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- W17503400 abstract "ABSTRACT Bridging of IgE-receptors by binding of divalent or multivalent antigen, or anti-IgE, to adjacent IgE molecules, or direct binding of anti-IgEreceptor antibody to the IgE-receptor, results in membrane perturbation, cell activation and release of granule mediators. Within 15 sec of coupled activation and secretion there occurs a transient monophasic rise in cAMP (100-150% over baseline). Pharmacologic manipulation of adenylate cyclase, using adenosine analogues which either inhibit or potentiate IgE-receptoragonist- linked activation of adenylate cyclase, results in either an inhibition or an increase in secretion of mediators, which correlates with an attenuation or increase in the monosphasic rise in cAMP, and an attenuation or no change in the extent of activation (20-30%) of the two isoenzymes of cAMP-dependent protein kinase (cAPK). Phosphodiesterase inhibitors also inhibit mediator release, and IgE-receptor perturbation in the presence of methylxanthines results in a rise in cAMP of 300-500% over baseline, as well as increased activation (50-100%) of both cAPK isoenzymes. Thus, prolonged elevation of cAMP and extensive activation of the protein kinases may have an antagonistic effect on mediator release, whereas transient elevation of cAMP and activation of cAPK in the range of 20-30% has an agonist function in mediator release. Possible sites of cAPK regulation of mast cell function will be discussed." @default.
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- W17503400 date "1983-01-01" @default.
- W17503400 modified "2023-09-26" @default.
- W17503400 title "IgE Receptor and cAMP in Mast Cell Activation" @default.
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- W17503400 doi "https://doi.org/10.1016/b978-0-08-029775-0.50089-4" @default.
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