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* Infectious Diseases Section, Department of Veterans Affairs Western New York Healthcare System and State University of New York at Buffalo, Buffalo, New York;
Genetics Institute, Cambridge, Massachusetts;
Department of Veterans Affairs, White River Junction, Vermont; and
Department of Pharmacology and Toxicology, Dartmouth Medical School, Hanover, New Hampshire
Correspondence: Charles S. Berenson, Infectious Diseases Laboratory-151, Buffalo V.A. Medical Center, Buffalo, NY 14215. E-mail: berenson{at}acsu.buffalo.edu
Endotoxin-responsive (C3H/HeN) and -hyporesponsive (C3H/HeJ) murine B lymphocytes purified by adherence to anti-immunoglobulin ("antibody panning") possess identical gangliosides but different ganglioside surface accessibilities. We investigated the distribution and surface accessibility of gangliosides of B lymphocytes purified by adherence to plastic ("plastic panning") or by subtraction of non-B-lymphocyte components. As with antibody panning, there were no entirely new or absent gangliosides in plastic-panned or subtraction-purified B lymphocytes of each strain. However, striking changes in relative expression of five gangliosides were detected with each purification protocol. Moreover, five gangliosides of antibody-panned and plastic-panned B lymphocytes but only two gangliosides of subtraction-purified B lymphocytes were inaccessible to surface labeling. Unlike the situation for antibody-panned B lymphocytes, no interstrain (HeN vs. HeJ) surface accessibility differences existed in gangliosides of plastic-panned or subtraction-purified cells. Exposure of subtraction-purified B lymphocytes to anti-immunoglobulin failed to elicit changes in ganglioside expression. Murine B lymphocytes have distinct protocol-dependent differences in glycolipid phenotype which likely denote individual subpopulations.
Key Words: glycosphingolipids surface accessibility immune cells thin-layer chromatography
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