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From the Section on Chemical Immunology, Arthritis and Rheumatism Branch, National Institute of Arthritis, Metabolism and Digestive Diseases, and the Ultrastructural Pathology Section, Laboratory of Pathology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20014
Abstract
The present study investigates the fate of the cell-bound IgE by using a well-characterized rat basophilic leukemia cell line and a purified IgE myeloma protein. Both histamine-releasing and nonreleasing cell lines were examined. In both cases, no evidence for cell-mediated IgE catabolism could be elicited. Both the dissociated IgE and the receptors remained intact for prolonged periods of time, as demonstrated by binding assays. Internalization and/or recycling of membrane-bound IgE could not be demonstrated by E. M. autoradiography. We found only limited time-dependent changes in accessibility to anti-IgE antibody, trypsin, or elution at low pH (2.9 to 3.1). A biphasic dissociation of cell-bound 125I-IgE during incubation in the presence of excess unlabeled IgE was reproducibly observed; the more slowly dissociated IgE was also less readily dissociated at pH 3.4. These studies lead us to conclude that, in vitro, IgE resides in a functional orientation on the surface of RBL-1 cells, for prolonged periods of time.
Footnotes
1 This work was presented in part at the Third International Congress of Immunology, Sydney, Australia, July 1977, and at the American Society of Biological Chemists/American Association of Immunologists Joint Meeting in Atlanta, Georgia, 1978.
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