Calcium mobilization via sphingosine kinase in signalling by the Fc-epsilon-RI antigen receptor

Article Abstract:

The high affinity IgE receptors (Fc-epsilon-RI) mobilize calcium through a sphingosine kinase (SK) pathway. SK is activated by the antigen clustering of Fc-epsilon-RI on the rat mast-cell line and forms sphingosine-1-phosphate (S1P). S1P is responsible for the release of intracellular calcium. Suppression of SK by the sphingosine analogue, D-L-threo-dihydrosphingosine, inhibits calcium release induced by Fc-epsilon-RI.

Analysis, Calcium in the body, Calcium (Nutrient), Fc receptors

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Signalling through the high-affinity IgE receptor FcepsilonR1

Article Abstract:

The FcepsilonR1 complex forms a high-affinity cell-surface receptor for the Fc area of immunoglobulin E (IgE) molecules. FcepsilonR1 controls the activation of mast cells in humans and is involved in IgE-mediated antigen presentation, and is thus central to the induction and maintenance of an allergic response.

Allergy, Immunoglobulin E

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Structure of the Fc fragment of human IgE bound to its high-affinity receptor Fc epsilon RI alpha

Article Abstract:

The structure of the Fc fragment of human immunoglobulin-E bound to its receptor Fc epsilon RI alpha, is described.

Immunoglobulins

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