Journal article
Analysis of Fc(epsilon)RI-mediated mast cell stimulation by surface-carried antigens
Biophysical journal, v 72(6), pp 2470-2478
01 Jun 1997
PMID: 9168023
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Clustering of the type I receptor for IgE (Fc[epsilon]RI) on mast cells initiates a cascade of biochemical processes that result in secretion of inflammatory mediators. To determine the Fc(epsilon)RI proximity, cluster size, and mobility requirements for initiating the Fc(epsilon)RI cascade, a novel experimental protocol has been developed in which mast cells are reacted with glass surfaces carrying different densities of both antigen and bound IgE, and the cell's secretory response to these stimuli is measured. The results have been analyzed in terms of a model based on the following assumptions: 1) the glass surface antigen distribution and consequently that of the bound IgE are random; 2) Fc(epsilon)RI binding to these surface-bound IgEs immobilizes the former and saturates the latter; 3) the cell surface is formally divided into small elements, which function as a secretory stimulus unit when occupied by two or more immobilized IgE-Fc(epsilon)RI complexes; 4) alternatively, similar stimulatory units can be formed by binding of surface-carried IgE dimers to two Fc(epsilon)RI. This model yielded a satisfactory and self-consistent fitting of all of the different experimental data sets. Hence the present results establish the essential role of Fc(epsilon)RI immobilization for initiating its signaling cascade. Moreover, it provides independent support for the notion that as few as two Fc(epsilon)RIs immobilized at van der Waals contact constitute an "elementary stimulatory unit" leading to mast cell (RBL-2H3 line) secretory response.
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Details
- Title
- Analysis of Fc(epsilon)RI-mediated mast cell stimulation by surface-carried antigens
- Creators
- R Schweitzer-Stenner - University of BremenI Tamir - University of BremenI Pecht - University of Bremen
- Publication Details
- Biophysical journal, v 72(6), pp 2470-2478
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Chemistry
- Web of Science ID
- WOS:A1997XA63600008
- Scopus ID
- 2-s2.0-0030612102
- Other Identifier
- 991019196446904721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Biophysics