Phorbol ester-sensitive phospholipase D is mainly localized in the endoplasmic reticulum of BHK cells

Biochem J. 1996 Dec 15;320 ( Pt 3)(Pt 3):885-90. doi: 10.1042/bj3200885.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetic Acid / metabolism
  • Animals
  • Butanols / pharmacology
  • Cells, Cultured
  • Centrifugation, Density Gradient
  • Cholesterol / metabolism
  • Choline / metabolism
  • Chromatography, Thin Layer
  • Cricetinae
  • Endoplasmic Reticulum / enzymology*
  • Ethanol / pharmacology
  • Glycerophospholipids*
  • Kidney
  • Phosphatidic Acids / metabolism
  • Phosphatidylcholines / metabolism
  • Phospholipase D / metabolism*
  • Phospholipids / analysis
  • Phospholipids / metabolism
  • Sphingomyelins / metabolism
  • Tetradecanoylphorbol Acetate / pharmacology*

Substances

  • Butanols
  • Glycerophospholipids
  • Phosphatidic Acids
  • Phosphatidylcholines
  • Phospholipids
  • Sphingomyelins
  • phosphatidylbutanol
  • Ethanol
  • Cholesterol
  • Phospholipase D
  • Choline
  • Tetradecanoylphorbol Acetate
  • Acetic Acid