Effect ofClostridium difficileToxin B on IgE Receptor-Mediated Signal Transduction in Rat Basophilic Leukemia Cells: Inhibition of Phospholipase D Activation

1996 ◽  
Vol 224 (2) ◽  
pp. 591-596 ◽  
Author(s):  
Katsuhiro Ojio ◽  
Yoshiko Banno ◽  
Shigeru Nakashima ◽  
Naoki Kato ◽  
Kunitomo Watanabe ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Phospholipase D ◽  
Leukemia Cells ◽  
Ige Receptor ◽  
Rat Basophilic Leukemia Cells ◽  
Basophilic Leukemia

scholarly journals Cross-linking of IgE-receptor complexes by rigid bivalent antigens greater than 200 A in length triggers cellular degranulation.

1988 ◽  
Vol 107 (3) ◽  
pp. 969-980 ◽  
Author(s):  
P M Kane ◽  
D Holowka ◽  
B Baird
Keyword(s):  
Signal Transduction ◽  
Leukemia Cells ◽  
Cross Linking ◽  
Linear Polymers ◽  
Ige Receptor ◽  
Surface Receptors ◽  
Receptor Complexes ◽  
Rat Basophilic Leukemia Cells ◽  
Biotin Binding ◽  
Basophilic Leukemia

We have examined the effect of cross-linking IgE-receptor complexes with variable receptor-receptor distances on the transmembrane signaling that leads to degranulation of rat basophilic leukemia cells. Linear polymers of the biotin-binding protein avidin were generated with bis biotin-1,12-diamidododecane, and a dinitrophenyl-biotin conjugate was bound at each end of the polymers to form a series of rigid bivalent haptens of well-defined length. The polymers were fractionated by size with nondenaturing PAGE, electro-eluted, and tested for their ability to stimulate degranulation of rat basophilic leukemia cells sensitized with anti-DNP IgE. We found that hexamers of avidin (of length greater than or equal to 240 A) were as effective in triggering degranulation as dimers (of length approximately 80 A), while the monomeric avidin antigen (of length approximately 40 A) elicited a poorer degranulation response from the cells. The mechanism by which aggregation of cell surface receptors can initiate signal transduction is discussed in light of these results.

The distribution of antigen on the surface of RBL-2H3 rat basophilic leukemia cells observed by back-scattered electron imaging

1986 ◽  
Vol 44 ◽  
pp. 274-275
Author(s):  
R.F. Stump ◽  
J.R. Pfeiffer ◽  
JC. Seagrave ◽  
D. Huskisson ◽  
J.M. Oliver
Keyword(s):  
Cell Surface ◽  
Dynamic Properties ◽  
Leukemia Cells ◽  
Antigen Binding ◽  
Scattered Electron ◽  
Ige Receptor ◽  
Receptor Complexes ◽  
Rat Basophilic Leukemia Cells ◽  
Electron Imaging ◽  
Basophilic Leukemia

In RBL-2H3 rat basophilic leukemia cells, antigen binding to cell surface IgE-receptor complexes stimulates the release of inflammatory mediators and initiates a series of membrane and cytoskeletal events including a transformation of the cell surface from a microvillous to a lamellar topography. It is likely that dynamic properties of the IgE receptor contribute to the activation of these responses. Fewtrell and Metzger have established that limited crosslinking of IgE-receptor complexes is essential to trigger secretion. In addition, Baird and colleagues have reported that antigen binding causes a rapid immobilization of IgE-receptor complexes, and we have demonstrated an apparent increase with time in the affinity of IgE-receptor complexes for antigen.

scholarly journals Cross-linking of receptor-bound IgE to aggregates larger than dimers leads to rapid immobilization.

1986 ◽  
Vol 102 (2) ◽  
pp. 541-550 ◽  
Author(s):  
A K Menon ◽  
D Holowka ◽  
W W Webb ◽  
B Baird
Keyword(s):  
High Efficiency ◽  
Leukemia Cells ◽  
Cross Linking ◽  
Ige Receptor ◽  
Triggering Mechanism ◽  
Receptor Complexes ◽  
Rat Basophilic Leukemia Cells ◽  
Receptor Clusters ◽  
Receptor Dimers ◽  
Basophilic Leukemia

Controlled cross-linking of IgE-receptor complexes on the surface of rat basophilic leukemia cells and mast cells has allowed a comparison of the lateral mobility and cell triggering activity of monomers, dimers, and higher oligomers of receptors. Addition of a monoclonal anti-IgE(Fc) antibody to IgE-sensitized cells in stoichiometric amounts relative to IgE produces IgE-receptor dimers with high efficiency. These dimers are nearly as mobile as IgE-receptor monomers and trigger cellular degranulation poorly, but in the presence of 30% D2O, substantial immobilization of the dimers is seen and degranulation activity doubles. Addition of this monoclonal antibody in larger amounts results in the formation of larger oligomeric receptor clusters which are immobile and effectively trigger the cells. Thus, small receptor clusters that are active in stimulating degranulation are immobilized in a process that is not anticipated by simple hydrodynamic theories. Further experiments involving cross-linking of receptor-bound IgE by multivalent antigen demonstrate that immobilization of receptors occurs rapidly (less than 2 min) upon cross-linking and is fully and rapidly reversible by the addition of excess monovalent hapten. The rapidity and reversibility of the immobilization process are entirely consistent with the possibility that immobilization represents a recognition event between clustered receptors and cytoskeleton-associated components that plays an important role early in the cell triggering mechanism.

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