The DOI matches its Crossref record; 131 of the 131 references it cites were found in a registry or an index.
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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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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