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  • 1
    Online Resource
    Online Resource
    Mitochondrial Diseases : Theory, Diagnosis and Therapy (2021)
    Cham :Springer International Publishing :
    Details
    Keywords: Medicine Research. ; Biology Research. ; Medical sciences. ; Genetics. ; Biochemistry. ; Neurosciences. ; Biomedical Research. ; Health Sciences. ; Genetics and Genomics. ; Biochemistry. ; Neuroscience.
    Description / Table of Contents: Chapter 1. MTOCHONRIAL NEUROLOGY: A TALE OF TWO GENOMES (Salvatore DiMauro and Emanuele Barca) -- Chapter 2. Mutations in assembly factors required for the biogenesis of mitochondrial respiratory chain (Cristina Cerqua, Lisa Buson and Eva Trevisson) -- Chapter 3. Mitochondrial DNA: defects, maintenance genes and depletion (Miguel A. Fernández-Moreno, Luis Vázquez-Fonseca, Sara Palacios Zambrano and Rafael Garesse) -- Chapter 4. Mitochondrial translation deficiencies (Veronika Boczonadi, Juliane S. Müller and Rita Horvath) -- Chapter 5. Mitochondria dynamics: definition, players and associated disorders (Maria EugeniaSoriano, Marta Carro Alvarellos, Giovanni Rigoni, and Luca Scorrano) -- Chapter 6. Coenzyme Q biosynthesis disorders (Gloria Brea-Calvo, María Alcázar-Fabra, Eva Trevisson and Plácido Navas) -- Chapter 7. Cytochrome c defects in human disease (Leonardo Salviati) -- Chapter 8. Biochemical diagnosis of mitocondrial disorders (Delia Yubero, Raquel Montero, Rafael Artuch) -- Chapter 9. Molecular genetics in the Next Generation Sequencing era (Joaquin Dopazo) -- Chapter 10. Model cells and organisms in mitochondrial diseases (Rhoda Stefanatos, Alberto Sanz, Daniel J M Fernandez-Ayala) -- Chapter 11. Therapies approaches in mitochondrial diseases (Valentina Emmanuele, Catarina M Quinzii, and Michio Hirano).
    Abstract: Mitochondrial diseases comprise a clinically and genetically heterogeneous group of rare disorders that may affect virtually any system of the body at any age. Due to their complexity, understanding and diagnosing these diseases requires a multidisciplinary approach. This book provides an update on the major features of human mitochondrial diseases: genetic bases, pathophysiology, diagnosis, and treatment, and of the new technologies involved in the diagnosis and on the characterization of patients. The 11 chapters examine the unique complex interactions between the mitochondrial and the nuclear genomes involved in the biogenesis and the regulation of the mitochondrial respiratory chain, and their relevance to human disease. We discuss the traditional biochemical and genetic approaches, as well as the new omic technologies, and the cellular and animal models used in mitochondrial research. The last chapter is dedicated to the current treatment options. Authors are worldwide experts in these fields and integrate expertise in both basic science and clinical research. This book is particularly important for both scientists and clinicians interested in the diagnosis and treatment of these diseases.
    Type of Medium: Online Resource
    Pages: VI, 305 p. 29 illus., 23 illus. in color. , online resource.
    Edition: 1st ed. 2021.
    ISBN: 9783030701475
    URL: https://doi.org/10.1007/978-3-030-70147-5
    DOI: 10.1007/978-3-030-70147-5
    DDC: 610.72
    Language: English
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  • 2
    Electronic Resource
    Electronic Resource
    Resveratrol improves health and survival of mice on a high-calorie diet (2006)
    [s.l.] : Nature Publishing Group
    Nature 444 (2006), S. 337-342 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Resveratrol (3,5,4′-trihydroxystilbene) extends the lifespan of diverse species including Saccharomyces cerevisiae, Caenorhabditis elegans and Drosophila melanogaster. In these organisms, lifespan extension is dependent on Sir2, a conserved deacetylase proposed to underlie the beneficial ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nature05354
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  • 3
    Electronic Resource
    Electronic Resource
    The Role of Ascorbate in Biomembrane Energetics (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 498 (1987), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1987.tb23759.x
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  • 4
    Electronic Resource
    Electronic Resource
    Extracellular ascorbate stabilization as a result of transplasma electron transfer inSaccharomyces cerevisiae (1995)
    Springer
    Journal of bioenergetics and biomembranes 27 (1995), S. 597-603 
    Details
    ISSN: 1573-6881
    Keywords: Saccharomyces ; ascorbate stabilization ; plasma membrane
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The presence of yeast cells in the incubation medium prevents the oxidation of ascorbate catalyzed by copper ions. Ethanol increases ascorbate retention. Pyrazole, an alcohol dehydrogenase inhibitor, prevents ascorbate stabilization by cells. Chelation of copper ions does not account for stabilization, since oxidation rates with broken or boiled cells or conditioned media are similar to control rates in the absence of cells. Protoplast integrity is needed to reach optimal values of stabilization. Chloroquine, a known inhibitor of plasma membrane redox systems, inhibits the ascorbate stabilization, the inhibition being partially reversed by coenzyme Q6. Chloroquine does not inhibit ferricyanide reduction. Growth of yeast in iron-deficient media to increase ferric ion reductase activity also increases the stabilization. In conclusion, extracellular ascorbate stabilization by yeast cells can reflect a coenzyme Q dependent transplasmalemma electron transfer which uses NADH as electron donor. Iron deficiency increases the ascorbate stabilization but the transmembrane ferricyanide reduction system can act independently of ascorbate stabilization.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02111657
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  • 5
    Electronic Resource
    Electronic Resource
    Antioxidant Ascorbate Is Stabilized by NADH-Coenzyme Q10 Reductase in the Plasma Membrane (1997)
    Springer
    Journal of bioenergetics and biomembranes 29 (1997), S. 251-257 
    Details
    ISSN: 1573-6881
    Keywords: Plasma membrane ; ascorbate stabilization ; coenzyme Q ; cytochrome b 5 reductase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Plasma membranes isolated from K562 cells contain an NADH-ascorbate free radical reductase activity and intact cells show the capacity to reduce the rate of chemical oxidation of ascorbate leading to its stabilization at the extracellular space. Both activities are stimulated by CoQ10 and inhibited by capsaicin and dicumarol. A 34-kDa protein (p34) isolated from pig liver plasma membrane, displaying NADH-CoQ10 reductase activity and its internal sequence being identical to cytochrome b 5 reductase, increases the NADH-ascorbate free radical reductase activity of K562 cells plasma membranes. Also, the incorporation of this protein into K562 cells by p34-reconstituted liposomes also increased the stabilization of ascorbate by these cells. TPA-induced differentiation of K562 cells increases ascorbate stabilization by whole cells and both NADH-ascorbate free radical reductase and CoQ10 content in isolated plasma membranes. We show here the role of CoQ10 and its NADH-dependent reductase in both plasma membrane NADH-ascorbate free radical reductase and ascorbate stabilization by K562 cells. These data support the idea that besides intracellular cytochrome b 5-dependent ascorbate regeneration, the extracellular stabilization of ascorbate is mediated by CoQ10 and its NADH-dependent reductase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1022410127104
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  • 6
    Electronic Resource
    Electronic Resource
    Genetic Evidence for Coenzyme Q Requirement in Plasma Membrane Electron Transport (1998)
    Springer
    Journal of bioenergetics and biomembranes 30 (1998), S. 465-475 
    Details
    ISSN: 1573-6881
    Keywords: Coenzyme Q ; plasma membranes ; electron transport ; ascorbate stabilization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Plasma membranes isolated from wild-type Saccharomyces cerevisiae crude membrane fractions catalyzed NADH oxidation using a variety of electron acceptors, such as ferricyanide, cytochrome c, and ascorbate free radical. Plasma membranes from the deletion mutant strain coq3Δ, defective in coenzyme Q (ubiquinone) biosynthesis, were completely devoid of coenzyme Q6 and contained greatly diminished levels of NADH–ascorbate free radical reductase activity (about 10% of wild-type yeasts). In contrast, the lack of coenzyme Q6 in these membranes resulted in only a partial inhibition of either the ferricyanide or cytochrome-c reductase. Coenzyme Q dependence of ferricyanide and cytochrome-c reductases was based mainly on superoxide generation by one-electron reduction of quinones to semiquinones. Ascorbate free radical reductase was unique because it was highly dependent on coenzyme Q and did not involve superoxide since it was not affected by superoxide dismutase (SOD). Both coenzyme Q6 and NADH–ascorbate free radical reductase were rescued in plasma membranes derived from a strain obtained by transformation of the coq3Δ strain with a single-copy plasmid bearing the wild type COQ3 gene and in plasma membranes isolated form the coq3Δ strain grown in the presence of coenzyme Q6. The enzyme activity was inhibited by the quinone antagonists chloroquine and dicumarol, and after membrane solubilization with the nondenaturing detergent Zwittergent 3–14. The various inhibitors used did not affect residual ascorbate free radical reductase of the coq3Δ strain. Ascorbate free radical reductase was not altered significantly in mutants atp2Δ and cor1Δ which are also respiration-deficient but not defective in ubiquinone biosynthesis, demonstrating that the lack of ascorbate free radical reductase in coq3Δ mutants is related solely to the inability to synthesize ubiquinone and not to the respiratory-defective phenotype. For the first time, our results provide genetic evidence for the participation of ubiquinone in NADH–ascorbate free radical reductase, as a source of electrons for transmembrane ascorbate stabilization.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1020542230308
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  • 7
    Electronic Resource
    Electronic Resource
    Interactions Between Ascorbyl Free Radical and Coenzyme Q at the Plasma Membrane (2000)
    Springer
    Journal of bioenergetics and biomembranes 32 (2000), S. 199-210 
    Details
    ISSN: 1573-6881
    Keywords: Plasma membrane ; ascorbate regeneration ; ascorbyl free radical ; coenzyme Q
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract A role for coenzyme Q in the stabilization of extracellular ascorbate by intact cells has beenrecently recognized. The aim of this work was to study the interactions between reducedubiquinone in the plasma membrane and the ascorbyl free radical, as an approach to understandubiquinone-mediated ascorbate stabilization at the cell surface. K-562 cells stabilized ascorbateand decreased the steady-state levels of the semiascorbyl radical. The ability of cells to reduceascorbyl free radical was inhibited by the quinone analogs capsaicin and chloroquine andstimulated by supplementing cells with coenzyme Q10. Purified plasma membranes also reducedascorbyl free radical in the presence of NADH. Free-radical reduction was notobserved inquinone-depleted plasma membranes, but restored after its reconstitution with coenzyme Q10.Addition of reduced coenzyme Q10 to depleted membranes allowed them toreduce the signalof the ascorbyl free radical without NADH incubation and the addition of an extra amount ofpurified plasma membrane quinone reductase further stimulated this activity. Reduction wasabolished by treatment with the reductase inhibitor p-hydroximercuribenzoate and by blockingsurface glycoconjugates with the lectin wheat germ agglutinin, which supports the participationof transmembrane electron flow. The activity showed saturation kinetics by NADH andcoenzyme Q, but not by the ascorbyl free radical in the range of concentrations used. Our resultssupport that reduction of ascorbyl free radicals at the cell surface involves coenzyme Qreduction by NADH and the membrane-mediated reduction of ascorbyl free radical.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005568132027
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  • 8
    Electronic Resource
    Electronic Resource
    Plasma Membrane Ubiquinone Controls Ceramide Production and Prevents Cell Death Induced by Serum Withdrawal (1997)
    Springer
    Journal of bioenergetics and biomembranes 29 (1997), S. 259-267 
    Details
    ISSN: 1573-6881
    Keywords: HL-60 ; ρ°HL-60 ; ubiquinone ; plasma membrane ; apoptosis ; ceramide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Serum provides cultured cells with survival factors required to maintain growth. Its withdrawal induces the development of programmed cell death. HL-60 cells were sensitive to serum removal, and an increase of lipid peroxidation and apoptosis was observed. Long-term treatment with ethidium bromide induced the mitochondria-deficient ρ°HL-60 cell line. These cells were surprisingly more resistant to serum removal, displaying fewer apoptotic cells and lower lipid peroxidation. HL-60 cells contained less ubiquinone at the plasma membrane than ρ°HL-60 cells. Both cell types increased plasma membrane ubiquinone in response to serum removal, although this increase was much higher in ρ° cells. Addition of ubiquinone to both cell cultures in the absence of serum improved cell survival with decreasing lipid peroxidation and apoptosis. Ceramide was accumulated after serum removal in HL-60 but not in ρ°HL-60 cells, and exogenous ubiquinone reduced this accumulation. These results demonstrate a relationship between ubiquinone levels in the plasma membrane and the induction of serum withdrawal induced apoptosis, and ceramide accumulation. Thus, ubiquinone, which is a central component of the plasma membrane electron transport system, can represent a first level of protection against oxidative damage caused by serum withdrawal.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1022462111175
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  • 9
    Electronic Resource
    Electronic Resource
    Redox modulation of the response of NADH oxidase activity of rat liver plasma membranes to cyclic AMP plus ATP (1997)
    Springer
    Molecular and cellular biochemistry 173 (1997), S. 71-77 
    Details
    ISSN: 1573-4919
    Keywords: NADH oxidase ; cyclic AMP ; ATP ; plasma membrane ; rat liver
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract NADH oxidase activity of rat liver plasma membranes was inhibited by lowconcentrations (1-100 nM) of ATP. The inhibition was amplified by additionof nanomolar concentrations (0.1-10) of cyclic AMP. The inhibition wascomplex and related to a marked increase in the Km for NADH at high NADHconcentrations together with a concomitant decrease in the Vmax. In theabsence of added or residual ATP, cyclic AMP was without effect. Theresponse of cyclic AMP + ATP was inhibited by low concentrations of theselective inhibitor of cyclic AMP-dependent protein kinase, H-89 but not bystaurosporin. The Vmax but not the Km was modified by treating the plasmamembranes with a mild oxidizing agent, N-chlorosuccinamide, or with thereducing agent, dithiothreitol. In the presence of dithiothreitol, the Vmaxwas reduced by cyclic AMP + ATP. In contrast, in the presence ofN-chlorosuccinamide, the Vmax was increased by cyclic AMP + ATP relative tocyclic AMP + ATP alone. Thus, the effect of cyclic AMP + ATP on the Vmaxcould be either an increase or a decrease depending on whether the membraneswere oxidized or reduced. The results demonstrate regulation of NADH oxidaseactivity of rat liver plasma membranes through cyclic AMP-mediatedphosphorylation by membrane-located protein kinase activities where thefinal response is dependent on the oxidation-reduction status of the plasmamembranes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006880419063
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  • 10
    Electronic Resource
    Electronic Resource
    Plasma membrane redox systems (1998)
    Springer
    Protoplasma 205 (1998), S. 1-1 
    Details
    ISSN: 1615-6102
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01279286
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