Activation of alternative oxidase and uncoupling protein lowers hydrogen peroxide formation in amoeba Acanthamoeba castellanii mitochondria.

Abstract:

:Mitochondria of amoeba Acanthamoeba castellanii were used to determine the role of two energy-dissipating systems, i.e., a free fatty acid (FFA)-activated, purine nucleotide-inhibited uncoupling protein (AcUCP) and a FFA-insensitive, purine nucleotide-activated ubiquinol alternative oxidase (AcAOX), in decreasing reactive oxygen species production in unicellular organisms. It is shown that the activation of AcUCP by externally added FFA resulted in a strong decrease in H2O2 production, whilst the inhibition of the FFA acid-induced AcUCP activity by GDP or addition of bovine serum albumin (BSA) enhanced production of H2O2. Similarly, the activation of antimycin-resistant AcAOX-mediated respiration by GMP significantly lowered H2O2 production, while inhibition of the oxidase by benzohydroxamate cancelled the GMP-induced effect on H2O2 production. When active together, both energy-dissipating systems revealed a cumulative effect on decreasing H2O2 formation. The results suggest that protection against mitochondrial oxidative stress may be a physiological role of AOX and UCP in unicellulars, such as A. castellanii.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Czarna M,Jarmuszkiewicz W

doi

10.1016/j.febslet.2005.04.081

keywords:

subject

Has Abstract

pub_date

2005-06-06 00:00:00

pages

3136-40

issue

14

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(05)00576-4

journal_volume

579

pub_type

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