Free fatty acids regulate the uncoupling protein and alternative oxidase activities in plant mitochondria

FEBS Lett. 1998 Aug 21;433(3):237-40. doi: 10.1016/s0014-5793(98)00922-3.

Abstract

Two energy-dissipating systems, an alternative oxidase and an uncoupling protein, are known to exist in plant mitochondria. In tomato fruit mitochondria linoleic acid, a substrate for the uncoupling protein, inhibited the alternative oxidase-sustained respiration and decreased the ADP/O ratio to the same value regardless of the level of alternative oxidase activity. Experiments with varying concentrations of linoleic acid have shown that inhibition of the alternative oxidase is more sensitive to the linoleic acid concentration than the uncoupling protein activation. It can be proposed that these dissipating systems work sequentially during the life of the plant cell, since a high level of free fatty acid-induced uncoupling protein activity excludes alternative oxidase activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carrier Proteins / metabolism*
  • Dithiothreitol / pharmacology
  • Fatty Acids, Nonesterified / pharmacology*
  • Guanosine Triphosphate / pharmacology
  • Ion Channels
  • Kinetics
  • Linoleic Acid / pharmacology
  • Membrane Proteins / metabolism*
  • Mitochondria / drug effects
  • Mitochondria / metabolism*
  • Mitochondrial Proteins
  • Oxidoreductases / metabolism*
  • Oxygen Consumption / drug effects
  • Plant Proteins
  • Potassium Cyanide / pharmacology
  • Pyruvic Acid / metabolism
  • Solanum lycopersicum / metabolism*
  • Uncoupling Protein 1

Substances

  • Carrier Proteins
  • Fatty Acids, Nonesterified
  • Ion Channels
  • Membrane Proteins
  • Mitochondrial Proteins
  • Plant Proteins
  • Uncoupling Protein 1
  • Pyruvic Acid
  • Guanosine Triphosphate
  • Linoleic Acid
  • Oxidoreductases
  • alternative oxidase
  • Potassium Cyanide
  • Dithiothreitol