Abstract
The localization of phorbol ester-sensitive phospholipase D (PLD) in baby hamster kidney cells has been investigated by determining the subcellular distribution of the phosphatidylbutanol produced when the cells are incubated with phorbol 12-myristate 13-acetate and n-butanol. Results derived by isolation of plasma membrane vesicles from intact cells or by subcellular fractionation on a sucrose density gradient suggest the PLD is specific for phosphatidylcholine and its primary site of action is not the plasma membrane but the endoplasmic reticulum.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetic Acid / metabolism
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Animals
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Butanols / pharmacology
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Cells, Cultured
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Centrifugation, Density Gradient
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Cholesterol / metabolism
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Choline / metabolism
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Chromatography, Thin Layer
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Cricetinae
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Endoplasmic Reticulum / enzymology*
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Ethanol / pharmacology
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Glycerophospholipids*
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Kidney
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Phosphatidic Acids / metabolism
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Phosphatidylcholines / metabolism
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Phospholipase D / metabolism*
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Phospholipids / analysis
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Phospholipids / metabolism
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Sphingomyelins / metabolism
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Tetradecanoylphorbol Acetate / pharmacology*
Substances
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Butanols
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Glycerophospholipids
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Phosphatidic Acids
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Phosphatidylcholines
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Phospholipids
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Sphingomyelins
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phosphatidylbutanol
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Ethanol
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Cholesterol
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Phospholipase D
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Choline
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Tetradecanoylphorbol Acetate
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Acetic Acid