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Polarized expression of immunoglobulin, spectrin, and protein kinase C beta II occurs in B cells from normal BALB/c, autoimmune lpr , and anti‐ssDNA transgenic, tolerant mice
Author(s) -
MassoWelch Patricia A.,
Black Jennifer D.,
Erikson Jan,
Repasky Elizabeth A.
Publication year - 1999
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.66.4.617
Subject(s) - biology , balb/c , microbiology and biotechnology , transgene , antibody , genetically modified mouse , immunoglobulin g , beta (programming language) , protein kinase a , kinase , gene , immune system , immunology , biochemistry , computer science , programming language
The rapid redistribution of B cell surface immunoglobulin to a cap upon cross‐linking treatment is a well‐described phenomenon, the physiological significance of which is unknown. We describe the observation that splenic B cells from unimmunized normal, autoimmune, and tolerant mice express naturally occurring capped immunoglobulin in the absence of exogenous stimulation. The percentage of capped B cells increases to 20% of B cells by age 16 weeks in the progressive autoimmune lpr mouse. Transgenic, tolerant mice expressing lpr‐derived genes for ssDNA‐binding antibody also demonstrate a large percentage (35–75%) of immunoglobulin‐capped splenic B cells. In these capped B cells, protein kinase C beta II, the cytoskeletal proteins spectrin and ankyrin, and the lipophilic probe diI are enriched beneath the site of the immunoglobulin cap. These data suggest that polarization of surface receptors, signaling molecules, anionic phospholipid domains, and cytoskeletal proteins may be an important part of the B cell immune response in vivo. J. Leukoc. Biol. 66: 617–624; 1999.