Article ID Journal Published Year Pages File Type
9266257 Immunology Letters 2005 11 Pages PDF
Abstract
The B cell antigen receptor (BCR) composed of the ligand-binding membrane IgM (mIgM) and the signaling component, Ig-α/β, is known to inducibly associate with membrane microdomains rich in cholesterol and sphingolipids, termed lipid rafts. In this study we tested whether the Ig-α/β portion of the BCR has targeting information that allows it to be localized in lipid rafts. In order to do this, we cross-linked the Ig-α/β on the cell surface of the variant B cell line, WEHI 303.1.5, a derivative of the immature murine B cell line WEHI 231 that lacks μ heavy chain and expresses the Ig-α/β on the cell surface by itself. Using two methods to isolate detergent-insoluble, lipid raft-like fractions, we found that Ig-α/β without accompanying mIgM was constitutively located in these raft-like fractions and that the amount was marginally increased after Ig-α/β cross-linking. These results suggest that the Ig-α/β portion of the BCR has the ability to be compartmentalized into raft-like membrane domains even when not associated with mIgM and perhaps this targeting information is normally regulated by the presence of the mIgM portion of the receptor.
Related Topics
Life Sciences Immunology and Microbiology Immunology
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