Phosphorylation and dephosphorylation of the high-affinity receptor for immunoglobulin E immediately after receptor engagement and disengagement

Nature ◽  
1991 ◽  
Vol 353 (6347) ◽  
pp. 855-858 ◽  
Author(s):  
Rossella Paolini ◽  
Marie-Hélène Jouvin ◽  
Jean-Pierre Kinet
Keyword(s):  
Immunoglobulin E ◽  
High Affinity ◽  
High Affinity Receptor ◽  
Affinity Receptor ◽  
Engagement And Disengagement

The High Affinity Receptor for Immunoglobulin E: New Developments

1989 ◽  
pp. 716-723 ◽  
Author(s):  
J.-P. Kinet ◽  
H. Metzger ◽  
G. Alber ◽  
U. Blank ◽  
K. Huppi ◽  
...  
Keyword(s):  
Immunoglobulin E ◽  
New Developments ◽  
High Affinity ◽  
High Affinity Receptor ◽  
Affinity Receptor

scholarly journals Human epidermal Langerhans cells express the high affinity receptor for immunoglobulin E (Fc epsilon RI).

1992 ◽  
Vol 175 (5) ◽  
pp. 1285-1290 ◽  
Author(s):  
T Bieber ◽  
H de la Salle ◽  
A Wollenberg ◽  
J Hakimi ◽  
R Chizzonite ◽  
...  
Keyword(s):  
Langerhans Cells ◽  
Immunoglobulin E ◽  
Atopic Disease ◽  
High Affinity ◽  
Basophil Cell ◽  
Ku812 Cells ◽  
High Affinity Receptor ◽  
Affinity Receptor ◽  
Human Basophils ◽  
Epidermal Langerhans Cells

It has been suggested that epidermal Langerhans cells (LC) bearing immunoglobulin E (IgE) may be involved in the genesis of atopic disease. The identity of the IgE receptor(s) on LC remained unclear, although it represents a crucial point in understanding cellular events linked to the binding of allergens to LC via IgE. In this report, we demonstrate that epidermal LC express the high affinity receptor for the Fc fragment of IgE (Fc epsilon RI) which has, so far, only been described on mast cells and basophils. Epidermal LC react with antibodies specific for the alpha subunit of the tetrameric (alpha, beta, 2 gamma) Fc epsilon RI. Specific transcripts for Fc epsilon RI alpha and Fc epsilon RI gamma were detected in LC and correspond to those of human basophils and of the human basophil cell line KU812. Furthermore, human basophils, KU812 cells, and LC express the putative beta subunit. Thus human LC express the complete structure of Fc epsilon RI. This finding opens new perspectives in the putative functional role of this structure on antigen-presenting cells.

Thermodynamics of the Interaction of Human Immunoglobulin E with Its High-Affinity Receptor FcεRI†

Biochemistry ◽  
1998 ◽  
Vol 37 (25) ◽  
pp. 8863-8869 ◽  
Author(s):  
Maura B. Keown ◽  
Alistair J. Henry ◽  
Rodolfo Ghirlando ◽  
Brian J. Sutton ◽  
Hannah J. Gould
Keyword(s):  
Immunoglobulin E ◽  
Human Immunoglobulin ◽  
High Affinity ◽  
High Affinity Receptor ◽  
Affinity Receptor
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