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- Title
Activation of Fc epsilon RI inhibits the pyruvate kinase through direct interaction with the gamma-chain.
- Authors
Oak, M H; Cheong, H; Kim, K M
- Abstract
The downstream signaling components of high-affinity IgE receptor (FcepsilonRI) were studied using yeast two-hybrid screening of the cDNA library constructed from RBL-2H3 cells. The cytoplasmic part of the gamma-chain but not that of the beta-chain was found to interact with pyruvate kinase in the yeast. The in-vitro-translated pyruvate kinase also specifically interacted with the bacterially expressed glutathione-S transferase fusion protein of the cytoplasmic part of the gamma-chain. When RBL-2H3 cells were challenged with antigen, the activity of pyruvate kinase gradually decreased, reaching the minimum activity around 5 min after the activation, and then slowly returned to the normal level. The dose-response curve (antigen vs. pyruvate kinase activity) plotted at 5 min after stimulation showed that the pyruvate kinase was dose-dependently inhibited and the maximum inhibition was reached at the concentration of 0.1 microgram/ml of antigen. Direct interaction between FcepsilonRI and pyruvate kinase was also demonstrated by co-immunoprecipitation in RBL-2H3 cells. These data suggest that pyruvate kinase is functionally linked with FcepsilonRI and might exert an important role in controlling cellular functions following the activation of FcepsilonRI.
- Publication
International archives of allergy and immunology, 1999, Vol 119, Issue 2, p95
- ISSN
1018-2438
- Publication type
Journal Article
- DOI
10.1159/000024183