Mitochondrial Contact Sites: Their Role in Energy Metabolism and Apoptosis.
From: Department of Pharmacology and Physiology, Box 711, University of Rochester, School of Medicine and Dentistry, 601 Elmwood Avenue, Rochester, NY 14642, USA. dieter.brdiczka@uni-konstanz.de
Biochimica et biophysica acta
- Publish Date: Feb 2006
- ISSN: 0006-3002
- Volume: 1762
- Issue: 2
- Pages: 148-63
- Medium: Print
- Language: English
- Citation (JAMA): Brdiczka Dieter G, Zorov Dmitry B, Sheu Shey-Shing, et al. Mitochondrial Contact Sites: Their Role in Energy Metabolism and Apoptosis.. Biochim. Biophys. Acta Feb 2006;1762:148-63
Abstract
The energy metabolism of the failing heart is characterised by a 30% decrease of the total adenine nucleotides content and what may be more important by a 60% loss of creatine and creatine phosphate [J.S. Ingwall, R.G. Weiss, Is the failing heart energy starved? On using chemical energy to support cardiac function, Circ. Res. 95 (2004) 35-145]. Besides the effect of these changes on the energy supply, failing heart is known to be more vulnerable to Ca2+ overload and apoptosis-inducing processes. Recent studies have pointed to the critical role of mitochondrial contact sites in controlling both the mitochondrial energy metabolism and Ca2+ homeostasis. This review focuses on the structure and function of protein complexes in mitochondrial contact sites and their regulatory role in the cellular bioenergetics, intra- and extra-mitochondrial Ca2+ levels, and release of apoptosis-inducing factors. Firstly, we review the compositions of different contact sites following by the discussion of experimental data obtained with isolated and reconstituted voltage-dependent anion channel-adenine nucleotide translocase complexes and consequences of the complex disassembling. Furthermore, we describe experiments involving the complex-stabilizing conditions in vitro and in intact cells. At the end, we discuss unsolved problems and opportunities for clinical application of the complex-stabilizing factors.
Mesh Headings (Keywords): Animals, Apoptosis, Cytochromes c, Energy Metabolism, Mitochondria, Mitochondrial ADP, ATP Translocases, Mitochondrial Membranes
Check for Full Text / PubMed Unique Identifier (PMID): 16324828
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