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Mitochondrial contact sites: Their role in energy metabolism and apoptosis
Open accessAbstract
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.
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“Voltage-dependent anion channel is found at contact sites between the OMM and the IMM (101) where it may complex with energetics-related proteins, such as hexokinase, ANT, and creatine kinase, or with apoptotic proteins of the Bcl-2 family (18), and as noted above, and discussed below in greater detail, appears to play a central role in facilitating mitochondrial steroidogenic cholesterol”
From Adrenal Mitochondria and Steroidogenesis: From Individual Proteins to Functional Protein Assemblies (2016) · cites this paper as [18]
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“Contact sites are broken in ischaemia, but stabilized if HK2 dissociation is prevented As noted earlier, contact sites are thought to play an important role in transporting ATP generated within the mitochondria to the cytosol as phosphocreatine (PCr) (Brdiczka et al., 2006).”
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“In this case VDAC apparently exposes a different structural motif at the cytosolic side that provides lower affinity for hexokinase [17].”
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“Marked decrease in the activities of complexes II and IV have been reported to decrease the rates of mitochondrial respiration and ATP production.(44) Therefore, decreased activities of complexes II and IV observed in the MTX-treated enterocytes may cause reduced ATP production leading to impaired nutrient absorption…”
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“Alternatively the hypotonic treatment may have been required to form contact sites between the inner and outer membrane that allow changes at the outer membrane to be conveyed to the inner membrane [31].”
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Metadata
- Authors
- Brdiczka, D. G., Zorov, D. B., & Sheu, S.-S.
- Affiliations
- University of Rochester Medicine (US)
- Lomonosov Moscow State University (RU)
- Corresponding author
- Brdiczka, Dieter G.
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
- Publisher
- Elsevier BV
- Published
- 2006-02
- Volume
- 1762
- Issue
- 2
- Pages
- 148-163
- ISSN
- 0925-4439 (ISSN-L)
- OpenAlex
- W2114758506
- Cited by
- 150
- References
- 129
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 5 · 2023: 2 · 2022: 3 · 2021: 4 · 2020: 5 · 2019: 2 · 2018: 5 · 2017: 15 · 2016: 10 · 2015: 8 · 2014: 7 · 2013: 9 · 2012: 9
- FWCI
- 0.65
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 2759 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Heart Association (HL-33333, 0050839T)
- New York State Department of Health
- National Institutes of Health (0050839T)
- National Heart, Lung, and Blood Institute (HL 33333, R01HL033333)
- National Institute of Neurological Disorders and Stroke (NS-37710, R01NS037710)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- mitochondrial contact sites, mitochondrial bioenergetics, apoptosis, heart failure, voltage-dependent anion channel, adenine nucleotide translocase, mitochondrial calcium homeostasis, mitochondrial protein complexes, complex stabilization, calcium overload
- MeSH terms
- Mitochondrial ADP, ATP Translocases, Animals, Energy Metabolism, Mitochondria, Apoptosis, Cytochromes c, Mitochondrial Membranes
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