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Studies on the effect of the phosphorylated IgE-dependent histamine-releasing factor on Na,K-ATPase activity in HeLa cell

Title
Studies on the effect of the phosphorylated IgE-dependent histamine-releasing factor on Na,K-ATPase activity in HeLa cell
Authors
Kim J.-A.Ha H.Lee K.
Ewha Authors
이경림하헌주
SCOPUS Author ID
이경림scopus; 하헌주scopus
Issue Date
2005
Journal Title
Korean Journal of Microbiology and Biotechnology
ISSN
1598-642XJCR Link
Citation
vol. 33, no. 3, pp. 184 - 188
Indexed
SCOPUS; KCI scopus
Abstract
IgE-dependent histamine-releasing factor (HRF) is found extracellularly to regulate the degranulation process of histamine in mast cells and basophils and known to play a predominant role in the pathogenesis of chronic allergic disease. HRF has been also identified in the intracellular region of the cell. Previously, we reported that HRF interacts with the 3rd cytoplasmic domain of the alpha subunit of Na,K ATPase and inhibits Na,K-ATPase activity. The predicated phosphorylation site in HRF by PKC was mapped to one serine residues (S98) by the computer analysis. In this study, 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. We also performed 86Rb +-uptake assay to understand the role of HRF wild-type and HRFS98A mutants on the regulation of Na,K-ATPase activity. Dephosphorylation of HRF at serine 98 residue recovers slightly the inhibitory function of HRF, suggesting that phosphorylated HRF at serine 98 may not suppress the Na,K-ATPase activity.
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약학대학 > 약학과 > Journal papers
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