PT  - JOURNAL ARTICLE
AU  - S J Smith
AU  - A Galvin
AU  - I Hall
AU  - F Shakib
TI  - Circulating human IgG autoanti-IgE antibodies in asthma patients block the binding of IgE to its high affinity receptor
AID  - 10.1136/mp.48.3.M148
DP  - 1995 Jun 01
TA  - Clinical Molecular Pathology
PG  - M148--M152
VI  - 48
IP  - 3
4099  - http://mp.bmj.com/content/48/3/M148.short
4100  - http://mp.bmj.com/content/48/3/M148.full
SO  - Clin Mol Pathol1995 Jun 01; 48
AB  - Aims—To investigate the ability of circulating human IgG autoanti-IgE antibodies from asthma patients to block the binding of IgE to the α chain of the high affinity receptor (FcεRI).Methods—This involved the use of a well validated flow cytometric method to detect inhibition of FITC labelled IgE binding to a fibroblast cell line (CHK1E1) transfected with the α chain of FcεRI.Results—IgG autoanti-IgE-containing sera blocked the binding of IgE-FITC to the CHK1E1 cells. No such inhibition was demonstrable with rheumatoid sera containing autoanti-IgG (that is, rheumatoid factor) but lacking autoanti-IgE. Percentage inhibition (up to 50%) of IgE binding to the CHK1E1 cells was directly related to the titre of IgG1, but not IgG4, autoanti-IgE in the sera tested (correlation coefficient 0·66, probability 0·003).Conclusions—The capacity of anti-IgE to block the binding of IgE to FcεRI has important clinical implications, particularly in terms of downregulation of allergic reactions.