A Possible Role of Tyrosine Kinases in the Regulation of Muscarinic Receptor-Activated Cation Channels in Guinea-Pig Ileum

書誌事項

公開日
1994-09
権利情報
  • https://www.elsevier.com/tdm/userlicense/1.0/
DOI
  • 10.1006/bbrc.1994.2339
公開者
Elsevier BV

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説明

We investigated the effects of inhibitors for tyrosine kinases and phosphatases on the muscarinic receptor-activated nonselective cationic current. With nystatin-perforated whole-cell recording, the tyrosine kinase inhibitor genistein (1 approximately 10 micrograms/ml) reduced the amplitude of currents evoked by iontophoretically applied acetylcholine in a dose-dependent manner, the maximum inhibition being to about 46% of the control. In contrast, daidzein (10 micrograms/ml), an inactive analog of genistein, exerted little effect. These effects were unchanged when the cationic current was activated by internal perfusion of GTP gamma S (50 microM) bypassing the muscarinic receptor. A potent phosphatase inhibitor, orthovanadate (30 approximately 100 microM), on the other hand, increased the GTP gamma S-induced cationic current. These results suggest that tyrosine phosphorylation may be essential to regulate the Ca mobilization associated with muscarinic receptor-operated nonselective cation channels.

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