Literature DB >> 1587638

The recognition of a recombinant human Fc epsilon fragment by the subclasses of IgG autoanti-IgE: disproportional subclasses distribution of complexed autoantibody.

F Shakib1, C S Mills, A Powell-Richards.   

Abstract

Circulating IgG autoanti-IgE is detectable in a large proportion of individuals with allergic asthma where it is suggested to be potentially involved in the removal of IgE-allergen complexes. Since such a putative role will largely be determined by the subclass profile of complexed (i.e. IgE-bound) IgG anti-IgE, a study was undertaken to determine the subclass distribution of complexed IgG anti-IgE antibody in the sera of asthmatic patients. The study exploits the heat-labile property of IgE by heating (30 min at 56 degrees C) serum to liberate bound anti-IgE, pre- and post-heated sera are then assayed for IgG subclass anti-recombinant human Fc epsilon (rFc epsilon) activities by ELISA and any heat-induced increase in antibody activity is taken as a measure of complexed anti-IgE. This has revealed a disproportionately high amount of IgG4 in complexed (but not free) IgG anti-IgE. The propensity of IgG4 to form complexes with IgE has important biological consequences, particularly with regard to the activation of C1q and Fc gamma R by other subclasses.

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Year:  1992        PMID: 1587638     DOI: 10.1159/000236127

Source DB:  PubMed          Journal:  Int Arch Allergy Immunol        ISSN: 1018-2438            Impact factor:   2.749


  1 in total

1.  Circulating human IgG autoanti-IgE antibodies in asthma patients block the binding of IgE to its high affinity receptor.

Authors:  S J Smith; A Galvin; I Hall; F Shakib
Journal:  Clin Mol Pathol       Date:  1995-06
  1 in total

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