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The phospholipid analogue hexadecylphosphocholine inhibits phosphatidylcholine biosynthesis in Madin—Darby canine kidney cells
Author(s) -
Haase Rüdiger,
Wieder Thomas,
Geilen Christoph C.,
Reutter Werner
Publication year - 1991
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(91)81018-4
Subject(s) - phosphatidylcholine , phosphocholine , phospholipid , choline , phosphatidylethanolamine , choline kinase , biosynthesis , biochemistry , enzyme , in vitro , chemistry , biology , membrane
The influence of the phospholipid analogue hexadecylphosphocholine on phosphatidylcholine biosynthesis was investigated in Madin—Darby canine kidney (MDCK) cells. It inhibits the incorporation rate of [ methyl ‐ 3 H]choline into phosphatidylcholine at a concentration of 50 μM by about 50%. The radiolabelled precursor accumulates in the phosphocholine pool indicating that hexadecylphosphocholine inhibits the formation of phosphatidylcholine via the CDP‐choline pathway at the level of the rate‐limiting enzyme, CTP:phosphocholine cytidylyl transferase (EC 2.7.7.15). This was verified by the determination of the activity of the enzyme in vitro. In consequence of its inhibitory effect it could be shown that the treatment of MDGK cells for 24 h with 50 μM hexadecylphosphocholine induces alterations of the phospholipid composition. Whereas in treated cells the relative phosphatidylcholine content was decreased from the control level of 36.0±0.9% to 29.9±0.2%; in contrast, the relative content of phosphatidylethanolamine was increased from 19.3±0.9% to 24.3±0.9%.