In vitro synthesis of IgE by human lymphocytes. II. Enhancement of the spontaneous IgE synthesis by IgE-binding factors secreted by RPMI 8866 lymphoblastoid B cells. 1984

M Sarfati, and E Rector, and K Wong, and M Rubio-Trujillo, and A H Sehon, and G Delespesse

RPMI 8866 lymphoblastoid cells, known to express surface Fc epsilon R, were tested for their ability to regulate the in vitro synthesis of human IgE. Cell-free supernatants (CFS) of RPMI 8866 cells enhanced in a dose-dependent fashion the spontaneous IgE synthesis by B cells of allergic individuals. For maximum activity the CFS had to be added during the first 3 days of culture. CFS did not significantly alter the spontaneous synthesis of IgM or IgG, but they suppressed IgA synthesis both in B cell cultures and in pokeweed mitogen-stimulated peripheral blood mononuclear cells cultures. Cyclosporin A did not suppress either the spontaneous Ig production by B cells nor the IgE-potentiating activity of CFS. The enhancing activity of CFS was related to its content in IgE binding factors (IgE-BFs); these factors were detected by their ability to inhibit the rosetting of RPMI 8866 cells with IgE-coated erythrocytes (E-IgE). Both the IgE-BFs and the IgE-potentiating activity of the supernatants of RPMI 8866 cell cultures could be removed by absorption with IgE-Sepharose, from which they could subsequently be eluted with glycine-HCl buffer. IgE-BFs were identified as glycoproteins on the basis of their sensitivity to trypsin and to neuraminidase. By filtration of the RPMI 8866 cell supernatants through a Sephadex G75 column, IgE-binding activity was found to be associated with two fractions with molecular sizes in the range of 10,000-15,000 and 30,000-40,000. The IgA-suppressing activity of the RPMI 8866 culture filtrates could be absorbed with sIgA-Sepharose from which it was subsequently recovered by elution with glycine-HCl buffer. Most unexpectedly, sIgA-Sepharose also removed IgE-BFs and IgE-potentiating activity from the RPMI 8866 supernatants; both could be recovered by subsequent elution from sIgA-Sepharose with gycline-HCl buffer. These data are provisionally interpreted as indicating that the IgE-BFs secreted by RPMI 8866 cells had affinity for both IgE and sIgA and that they exerted a reciprocal effect on the in vitro synthesis of IgE and IgA.

UI MeSH Term Description Entries
D006968 Hypersensitivity, Delayed An increased reactivity to specific antigens mediated not by antibodies but by sensitized T CELLS. Hypersensitivity, Tuberculin-Type,Hypersensitivity, Type IV,Tuberculin-Type Hypersensitivity,Type IV Hypersensitivity,Delayed Hypersensitivity,Delayed Hypersensitivities,Hypersensitivity, Tuberculin Type,Tuberculin Type Hypersensitivity,Tuberculin-Type Hypersensitivities,Type IV Hypersensitivities
D007073 Immunoglobulin E An immunoglobulin associated with MAST CELLS. Overexpression has been associated with allergic hypersensitivity (HYPERSENSITIVITY, IMMEDIATE). IgE
D007136 Immunoglobulins Multi-subunit proteins which function in IMMUNITY. They are produced by B LYMPHOCYTES from the IMMUNOGLOBULIN GENES. They are comprised of two heavy (IMMUNOGLOBULIN HEAVY CHAINS) and two light chains (IMMUNOGLOBULIN LIGHT CHAINS) with additional ancillary polypeptide chains depending on their isoforms. The variety of isoforms include monomeric or polymeric forms, and transmembrane forms (B-CELL ANTIGEN RECEPTORS) or secreted forms (ANTIBODIES). They are divided by the amino acid sequence of their heavy chains into five classes (IMMUNOGLOBULIN A; IMMUNOGLOBULIN D; IMMUNOGLOBULIN E; IMMUNOGLOBULIN G; IMMUNOGLOBULIN M) and various subclasses. Globulins, Immune,Immune Globulin,Immune Globulins,Immunoglobulin,Globulin, Immune
D008213 Lymphocyte Activation Morphologic alteration of small B LYMPHOCYTES or T LYMPHOCYTES in culture into large blast-like cells able to synthesize DNA and RNA and to divide mitotically. It is induced by INTERLEUKINS; MITOGENS such as PHYTOHEMAGGLUTININS, and by specific ANTIGENS. It may also occur in vivo as in GRAFT REJECTION. Blast Transformation,Blastogenesis,Lymphoblast Transformation,Lymphocyte Stimulation,Lymphocyte Transformation,Transformation, Blast,Transformation, Lymphoblast,Transformation, Lymphocyte,Activation, Lymphocyte,Stimulation, Lymphocyte
D008222 Lymphokines Soluble protein factors generated by activated lymphocytes that affect other cells, primarily those involved in cellular immunity. Lymphocyte Mediators,Mediators, Lymphocyte
D009439 Neuraminidase An enzyme that catalyzes the hydrolysis of alpha-2,3, alpha-2,6-, and alpha-2,8-glycosidic linkages (at a decreasing rate, respectively) of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid, and synthetic substrate. (From Enzyme Nomenclature, 1992) Sialidase,Exo-alpha-Sialidase,N-Acylneuraminate Glycohydrolases,Oligosaccharide Sialidase,Exo alpha Sialidase,Glycohydrolases, N-Acylneuraminate,N Acylneuraminate Glycohydrolases,Sialidase, Oligosaccharide
D011961 Receptors, Fc Molecules found on the surface of some, but not all, B-lymphocytes, T-lymphocytes, and macrophages, which recognize and combine with the Fc (crystallizable) portion of immunoglobulin molecules. Fc Receptors,Fc Receptor,Receptor, Fc
D002460 Cell Line Established cell cultures that have the potential to propagate indefinitely. Cell Lines,Line, Cell,Lines, Cell
D002474 Cell-Free System A fractionated cell extract that maintains a biological function. A subcellular fraction isolated by ultracentrifugation or other separation techniques must first be isolated so that a process can be studied free from all of the complex side reactions that occur in a cell. The cell-free system is therefore widely used in cell biology. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p166) Cellfree System,Cell Free System,Cell-Free Systems,Cellfree Systems,System, Cell-Free,System, Cellfree,Systems, Cell-Free,Systems, Cellfree
D002846 Chromatography, Affinity A chromatographic technique that utilizes the ability of biological molecules, often ANTIBODIES, to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Chromatography, Bioaffinity,Immunochromatography,Affinity Chromatography,Bioaffinity Chromatography

Related Publications

M Sarfati, and E Rector, and K Wong, and M Rubio-Trujillo, and A H Sehon, and G Delespesse
April 1987, Immunology,
M Sarfati, and E Rector, and K Wong, and M Rubio-Trujillo, and A H Sehon, and G Delespesse
September 1988, Immunology,
M Sarfati, and E Rector, and K Wong, and M Rubio-Trujillo, and A H Sehon, and G Delespesse
November 1988, European journal of immunology,
M Sarfati, and E Rector, and K Wong, and M Rubio-Trujillo, and A H Sehon, and G Delespesse
January 1987, Immunology,
M Sarfati, and E Rector, and K Wong, and M Rubio-Trujillo, and A H Sehon, and G Delespesse
January 1988, International archives of allergy and applied immunology,
M Sarfati, and E Rector, and K Wong, and M Rubio-Trujillo, and A H Sehon, and G Delespesse
May 1981, Journal of immunology (Baltimore, Md. : 1950),
M Sarfati, and E Rector, and K Wong, and M Rubio-Trujillo, and A H Sehon, and G Delespesse
November 1982, Clinical immunology and immunopathology,
M Sarfati, and E Rector, and K Wong, and M Rubio-Trujillo, and A H Sehon, and G Delespesse
November 1976, Journal of immunology (Baltimore, Md. : 1950),
M Sarfati, and E Rector, and K Wong, and M Rubio-Trujillo, and A H Sehon, and G Delespesse
September 1981, Clinical and experimental immunology,
Copied contents to your clipboard!