Phorbol ester selectively stimulates the phospholipase D-mediated hydrolysis of phosphatidylethanolamine in multidrug-resistant MCF-7 human breast carcinoma cells

The phospholipase D (PLD)-mediated synthesis of phosphatidylethanol (PtdEtOH) and the hydrolysis of phosphatidylethanolamine (PtdEtn) and phosphatidylcholine (PtdCho) were examined in drug-sensitive and multidrug-resistant lines of MCF-7 human breast carcinoma cells. In drug-sensitive (MCF-7/WT) cel...

Full description

Saved in:
Bibliographic Details
Published in:Biochemical journal 1994-09, Vol.302 (3), p.649-654
Main Authors: KISS, Z, TOMONO, M, ANDERSON, W. B
Format: Article
Language:English
Subjects:
Biological and medical sciences
Breast Neoplasms - metabolism
Drug Resistance, Multiple
Glycerophospholipids
Glycerylphosphorylcholine - biosynthesis
Gynecology. Andrology. Obstetrics
Humans
Hydrogen Peroxide - pharmacology
Hydrolysis - drug effects
Mammary gland diseases
Medical sciences
Phosphatidic Acids - biosynthesis
Phosphatidylcholines - metabolism
Phosphatidylethanolamines - biosynthesis
Phosphatidylethanolamines - metabolism
Phospholipase D - metabolism
Sphingosine - pharmacology
Tetradecanoylphorbol Acetate - pharmacology
Tumor Cells, Cultured
Tumors
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The phospholipase D (PLD)-mediated synthesis of phosphatidylethanol (PtdEtOH) and the hydrolysis of phosphatidylethanolamine (PtdEtn) and phosphatidylcholine (PtdCho) were examined in drug-sensitive and multidrug-resistant lines of MCF-7 human breast carcinoma cells. In drug-sensitive (MCF-7/WT) cells, the protein kinase C (PKC) activator phorbol 12-myristate 13-acetate (PMA) failed to enhance either the synthesis of PtdEtOH or the hydrolysis of either phospholipid. In the drug-resistant (MCF-7/MDR) cells, 100 nM PMA greatly enhanced both the synthesis of PtdEtOH (approximately 21-fold) and the hydrolysis of PtdEtn (approximately 29-fold), but had no effect on the hydrolysis of PtdCho. The PLD activators sphingosine and H2O2 were found to elicit only a slight (1.28-1.4-fold) stimulatory effect on PtdCho hydrolysis in both the MCF-7/WT and MCF-7/MDR cell types, and had only a small effect on PtdEtn hydrolysis in the MCF-7/WT cells as well. However, these agents significantly (approximately 2.6-3.5-fold) stimulated PtdEtn hydrolysis in the MCF-7/MDR cells. These data indicate that MCF-7/MDR cells contain a PtdEtn-specific PLD activity which can be selectively stimulated by PMA, sphingosine and H2O2.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj3020649