Mitochondrial oxidative phosphorylation in autosomal dominant optic atrophy

• Type of Material: Article
• Authors: Vladimir I Mayorov, Mercer University; Angela J Lowrey, Mercer University; Valerie Biousse, Emory University; Nancy J Newman, Emory University; Susan D Cline, Mercer University; Michael D Brown, The Coca-Cola Company
• Language: English
• Date: 2008
• Publisher: BioMed Central
• Publication Version: Final Published Version
• Copyright Statement: © 2008 Mayorov et al
• License: Creative Commons Attribution 2.0 Generic
• Final Published Version (URL): http://www.biomedcentral.com/1471-2091/9/22
• Title of Journal or Parent Work: BMC Biochemistry
• ISSN: 1471-2091
• Volume: 9
• Start Page: 22
• End Page: 22
• Grant/Funding Information: We thank the patients and their families for their contributions, the National Eye Institute for support through grant award EY014393 (M.D.B./S.D.C.), and Research to Prevent Blindness (New York, NY) for an unrestricted grant to the Emory University School of Medicine Department of Ophthalmology.
• Research Categories: Biology, Neuroscience; Health Sciences, Opthamology

Abstract

Background Autosomal dominant optic atrophy (ADOA), a form of progressive bilateral blindness due to loss of retinal ganglion cells and optic nerve deterioration, arises predominantly from mutations in the nuclear gene for the mitochondrial GTPase, OPA1. OPA1 localizes to mitochondrial cristae in the inner membrane where electron transport chain complexes are enriched. While OPA1 has been characterized for its role in mitochondrial cristae structure and organelle fusion, possible effects of OPA1 on mitochondrial function have not been determined. Results Mitochondria from six ADOA patients bearing OPA1 mutations and ten ADOA patients with unidentified gene mutations were studied for respiratory capacity and electron transport complex function. Results suggest that the nuclear DNA mutations that give rise to ADOA in our patient population do not alter mitochondrial electron transport. Conclusion We conclude that the pathophysiology of ADOA likely stems from the role of OPA1 in mitochondrial structure or fusion and not from OPA1 support of oxidative phosphorylation.