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  • 1
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    Online Resource
    Oligomeric C‐terminal truncated Bax preferentially releases cytochrome c but not adenylate kinase from mitochondria, outer membrane vesicles and proteoliposomes
    Wiley ; 2001
    In:  FEBS Letters Vol. 505, No. 3 ( 2001-09-21), p. 453-459
    Details
    In: FEBS Letters, Wiley, Vol. 505, No. 3 ( 2001-09-21), p. 453-459
    Abstract: The mechanism by which the proapoptotic protein Bax releases cytochrome c from mitochondria is not fully understood. The present work approaches this problem using C‐terminal truncated oligomeric Bax (BaxΔC). Micromolar concentrations of BaxΔC released cytochrome c from isolated rat heart and liver mitochondria, while the release of adenylate kinase was not significantly affected. BaxΔC also released cytochrome c but not adenylate kinase from outer membrane vesicles filled with these proteins. However, BaxΔC was ineffective in releasing cytochrome c when outer membrane vesicles were obtained in the presence of glycerol, conditions under which the number of contact sites was drastically reduced. BaxΔC did not liberate encapsulated cytochrome c and adenylate kinase from pure phospholipid vesicles or vesicles reconstituted with porin. However, when the hexokinase–porin–adenine nucleotide translocase complex from brain mitochondria was reconstituted in vesicles, BaxΔC released internal cytochrome c but not adenylate kinase. In all these systems, only a small portion of total cytochrome c present in either mitochondria or vesicles could be liberated by BaxΔC. BaxΔC also increased the accessibility of external cytochrome c to either oxidation by complex IV or reduction by complex III in intact liver and heart mitochondria. Conclusions: (1) BaxΔC selectively releases cytochrome c and enables a bidirectional movement of cytochrome c across the outer mitochondrial membrane. (2) A multiprotein complex that resembles the mitochondrial contact sites is a prerequisite for BaxΔC action. (3) A limited pool of cytochrome c becomes the first target for BaxΔC.
    Type of Medium: Online Resource
    ISSN: 0014-5793 , 1873-3468
    URL: Article
    DOI: 10.1016/S0014-5793(01)02858-7
    RVK:
    WA 15000
    Language: English
    Publisher: Wiley
    Publication Date: 2001
    detail.hit.zdb_id: 1460391-3
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  • 2
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    Inhibition of adenine nucleotide transport through the mitochondrial porin by a synthetic polyanion
    Wiley ; 1988
    In:  FEBS Letters Vol. 231, No. 1 ( 1988-04-11), p. 75-80
    Details
    In: FEBS Letters, Wiley, Vol. 231, No. 1 ( 1988-04-11), p. 75-80
    Abstract: The effect of a synthetic polyanion of M r 10 000 (a copolymer of methacrylate, maleate and styrene in a 1:2:3 proportion) was studied on isolated rat liver mitochondria and on mitochondrial porin reconstituted into lipid bilayer membranes. Increasing concentrations of the polyanion inhibited the adenyl kinase located between both mitochrondrial membranes in a dose‐dependent fashion. Upon addition of the detergent digitonin in increasing concentrations the adenyl kinase activity was fully reversible. In reconstitution experiments with mitochondrial porin the polyanion increased the voltage dependence of the pore in such a way that the pore is switched into the closed state at much smaller voltages than in the absence of the polyanion. The asymmetric addition of the polyanion resulted in an asymmetric shift of the voltage‐dependence of the pore. If the voltage is negative at the cis ‐side (the side of the addition of the polyanion) the pore closed rapidly whereas it was always open for potentials of opposite polarity. The results are discussed on the basis of a modification of the gate properties of the mitochondrial porin by the polyanion and by the assumption that the closed state of the pore is not permeable for nucleotides.
    Type of Medium: Online Resource
    ISSN: 0014-5793 , 1873-3468
    URL: Article
    DOI: 10.1016/0014-5793(88)80706-3
    RVK:
    WA 15000
    Language: English
    Publisher: Wiley
    Publication Date: 1988
    detail.hit.zdb_id: 1460391-3
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  • 3
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    Online Resource
    Intra‐ and Extramitochondrial Isozymes of (NADP) Malate Dehydrogenase
    Wiley ; 1971
    In:  European Journal of Biochemistry Vol. 19, No. 4 ( 1971-04), p. 546-551
    Details
    In: European Journal of Biochemistry, Wiley, Vol. 19, No. 4 ( 1971-04), p. 546-551
    Abstract: The intracellular distribution of (NADP) malate dehydrogenase (decarboxylating) was studied by means of fractional extraction of extra‐ and intramitochondrial enzymes in various tissues of mouse, rat, rabbit, guinea pig, pig, beef, sea gull and pigeon. Absolute activity levels of (NADP) malate dehydrogenase in the same tissues of different species vary greatly. In white adipose tissue and adrenal medulla, (NADP) malate dehydrogenase is located exclusively within the extramitochondrial compartment. In liver, 95% of (NADP) malate dehydrogenase activity is extramitochondrial and only 5% intramitochondrial. Mitochondrial subfractionation reveals a location of this enzyme within the inner mitochondrial compartment. Brain, heart, adrenal cortex and kidney also contain extra‐ and intramitochondrial (NADP) malate dehydrogenase. In kidney and adrenal cortex, the ratio of extra‐ and intramitochondrial isozymes varies between different species. In heart, a relatively constant distribution is found, i. e. 30% of the enzyme activity is extramitochondrial and 70% is intramitochondrial. Extra‐ and intramitochondrial (NADP) malate dehydrogenases show different electrophoretic mobility in all tissues examined and can be characterized as two distinct isoenzymes. Extra‐ and intramitochondrial isozymes of (NADP) malate dehydrogenase are probably related to different metabolic functions in various tissues, e. g. extra‐intramitochondrial hydrogen transfer (malate shuttle) or transhydrogenation reactions.
    Type of Medium: Online Resource
    ISSN: 0014-2956 , 1432-1033
    URL: Issue
    URL: Article
    DOI: 10.1111/ejb.1971.19.issue-4
    DOI: 10.1111/j.1432-1033.1971.tb01347.x
    RVK:
    WA 15000
    Language: English
    Publisher: Wiley
    Publication Date: 1971
    detail.hit.zdb_id: 1398347-7
    detail.hit.zdb_id: 2172518-4
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  • 4
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    ATPase Activities, Ca2+ Transport and Phosphoprotein Formation in Sarcoplasmic Reticulum Subfractions of Fast and Slow Rabbit Muscles
    Wiley ; 1977
    In:  European Journal of Biochemistry Vol. 81, No. 2 ( 1977-12), p. 211-222
    Details
    In: European Journal of Biochemistry, Wiley, Vol. 81, No. 2 ( 1977-12), p. 211-222
    Type of Medium: Online Resource
    ISSN: 0014-2956 , 1432-1033
    URL: Issue
    URL: Article
    DOI: 10.1111/ejb.1977.81.issue-2
    DOI: 10.1111/j.1432-1033.1977.tb11943.x
    RVK:
    WA 15000
    Language: English
    Publisher: Wiley
    Publication Date: 1977
    detail.hit.zdb_id: 1398347-7
    detail.hit.zdb_id: 2172518-4
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  • 5
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    Complexes between kinases, mitochondrial porin and adenylate translocator in rat brain resemble the permeability transition pore
    Wiley ; 1996
    In:  FEBS Letters Vol. 396, No. 2-3 ( 1996-11-04), p. 189-195
    Details
    In: FEBS Letters, Wiley, Vol. 396, No. 2-3 ( 1996-11-04), p. 189-195
    Abstract: In vitro incubation of isolated hexokinase isozyme I or isolated dimer of mitochondrial creatine kinase with the outer mitochondrial membrane pore led to high molecular weight complexes of enzyme oligomers. Similar complexes of hexokinase and mitochondrial creatine kinase could be extracted by 0.5% Triton X‐100 from homogenates of rat brain. Hexokinase and creatine kinase complexes could be separated by subsequent chromatography on DEAE anion exchanger. The molecular weight, as determined by gel‐permeation chromatography, was approximately 400 kDa for both complexes. The M r suggested tetramers of hexokinase (monomer 100 kDa) and creatine kinase (active enzyme is a dimer of 80 kDa). The composition of the complexes was further characterised by specific antibodies. Besides either hexokinase or creatine kinase molecules the complexes contained porin and adenylate translocator. It was possible to incorporate the complexes into artificial bilayer membranes and to measure conductance in 1 M KCl. The incorporating channels had a high conductance of 6 nS that was asymmetrically voltage dependent. The complexes were also reconstituted in phospholipid vesicles that were loaded with ATP. Complex containing vesicles retained ATP while vesicles reconstituted with pure porin were leaky. The internal ATP could be used by creatine kinase and hexokinase in the complex to phosphorylate external creatine or glucose. This process was inhibited by atractyloside. The hexokinase complex containing vesicles were furthermore loaded with malate or ATP that was gradually released by addition of Ca 2+ between 100 and 600 μM. The liberation of malate or ATP by Ca 2+ could be inhibited by N ‐methylVal‐4‐cyclosporin, suggesting that the porin translocator complex constitutes the permeability transition pore. The results show the physiological existence of kinase porin translocator complexes at the mitochondrial surface. It is assumed that such complexes between inner and outer membrane components are the molecular basis of contact sites observed by electron microscopy. Kinase complex formation may serve three regulatory functions, firstly regulation of the kinase activity, secondly stimulation of oxidative phosphorylation and thirdly regulation of the permeability transition pore.
    Type of Medium: Online Resource
    ISSN: 0014-5793 , 1873-3468
    URL: Article
    DOI: 10.1016/0014-5793(96)01092-7
    RVK:
    WA 15000
    Language: English
    Publisher: Wiley
    Publication Date: 1996
    detail.hit.zdb_id: 1460391-3
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  • 6
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    Long‐chain fatty acids promote opening of the reconstituted mitochondrial permeability transition pore
    Wiley ; 2000
    In:  FEBS Letters Vol. 484, No. 2 ( 2000-11-03), p. 61-64
    Details
    In: FEBS Letters, Wiley, Vol. 484, No. 2 ( 2000-11-03), p. 61-64
    Abstract: Adenine nucleotide translocase–porin–hexokinase complex isolated from rat brain, when reconstituted into phospholipid‐cholesterol vesicles, exhibits all properties of the mitochondrial permeability transition pore [Beutner, G., Rück, A., Riede, B., Welte, W. and Brdiczka, D. (1996) FEBS Lett. 396, 189–195]. In the present work, the effect of long‐chain fatty acids on such reconstituted pore was examined. Opening of the pore was measured by leakage of either malate or fluorescein sulphonate entrapped inside the vesicles. It was found that myristate and oleate in the presence of 50 or 100 μM Ca 2+ produced a partial release of the probes in a dose‐dependent way. A dicarboxylic fatty acid analogue, that appeared inactive as protonophore in intact mitochondria, exerted no effect on pore opening in the reconstituted system. 100 μM Ca 2+ alone was without effect. Pore opening by fatty acids in the reconstituted system was partly prevented by cyclosporin A. The pore opening also occurred when the vesicles were incubated in the presence of pancreatic phospholipase A 2 . In this case, the opening was decreased by cyclosporin A or serum albumin. These results indicate that long‐chain fatty acids elicit opening of the permeability transition pore reconstituted in phospholipid vesicles in a similar way as in intact mitochondria [Wiȩckowski, M.R. and Wojtczak, L. (1998) FEBS Lett. 423, 339–342].
    Type of Medium: Online Resource
    ISSN: 0014-5793 , 1873-3468
    URL: Article
    DOI: 10.1016/S0014-5793(00)02127-X
    RVK:
    WA 15000
    Language: English
    Publisher: Wiley
    Publication Date: 2000
    detail.hit.zdb_id: 1460391-3
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  • 7
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    Online Resource
    Reconstituted adenine nucleotide translocase forms a channel for small molecules comparable to the mitochondrial permeability transition pore
    Wiley ; 1998
    In:  FEBS Letters Vol. 426, No. 1 ( 1998-04-10), p. 97-101
    Details
    In: FEBS Letters, Wiley, Vol. 426, No. 1 ( 1998-04-10), p. 97-101
    Abstract: Highly purified adenylate translocase (ANT) from rat heart mitochondria was functionally reconstituted as ATP/ADP exchange carrier in asolectin/cardiolipin vesicles. The ANT preparations used were free of porin, cyclophilin D, and Bax as analysed immunologically and by activity measurements. After pre‐loading the ANT‐containing proteoliposomes with ATP, malate or AMP, a gradual release of the trapped compounds by increasing the external Ca 2+ concentrations could be demonstrated. N ‐Methyl‐Val‐4‐cyclosporin did not inhibit the Ca 2+ dependent release of internal substances from ANT liposomes. This inhibitor was found to be specific for the mitochondrial permeability transition pore (MTP) in intact mitochondria or reconstituted MTP‐like protein complexes (e.g. hexokinase, porin, ANT complex). However, ADP in concentrations 〉 20 μM inhibited the liberation of internal compounds, while in contrast, atractyloside (30 μM) and HgCl 2 (5 μM) both induced permeability of the ANT‐containing liposomes resulting in a release of trapped substances. These results strongly suggest that ANT itself is capable to adopt a pore‐like structure under conditions known to induce the permeability transition in mitochondria.
    Type of Medium: Online Resource
    ISSN: 0014-5793 , 1873-3468
    URL: Article
    DOI: 10.1016/S0014-5793(98)00317-2
    RVK:
    WA 15000
    Language: English
    Publisher: Wiley
    Publication Date: 1998
    detail.hit.zdb_id: 1460391-3
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  • 8
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    Online Resource
    The molecular structure of mitochondrial contact sites. Their role in regulation of energy metabolism and permeability transition
    Wiley ; 1998
    In:  BioFactors Vol. 8, No. 3-4 ( 1998-01), p. 235-242
    Details
    In: BioFactors, Wiley, Vol. 8, No. 3-4 ( 1998-01), p. 235-242
    Abstract: Contact sites between the outer and peripheral inner membrane of mitochondria are involved in protein precursor uptake and energy transfer. Hexokinase and mitochondrial creatine kinase could be attributed by different techniques to the energy transfer contacts. Kinetic analyses suggested a functional interaction between the kinases, outer membrane pore protein, and inner membrane adenylate translocator (ANT). This suggestion was strongly supported by isolation of hexokinase and creatine kinase complexes that were constituted of kinase oligomers, porin and ANT. Phospholipid vesicles carrying reconstituted kinase—porin—ANT complexes enclosed internal ATP in contrast to vesicles containing free porin only. This indicated that unspecific transport through porin was regulated by its interaction with a specific antiporter, ANT. A direct interaction between porin and ANT in the hexokinase complex conferred the reconstituted system with permeability properties reminiscent of the mitochondrial permeability transition (PT) pore. In the creatine kinase complex this interaction between porin and ANT was replaced by contact of both with the kinase octamer. Thus PT‐pore‐like functions were not observed unless the creatine kinase octamer was dissociated, suggesting that the ANT was locked in the antiporter state by interaction with the octamer. Indeed, reconstituted pure ANT showed PT‐pore‐like properties concerning Ca 2+ sensitivity. However, as cyclophilin was missing, sensitivity against cyclosporin was not observed.
    Type of Medium: Online Resource
    ISSN: 0951-6433 , 1872-8081
    URL: Issue
    URL: Article
    DOI: 10.1002/biof.v8:3/4
    DOI: 10.1002/biof.5520080311
    Language: English
    Publisher: Wiley
    Publication Date: 1998
    detail.hit.zdb_id: 2011592-1
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  • 9
    Online Resource
    Online Resource
    Some new aspects of creatine kinase (CK): compartmentation, structure, function and regulation for cellular and mitochondrial bioenergetics and physiology
    Wiley ; 1998
    In:  BioFactors Vol. 8, No. 3-4 ( 1998-01), p. 229-234
    Details
    In: BioFactors, Wiley, Vol. 8, No. 3-4 ( 1998-01), p. 229-234
    Abstract: Creatine kinase (CK) isoenzymes, specifically located at places of energy demand and energy production, are linked by a phosphocreatine/creatine (PCr/Cr) circuit, found in cells with intermittently high energy demands. Cytosolic CKs, in close conjunction with Ca 2+ ‐pumps, play a crucial role for the energetics of Ca 2+ ‐homeostasis. Mitochondrial Mi‐CK, a cuboidal‐shaped octamer with a central channel, binds and crosslinks mitochondrial membranes and forms a functionally coupled microcompartment with porin and adenine nucleotide translocase for vectorial export of PCr into the cytosol. The CK system is regulated by AMP‐activated protein kinase via PCr/Cr and ATP/AMP ratios. Mi‐CK stabilizes and cross‐links cristae‐ or inner/outer membranes to form parallel membrane stacks and, if overexpressed due to creatine depletion or cellular energy stress, forms those crystalline intramitochondrial inclusions seen in some mitochondrial cytopathy patients. Mi‐CK is a prime target for free radical damage by peroxynitrite. Mi‐CK octamers, together with CK substrates have a marked stabilizing and protective effect against mitochondrial permeability transition pore opening, thus providing a rationale for creatine supplementation of patients with neuromuscular and neurodegenerative diseases.
    Type of Medium: Online Resource
    ISSN: 0951-6433 , 1872-8081
    URL: Issue
    URL: Article
    DOI: 10.1002/biof.v8:3/4
    DOI: 10.1002/biof.5520080310
    Language: English
    Publisher: Wiley
    Publication Date: 1998
    detail.hit.zdb_id: 2011592-1
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  • 10
    Online Resource
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    Mass spectrometric mapping of ion channel proteins (porins) and identification of their supramolecular membrane assembly
    Wiley ; 1998
    In:  Proteins: Structure, Function, and Genetics Vol. 33, No. S2 ( 1998), p. 63-73
    Details
    In: Proteins: Structure, Function, and Genetics, Wiley, Vol. 33, No. S2 ( 1998), p. 63-73
    Type of Medium: Online Resource
    ISSN: 0887-3585 , 1097-0134
    URL: Issue
    URL: Journal
    URL: Article
    DOI: 10.1002/(SICI)1097-0134(1998)33:2+〈〉1.0.CO;2-L
    DOI: 10.1002/(ISSN)1097-0134
    DOI: 10.1002/(SICI)1097-0134(1998)33:2+〈63::AID-PROT8〉3.0.CO;2-I
    RVK:
    WA 15000
    Language: English
    Publisher: Wiley
    Publication Date: 1998
    detail.hit.zdb_id: 1475032-6
    SSG: 12
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