Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE
Volume 1688, Issue 2, Pages 95-101Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbadis.2003.11.007
Keywords
oxidative stress; mitochondrial dysftmction; carbonylation; nitration; 4-hydroxynonenal; lipid peroxidation adduct
Funding
- NIA NIH HHS [P02 AG10514, P30 AG024832] Funding Source: Medline
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Protein modifications, such as carbonylation, nitration and formation of lipid peroxidation adducts, e.g. 4-hydroxynonenal (HNE), are products of oxidative damage attributed to reactive oxygen species (ROS). The mitochondrial respiratory chain Complexes I and III have been shown to be a major source of ROS in vitro. Additionally, modifications of the respiratory chain Complexes (I-V) by nitration, carbonylation and HNE adduct decrease their enzymatic activity in vitro. However, modification of these respiratory chain complex proteins due to in vivo basal level ROS generation has not been investigated. In this study, we show a basal level of oxidative damage to specific proteins of adult bovine heart submitochondrial particle (SMP) complexes, and find that most of these proteins are localized in the mitochondrial matrix. We postulate that electron leakage from respiratory chain complexes and subsequent ROS formation may cause damage to specific complex subunits and contribute to long-term accumulation of mitochondrial dysfunction. (C) 2003 Elsevier B.V. All rights reserved.
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