Phosphatidylcholine turnover in activated human neutrophils. Agonist-induced cytidylyltransferase translocation is subsequent to phospholipase D activation

Phosphatidylcholine synthesis and degradation are tightly regulated to assure a constant amount of the phospholipid in cellular membranes. The chemotactic peptide fMLP and the phorbol ester, phorbol 12-myristate 13-acetate, are known to stimulate phosphatidylcholine degradation by phospholipase D in...

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Bibliographic Details
Published in:The Journal of biological chemistry 1995-06, Vol.270 (22), p.13138-13146
Main Authors: Tronchère, H, Planat, V, Record, M, Tercé, F, Ribbes, G, Chap, H
Format: Article
Language:English
Subjects:
Biological Transport
Catalysis
Choline - metabolism
Choline-Phosphate Cytidylyltransferase
Cytochalasin B - pharmacology
Enzyme Activation
Humans
Kinetics
N-Formylmethionine Leucyl-Phenylalanine - pharmacology
Neutrophil Activation
Neutrophils - cytology
Neutrophils - metabolism
Nucleotidyltransferases - agonists
Nucleotidyltransferases - metabolism
Oleic Acid
Oleic Acids - pharmacology
Phosphatidylcholines - biosynthesis
Phosphatidylcholines - metabolism
Phospholipase D - metabolism
Tetradecanoylphorbol Acetate - pharmacology
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Summary:Phosphatidylcholine synthesis and degradation are tightly regulated to assure a constant amount of the phospholipid in cellular membranes. The chemotactic peptide fMLP and the phorbol ester, phorbol 12-myristate 13-acetate, are known to stimulate phosphatidylcholine degradation by phospholipase D in human neutrophils. fMLP alone triggered phosphatidylcholine breakdown into phosphatidic acid, but did not stimulate phosphatidylcholine synthesis or activation of the rate-limiting enzyme CTP:phosphocholine cytidylyltransferase. Adding cytochalasin B to fMLP led to some conversion of phosphatidic acid into diglyceride, and fMLP was then able to trigger choline incorporation into phosphatidylcholine, and cytidylyltransferase translocation from cytosol to membranes. Inhibition of phosphatidyl-choline-phospholipase D activation with tyrphostin led to inhibition of choline incorporation. Therefore, phosphatidic acid-derived diglyceride but not phosphatidic acid alone was effective to promote cytidylyltransferase translocation. With phorbol 12-myristate 13-acetate as agonist, and by selective labeling of phosphatidylinositol and phosphatidylcholine, we demonstrated that only phosphatidylcholine-derived diglyceride participated in cytidylyltransferase translocation. Oleic acid stimulated phosphatidylcholine synthesis, but induced a weak increase in diglyceride and a slight cytidylyltransferase translocation, and did not stimulate phospholipase D activity. Our data established that only diglyceride derived from phosphatidylcholine degradation by the phospholipase D/phosphatidate phosphatase pathway are required for agonist-induced cytidylyltransferase translocation and subsequent choline incorporation into phosphatidylcholine.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.270.22.13138