The cross-reactivity of rat IgE and IgG with solubilized receptors of rat basophilic leukemia cells

Kepron, M.R.; Conrad, Daniel H.; Froese, Arnold

doi:10.1016/0161-5890(82)90274-7

Cited by 12 publications

(2 citation statements)

References 18 publications

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“…Moreover, mAb 51.3 had the same partial inhibitory effect on the binding of '"I-IgE No. 28.52, which is ~~1 1~ as on the SPE-7 which is e2xk (data not shown). We therefore prefer to assume that there is heterogeneity in the receptors on RBL cells for IgE.…”

Section: The Effect Of Anti-ige Mab On In Vivo Degranulationmentioning

confidence: 81%

Inhibition of IgE binding to mast cells and basophils by monoclonal antibodies to murine IgE

1984

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In an attempt to identify the site on IgE which binds with high affinity to the Fc epsilon receptor (Fc epsilon R) on mast cells, we established monoclonal anti-IgE antibodies (mAb) by fusion of myeloma cells with rat splenocytes immunized with purified murine IgE mAb. Six individual mAb were found to react with various IgE mAb of different specificities and not with immunoglobulins of other classes. Three different clusters of epitopes on the Fc epsilon portion could be detected by antibody competition studies. These antigenic determinants were expressed on the Fc epsilon portion and required the two heavy chains in their native conformation. Two groups of mAb and their Fab' fragments completely inhibited the binding of 125I-labeled IgE to rat basophilic leukemia cells (RBL), and one mAb inhibited the specific IgE binding only partially (55-65%). Likewise, the Fab' fragments of the purified mAb inhibited the antigen-mediated, IgE-dependent, serotonin release of RBL cells. These in vitro findings were confirmed by in vivo experiments, which demonstrated that the anti-IgE mAb could specifically block passive cutaneous anaphylaxis reaction when injected i.d., before challenging with the antigen. The differences in blocking reactivity of the various anti-IgE mAb are discussed in view of heterogeneity in the IgE-Fc epsilon R interaction.

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Section: The Effect Of Anti-ige Mab On In Vivo Degranulationmentioning

confidence: 81%

Inhibition of IgE binding to mast cells and basophils by monoclonal antibodies to murine IgE

1984

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“…hyorhinis was inhibited by IgE saturation of the R receptors [4]. Since excess IgE was removed by washing from mycoplasma-free CA10.7 cells before infection or from infected CAlO cells after 90-min incubation, and since the IgE would be expected to remain bound to high-affinity R receptor [6, 71 and be washed off the H receptor which binds IgE with a low affinity [38], it is most likely that the IgE was degraded while bound to R receptors. However, further studies are required to determine whether the observed IgE degradation is a result of M .…”

Section: Characterization Of the Cleavage Products By 2-d Sds-page Anmentioning

confidence: 99%

Mycoplasma‐induced degradation of IgE bound by Fcϵ receptors of rat basophilic leukemia cells

Chan

Froese

1987

Eur J Immunol

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Previous studies from this laboratory have shown that Mycoplasma hyorhinis interacts with some unoccupied, high-affinity 45-kDa receptors for IgE on rat basophilic leukemia (RBL) cells to induce the formation of 71-kDa receptors for IgE. The present study demonstrates that when IgE is bound to the high-affinity receptors, exposure of RBL cells to mycoplasma leads to a time-dependent degradation of the cell-bound IgE into fragments of 186 kDa, 158 kDa and 115 kDa, all of which remain bound to the receptors. Upon reduction, these fragments yield 67-kDa and 55-kDa epsilon chain-derived polypeptides. The degradation appears to start at the N-terminus of the IgE, leading eventually to a complete loss of L chains. In the absence of mycoplasma, the IgE remains relatively intact throughout the same time period with a molecular mass of 210 kDa. The observed degradation of receptor-bound IgE by mycoplasma, should it also occur in vivo, could have important consequences as far as the IgE-dependent mediator release is concerned.

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Effects of mycoplasma infection on Fc receptors for IgE of rat basophilic leukemia cells

et al. 1986

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Earlier studies from this laboratory had shown that rat basophilic leukemia cells carry two major receptors for IgE, named R and H, and a third minor receptor, designated 71K. It is now apparent that 71K is induced by the action of Mycoplasma hyorhinis, a common contaminant of tissue cultures. This induction is reversible. Decontamination either in in vitro or in vivo leads to a disappearance of 71K and re-infection causes its reappearance. The 71K receptor appears to be induced by the action of the mycoplasma on a surface molecule, most likely R, present on the cells at the time of infection. When receptors are occupied by IgE, 71K induction is inhibited. Other effects of mycoplasma infection include the significant reduction in the expression of transferrin receptors and increased histamine content of infected cells.

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The cross-reactivity of rat IgE and IgG with solubilized receptors of rat basophilic leukemia cells

Cited by 12 publications

References 18 publications

Inhibition of IgE binding to mast cells and basophils by monoclonal antibodies to murine IgE

Inhibition of IgE binding to mast cells and basophils by monoclonal antibodies to murine IgE

Mycoplasma‐induced degradation of IgE bound by Fcϵ receptors of rat basophilic leukemia cells

Effects of mycoplasma infection on Fc receptors for IgE of rat basophilic leukemia cells

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