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Trifluoperazine and other anaesthetics inhibit rat liver CTP: phosphocholine cytidylyltransferase
Author(s) -
Pelech Steven L.,
Jetha Fateem,
Vance Dennis E.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80682-6
Subject(s) - trifluoperazine , phosphocholine , biochemistry , phosphatidylcholine , chlorpromazine , chemistry , enzyme , cytosol , phosphorylcholine , microsome , biosynthesis , phospholipid , endoplasmic reticulum , biology , pharmacology , calmodulin , membrane
Chlorpromazine (25 μM) and trifluoperazine (25 μM) inhibited by 5‐fold the activity of CTP: phosphocholine cytidylyltransferase, the rate‐limiting enzyme for phosphatidylcholine biosynthesis, in rat liver cytosol. Addition of saturating amounts of rat liver phospholipid to the enzyme assay rapidly reversed the drug‐mediated inhibition. Three‐fold or greater concentrations of these drugs were required to produce a 50% inhibition of the microsomal cytidylyltransferase. Incubation of rat hepatocytes with 20 μM trifluoperazine or chlorpromazine did not inhibit phosphatidylcholine biosynthesis. These results provide additional evidence for the hypothesis that the active form of cytidylyltransferase is on the endoplasmic reticulum and the enzyme in cytosol appears to be latent.