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- W2017673826 abstract "The particulate-bound guanylate cyclase activity of Tetrahymena pyriformis was shown previously to be Ca2+-dependent and to be activated by an endogenous calmodulin-like protein (Tetrahymena Ca2+-binding protein, TCBP) [S. Nagao, Y. Suzuki, Y. Watanabe and Y. Nozawa, Biochem. biophys. Res. Commum.90, 261 (1979)]. Phenothiazine derivatives, such as chlorpromazine and trifluoperazine, that interact with calmodulin were found to inhibit the Ca2+-dependent guanylate cyclase activity and the TCBP-induced activation of the guanylate cyclase activity. Ethylene glycol-bis (β-aminoethyl ether)-N, N'-tetraacetic acid (EGTA), a Ca2+ chelator, also inhibited the activation of guanylate cyclase. However, the mechanisms by which EGTA and trifluoperazine act were different. The EGTA-induced inhibition could not be overcome by increasing the concentration of TCBP, whereas the trifluoperazine-induced inhibition could be overcome by increasing the concentration of TCBP, but not by increasing the concentration of Ca2+. These findings suggest that the mechanism by which trifluoperazine inhibits the activation of guanylate cyclase involves competition with TCBP." @default.
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- W2017673826 title "Effects of phenothiazines on the membrane-bound guanylate and adenylate cyclase in tetrahymena pyriformis" @default.
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- W2017673826 doi "https://doi.org/10.1016/0006-2952(81)90542-6" @default.
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