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Title: Histamine release due to bivalent penicilloyl haptens: the relation of activation and desensitization of basophils to dynamic aspects of ligand binding to cell surface antibody

Abstract

We study the time-dependent aspects of activation and desensitization of passively sensitized human basophils by a bivalent penicilloyl hapten, (BPO)/sub 2/, in the presence or absence of a monovalent penicilloyl hapten, (BPO)/sub 1/. Data presented in this and the preceeding paper are found to be consistent with a simple kinetic model of the binding and cross-linking reaction between (BPO)/sub 1/, (BPO)/sub 2/, and cell surface IgE. It is shown that the rapid perturbation of cross-linked IgE by simple dilution or washing of cells or by addition of excess (BPO)/sub 1/ causes re-equilibration of the rate of histamine release within a matter of seconds. This demonstrates that no stable antigen-independent activated state of basophils exists and that cross-linked antibody is necessary throughout the entire time course of histamine release. In addition, we show that desensitization requires the continuing presence of cross-linked antibody on the cell surface and that the rate of desensitization is a monotone increasing function of the number of cross-linked IgE molecules per cell. The rate of desensitization also appears to be a saturable function of the number of cross-linked IgE antibodies.

Authors:
; ; ;
Publication Date:
Research Org.:
Los Alamos Scientific Lab., New Mexico
OSTI Identifier:
6394393
Alternate Identifier(s):
OSTI ID: 6394393
Resource Type:
Journal Article
Journal Name:
J. Immunol.; (United States)
Additional Journal Information:
Journal Volume: 122:2
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; ANTIBODIES; BINDING ENERGY; BASOPHILS; IMMUNE REACTIONS; HISTAMINE; LIGANDS; ANIMAL CELLS; CHEMICAL ACTIVATION; MATHEMATICAL MODELS; SENSITIVITY; TIME DEPENDENCE; AMINES; AZOLES; BIOLOGICAL MATERIALS; BLOOD; BLOOD CELLS; BODY FLUIDS; ENERGY; HETEROCYCLIC COMPOUNDS; IMIDAZOLES; LEUKOCYTES; ORGANIC COMPOUNDS; ORGANIC NITROGEN COMPOUNDS 550500* -- Metabolism

Citation Formats

Dembo, M., Goldstein, B., Sobotka, A.K., and Lichtenstein, L.M. Histamine release due to bivalent penicilloyl haptens: the relation of activation and desensitization of basophils to dynamic aspects of ligand binding to cell surface antibody. United States: N. p., 1979. Web.
Dembo, M., Goldstein, B., Sobotka, A.K., & Lichtenstein, L.M. Histamine release due to bivalent penicilloyl haptens: the relation of activation and desensitization of basophils to dynamic aspects of ligand binding to cell surface antibody. United States.
Dembo, M., Goldstein, B., Sobotka, A.K., and Lichtenstein, L.M. Thu . "Histamine release due to bivalent penicilloyl haptens: the relation of activation and desensitization of basophils to dynamic aspects of ligand binding to cell surface antibody". United States.
@article{osti_6394393,
title = {Histamine release due to bivalent penicilloyl haptens: the relation of activation and desensitization of basophils to dynamic aspects of ligand binding to cell surface antibody},
author = {Dembo, M. and Goldstein, B. and Sobotka, A.K. and Lichtenstein, L.M.},
abstractNote = {We study the time-dependent aspects of activation and desensitization of passively sensitized human basophils by a bivalent penicilloyl hapten, (BPO)/sub 2/, in the presence or absence of a monovalent penicilloyl hapten, (BPO)/sub 1/. Data presented in this and the preceeding paper are found to be consistent with a simple kinetic model of the binding and cross-linking reaction between (BPO)/sub 1/, (BPO)/sub 2/, and cell surface IgE. It is shown that the rapid perturbation of cross-linked IgE by simple dilution or washing of cells or by addition of excess (BPO)/sub 1/ causes re-equilibration of the rate of histamine release within a matter of seconds. This demonstrates that no stable antigen-independent activated state of basophils exists and that cross-linked antibody is necessary throughout the entire time course of histamine release. In addition, we show that desensitization requires the continuing presence of cross-linked antibody on the cell surface and that the rate of desensitization is a monotone increasing function of the number of cross-linked IgE molecules per cell. The rate of desensitization also appears to be a saturable function of the number of cross-linked IgE antibodies.},
doi = {},
journal = {J. Immunol.; (United States)},
number = ,
volume = 122:2,
place = {United States},
year = {1979},
month = {2}
}