister M A, Monroe J G
Division of Rheumatology, Department of Medicine and Department of Pathology and Laboratory Medicine, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.
J Immunol. 2001 Jan 15;166(2):736-40. doi: 10.4049/jimmunol.166.2.736.
Glycosphingolipid-enriched domains (GEDs) are believed to act as platforms for transduction of B cell Ag receptor (BCR)-induced signals from the cell surface. We sought to study whether differential sequestration of BCR into GEDs may contribute to the described intrinsic signaling differences between mature and immature B cells. In this study we found that mature B cells copolarize the BCR with GEDs following BCR aggregation, whereas transitional immature B cells do not. Although anti-BCR treatment leads to receptor aggregation by immature stage B cells, the aggregated complexes do not colocalize with GEDs. We found this difference to be independent of the isotype of the receptor, thereby associating this difference in BCR-GED colocalization to the developmental stage of the B cell. These findings suggest a structural basis for the developmentally regulated differences observed in Ag receptor-mediated signal transduction.
富含糖鞘脂的结构域（GEDs）被认为是细胞表面B细胞抗原受体（BCR）诱导信号转导的平台。我们试图研究BCR在GEDs中的差异性隔离是否可能导致成熟和未成熟B细胞之间所述的内在信号差异。在本研究中，我们发现成熟B细胞在BCR聚集后会使BCR与GEDs共极化，而过渡性未成熟B细胞则不会。尽管抗BCR处理会导致未成熟阶段B细胞的受体聚集，但聚集的复合物并不与GEDs共定位。我们发现这种差异与受体的同种型无关，从而将BCR-GED共定位的这种差异与B细胞的发育阶段联系起来。这些发现为在抗原受体介导的信号转导中观察到的发育调控差异提供了结构基础。
