期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1981
卷号：78
期号：11
页码：6812-6816
DOI：10.1073/pnas.78.11.6812
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Bridging of IgE receptors on normal rat mast cells by divalent anti-receptor antibodies induced phospholipid methylation and an increase in intracellular cyclic AMP within 15 sec after the receptor bridging. These biochemical events were followed by Ca2+ influx and histamine release. When IgE receptors on isolated plasma membranes were bridged by the antibody, both the increase in the incorporation of [3H]methyl into lipid fraction and the synthesis of cyclic AMP were demonstrated. The synthesis of cyclic AMP in this system was enhanced in the presence of GTP. The results indicated that the bridged IgE receptors are linked to both methyltransferases and adenylate cyclase [ATP pyrophosphate-lyase (cyclizing), EC 4.6.1.1 ] in the plasma membrane. An increase in cyclic AMP prior to receptor bridging suppressed phospholipid methylation in the plasma membrane, Ca2+ uptake, and subsequent histamine release. On the other hand, inhibition of phospholipid methylation by (S)-isobutyryl-3-deazaadenosine resulted in the suppression of cyclic AMP synthesis in the plasma membrane. These findings suggest that the activation of phospholipid methylation and the activation of adenylate cyclase are e, and subsequent histamine release. On the other hand, inhibition of phospholipid methylation by (S)-isobutyryl-3-deazadenosine resulted in the suppression of cyclic AMP synthesis in the plasma membrane. These findings suggest that the activation of phospholipid methylation and the activation of adenylate cyclase are e, and subsequent histamine release. On the other hand, inhibition of phospholipid methylation by (S)-isobutyryl-3-deazadenosine resulted in the suppression of cyclic AMP synthesis in the plasma membrane. These findings suggest that the activation of phospholipid methylation and the activation of adenylate cyclase are mutually regulated.
