Changes in the receptor for immunoglobulin E coincident with receptor-mediated stimulation of basophilic leukemia cells

Biochemistry ◽  
1983 ◽  
Vol 22 (25) ◽  
pp. 5733-5737 ◽  
Author(s):  
Ruy Perez-Monfort ◽  
Clare Fewtrell ◽  
Henry Metzger
Keyword(s):  
Immunoglobulin E ◽  
Leukemia Cells ◽  
Basophilic Leukemia ◽  
Stimulation Of

Immunoglobulin E mediated membrane conductance changes in rat basophilic leukemia cells

1988 ◽  
Vol 66 (3) ◽  
pp. 328-331 ◽  
Author(s):  
Carlos Barajas-López ◽  
Jan D. Huizinga
Keyword(s):  
Immunoglobulin E ◽  
Calcium Influx ◽  
Membrane Conductance ◽  
Membrane Resistance ◽  
Leukemia Cells ◽  
Rat Basophilic Leukemia Cells ◽  
Conductance Changes ◽  
Electrophysiological Effects ◽  
Basophilic Leukemia ◽  
Stimulation Of

Electrophysiological effects of anaphylactic stimulation of rat basophilic leukemia cells (RBL-2H3) were studied using conventional microelectrodes. Stimulation of passively sensitized cells by anti-immunoglobulin E resulted in hyperpolarization followed by depolarization. These changes in membrane polarization were associated with a decrease in input membrane resistance. No effect of anaphylactic stimulation was seen in Ca2+-free solution or when Ca2+ influx was blocked by Co2+, but it was mimicked by the Ca2+ ionophore A-23187. This suggests that the changes in ionic conductances were associated with calcium influx. These results support the hypothesis that membrane conductance changes are involved in the stimulus-secretion process of the RBL-2H3 cells.

scholarly journals Small oligomers of immunoglobulin E (IgE) cause large-scale clustering of IgE receptors on the surface of rat basophilic leukemia cells.

1984 ◽  
Vol 98 (2) ◽  
pp. 577-583 ◽  
Author(s):  
A K Menon ◽  
D Holowka ◽  
B Baird
Keyword(s):  
Fluorescence Microscopy ◽  
Cell Surface ◽  
Large Scale ◽  
Immunoglobulin E ◽  
Leukemia Cells ◽  
Ige Receptors ◽  
Rat Basophilic Leukemia Cells ◽  
A Cell ◽  
Basophilic Leukemia

We examined the distribution of small oligomers of IgE bound to rat basophilic leukemia cells using fluorescence microscopy. The oligomers were seen to cluster into visible patches on the cell surface at 4 degrees C; at higher temperatures internalization also was observed. In contrast, cells labeled with IgE monomers remained predominantly ring-stained. Evidence is provided that the observed clustering of IgE oligomers is a cell-induced phenomenon, and the possible significance of this clustering is discussed in the context of the oligomer-triggered degranulation of rat basophilic leukemia cells.

scholarly journals Clustering, mobility, and triggering activity of small oligomers of immunoglobulin E on rat basophilic leukemia cells.

1986 ◽  
Vol 102 (2) ◽  
pp. 534-540 ◽  
Author(s):  
A K Menon ◽  
D Holowka ◽  
W W Webb ◽  
B Baird
Keyword(s):  
Large Scale ◽  
Immunoglobulin E ◽  
Gel Filtration ◽  
Leukemia Cells ◽  
Fluorescence Photobleaching Recovery ◽  
Photobleaching Recovery ◽  
Rat Basophilic Leukemia Cells ◽  
Cellular Components ◽  
Basophilic Leukemia ◽  
Selective Interactions

We have recently shown that small oligomers of IgE bound to univalent receptors for IgE on the surface of rat basophilic leukemia cells induce extensive aggregation of the receptors at 4 degrees C into patches resolvable by fluorescence microscopy and that this does not occur with monomeric IgE (Menon, A. K., D. Holowka, and B. Baird, 1984, J. Cell Biol. 98:577-583). Here we use fluorescence photobleaching recovery measurements to show that receptor oligomerization by this means is accompanied by a dramatic reduction of receptor lateral mobility, and that this immobilization occurs even when the clustering is not microscopically detectable. Furthermore, the degree of immobility induced by a particular oligomer fraction from a gel filtration column correlates positively with its ability to trigger cellular degranulation, whereas receptors labeled with monomeric IgE have no triggering activity and exhibit typical membrane protein mobility. The slow, large-scale oligomer-induced clustering appears to be a long term consequence of earlier selective interactions that result in receptor immobilization, and this highly clustered state provides a competent, noninhibitory triggering signal resulting in cellular degranulation upon warming to 37 degrees C. We conclude that even limited clustering of IgE receptors on rat basophilic leukemia cells induces interactions with other cellular components that constrain receptor mobility and eventually cause massive coalescence of the clusters. These primary selective interactions occurring at the level of receptor oligomers or small clusters of oligomers that result in immobilization may play a role in triggering cellular degranulation.

Rotational dynamics of the Fc receptor for immunoglobulin E on histamine-releasing rat basophilic leukemia cells

Biochemistry ◽  
1986 ◽  
Vol 25 (15) ◽  
pp. 4397-4401 ◽  
Author(s):  
Raphael Zidovetzki ◽  
Marty Bartholdi ◽  
Donna Arndt-Jovin ◽  
Thomas M. Jovin
Keyword(s):  
Immunoglobulin E ◽  
Fc Receptor ◽  
Rotational Dynamics ◽  
Leukemia Cells ◽  
Rat Basophilic Leukemia Cells ◽  
Basophilic Leukemia

scholarly journals Clustering of Syk is sufficient to induce tyrosine phosphorylation and release of allergic mediators from rat basophilic leukemia cells.

1995 ◽  
Vol 15 (3) ◽  
pp. 1582-1590 ◽  
Author(s):  
V M Rivera ◽  
J S Brugge
Keyword(s):  
Signaling Pathways ◽  
Tyrosine Phosphorylation ◽  
Immunoglobulin E ◽  
Transmembrane Protein ◽  
Allergic Response ◽  
Mediator Release ◽  
Leukemia Cells ◽  
Rat Basophilic Leukemia Cells ◽  
Multiple Signaling ◽  
Basophilic Leukemia

In mast cells, antigen-mediated aggregation of the high-affinity receptor for immunoglobulin E, Fc epsilon RI, stimulates tyrosine phosphorylation and activation of multiple signaling pathways leading to the release of several classes of mediators of the allergic response. Early events induced upon cross-linking of Fc epsilon RI include tyrosine phosphorylation of Fc epsilon RI subunits and activation of the tyrosine kinase p72syk (Syk), which binds to tyrosine-phosphorylated Fc epsilon RI. Clustering of Syk, as a result of its interaction with aggregated Fc epsilon RI, may play a role in activating one or more of the signaling pathways leading to mediator release. To test this possibility, Syk was introduced into a model mast cell line (rat basophilic leukemia cells) as part of a chimeric transmembrane protein containing the extracellular and transmembrane domains of CD16 and CD7, respectively. Clustering of the Syk chimera, using antibodies against CD16, was found to be sufficient to stimulate early and late events normally induced by clustering of Fc epsilon RI. Specifically, aggregation of Syk induced degranulation, leukotriene synthesis, and expression of cytokine genes. Induction of mediator release was dependent on the kinase activity of Syk. Consistent with this finding, clustering of Syk also induced the tyrosine phosphorylation of a profile of proteins, including phospholipase C-gamma 1 and mitogen-activated protein kinase, similar to that induced upon clustering of Fc epsilon RI. These results strongly suggest that Syk is an early and critical mediator of multiple signaling pathways that emanate from the Fc epsilon RI receptor and give rise to the allergic response.

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