Identification of Calcium/Calmodulin-Dependent Phosphatase as the Dephosphorylating Enzyme of IgE-Dependent Histamine-Releasing Factor in RBL-2H3
IgE-dependent histamine-releasing factor(HRF) was initially described as a secretagogue for secretion of histamine from IgE+ basophils from a subset of allergic donors. Previously, we identified that S98 residue of HRF was phosphorylated using anti-HRFpS98 antibody which specifically recognizes the...
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Veröffentlicht in: | Han'gug mi'saengmul saengmyeong gong haghoeji 2005-09, Vol.33 (3), p.189-193 |
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Sprache: | kor |
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Zusammenfassung: | IgE-dependent histamine-releasing factor(HRF) was initially described as a secretagogue for secretion of histamine from IgE+ basophils from a subset of allergic donors. Previously, we identified that S98 residue of HRF was phosphorylated using anti-HRFpS98 antibody which specifically recognizes the phosphorylated serine residue of HRF and HRFS98A mutant construct. In vitro kinase assay, only wild type HRF was phosphorylated by PKC, and S98A HRF was not affected by PKC. In this study, we attempted to characterize the phosphatase which specifically dephosphorylates HRF by immunoprecipitation and pull-down assay. |
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ISSN: | 1598-642X |