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1. Developmental and sex differences in cardiac tolerance to ischemia-reperfusion injury: the role of mitochondria1

Author

Ostadal, B., Drahota, Z., Houstek, J., Milerova, M., Ostadalova, I., Hlavackova, M., and Kolar, F.

Subjects
Reperfusion injury, Heart, Infants (Newborn), Permeability, Blood proteins, Biological sciences
Abstract

Age and sex play an essential role in the cardiac tolerance to ischemia-reperfusion injury: cardiac resistance significantly decreases during postnatal maturation and the female heart is more tolerant than the male myocardium. It is widely accepted that mitochondrial dysfunction, and particularly mitochondrial permeability transition pore (MPTP) opening, plays a major role in determining the extent of cardiac ischemia-reperfusion injury. We have observed that the MPTP sensitivity to the calcium load differs in mitochondria isolated from neonatal and adult myocardium, as well as from adult male and female hearts. Neonatal and female mitochondria are more resistant both in the extent and in the rate of mitochondrial swelling induced by high calcium concentration. Our data further suggest that age- and sex-dependent specificity of the MPTP is not the result of different amounts of ATP synthase and cyclophilin D: neonatal and adult hearts, similarly as the male and female hearts, contain comparable amounts of MPTP and its regulatory protein cyclophilin D. We can speculate that the lower sensitivity of MPTP to the calcium-induced swelling may be related to the higher ischemic tolerance of both neonatal and female myocardium. Key words: neonatal heart, female heart, ischemia-reperfusion injury, cardiac ischemic tolerance, mitochondrial permeability transition pore, calcium-induced swelling. L'age et le sexe jouent un role essentiel dans la tolerance du coeur aux lesions d'ischemie-reperfusion : la resistance du coeur diminue nettement pendant le murissement postnatal, et le coeur femelle est plus tolerant que le myocarde male. Il est largement accepte que le dysfonctionnement myocardique, et plus particulierement l'ouverture des pores de transition de permeabilite mitochondriale (PTPM), joue un role majeur dans la determination de l'etendue des lesions d'ischemie-reperfusion dans le coeur. Nous avons observe que la sensibilite des PTPM a la charge en calcium des mitochondries isolees de myocarde neonatal est differente de celle du myocarde adulte, ainsi qu'entre les coeurs males et femelles. Les mitochondries neonatales et femelles sont plus resistantes quant a l'ampleur et a la vitesse du gonflement mitochondrial provoque par des concentrations elevees de calcium. Nos donnees laissent aussi entendre que la specificite des PTPM en fonction de l'age et du sexe n'est pas le resultat de differences quant aux quantites d'ATP synthase et de cyclophiline D : les coeurs neonataux comme adultes, de maniere similaire aux coeurs males et femelles, contiennent des quantites comparables de PTPM et de cyclophiline D, leur proteine regulatrice. Nous sommes en mesure de speculer que la plus faible sensibilite des PTPM au gonflement provoque par le calcium pourrait etre liee a la plus grande tolerance a l'ischemie du myocarde neonatal comme du myocarde femelle. [Traduit par la Redaction] Mots-cles : coeur neonatal, coeur femelle, lesions d'ischemie-reperfusion, tolerance a l'ischemie cardiaque, pore de transition de permeabilite mitochondriale, gonflement provoque par le calcium., Introduction The most frequent (and hence the most widely studied) cardiovascular diseases of modern times undoubtedly include hypoxic states. They originate as a result of disproportion between the amount of [...]

Published
2019
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9. Mitochondrial respiratory states and rate

Author

Gnaiger, E., Aasander Frostner, E., Abdul Karim, N., Abumrad, NA., Acuna-Castroviejo, D., Adiele, RC., Ahn, B., Ali, SS., Alton, L., Alves, MG., Amati, F., Amoedo, ND., Andreadou, I., Arago, M., Aral, C., Arandarcikaite, O., Armand, AS., Arnould, T., Avram, VF., Bailey, DM., Bajpeyi, S., Bajzikova, M., Bakker, BM., Barlow, J., Bastos Sant'Anna Silva, AC., Batterson, P., Battino, M., Bazil, J., Beard, DA., Bednarczyk, P., Bello, F., Ben-Shachar, D., Bergdahl, A., Berge, RK., Bergmeister, L., Bernardi, P., Berridge, MV., Bettinazzi, S., Bishop, D., Blier, PU., Blindheim, DF., Boardman, NT., Boetker, HE., Borchard, S., Boros, M., Borsheim, E., Borutaite, V., Botella, J., Bouillaud, F., Bouitbir, J., Boushel, RC., Bovard, J., Breton, S., Brown, DA., Brown, GC., Brown, RA., Brozinick, JT., Buettner, GR., Burtscher, J., Calabria, E., Calbet, JA., Calzia, E., Cannon, DT., Cano Sanchez, M., Canto, AC., Cardoso, LHD., Carvalho, E., Casado Pinna, M., Cassar, S., Cassina, AM., Castelo, MP., Castro, L., Cavalcanti-de-Albuquerque, JP., Cervinkova, Z., Chabi, B., Chakrabarti, L., Chakrabarti, S., Chaurasia, B., Chen, Q., Chicco, AJ., Chinopoulos, C., Chowdhury, SK., Cizmarova, B., Clementi, E., Coen, PM., Cohen, BH., Coker, RH., Collin, A., Crisostomo, L., Dahdah, N., Dalgaard, LT., Dambrova, M., Danhelovska, T., Darveau, CA., Das, AM., Dash, RK., Davidova, E., Davis, MS., De Goede, P., De Palma, C., Dembinska-Kiec, A., Detraux, D., Devaux, Y., Di Marcello, M., Dias, TR., Distefano, G., Doermann, N., Doerrier, C., Dong, L., Donnelly, C., Drahota, Z., Duarte, FV., Dubouchaud, H., Duchen, MR., Dumas, JF., Durham, WJ., Dymkowska, D., Dyrstad, SE., Dyson, A., Dzialowski, EM., Eaton, S., Ehinger, J., Elmer, E., Endlicher, R., Engin, AB., Escames, G., Ezrova, Z., Falk, MJ., Fell, DA., Ferdinandy, P., Ferko, M., Ferreira, JCB., Ferreira, R., Ferri, A., Fessel, JP., Filipovska, A., Fisar, Z., Fischer, C., Fischer, M., Fisher, G., Fisher, JJ., Ford, E., Fornaro, M., Galina, A., Galkin, A., Gallee, L., Galli, GL., Gama Perez, P., Gan, Z., Ganetzky, R., Garcia-Rivas, G., Garcia-Roves, PM., Garcia-Souza, LF., Garipi, E., Garlid, KD., Garrabou, G., Garten, A., Gastaldelli, A., Gayen, J., Genders, AJ., Genova, ML., Giovarelli, M., Goncalo Teixeira da Silva, R., Goncalves, DF., Gonzalez-Armenta, JL., Gonzalez-Freire, M., Gonzalo, H., Goodpaster, BH., Gorr, TA., Gourlay, CW., Granata, C., Grefte, S., Guarch, ME., Gueguen, N., Gumeni, S., Haas, CB., Haavik, J., Haendeler, J., Haider, M., Hamann, A., Han, J., Han, WH., Hancock, CR., Hand, SC., Handl, J., Hargreaves, IP., Harper, ME., Harrison, DK., Hassan, H., Hausenloy, DJ., Heales, SJR., Heiestad, C., Hellgren, KT., Hepple, RT., Hernansanz-Agustin, P., Hewakapuge, S., Hickey, AJ., Ho, DH., Hoehn, KL., Hoel, F., Holland, OJ., Holloway, GP., Hoppel, CL., Hoppel, F., Houstek, J., Huete-Ortega, M., Hyrossova, P., Iglesias-Gonzalez, J., Irving, BA., Isola, R., Iyer, S., Jackson, CB., Jadiya, P., Jana, PF., Jang, DH., Jang, YC., Janowska, J., Jansen, K., Jansen-Duerr, P., Jansone, B., Jarmuszkiewicz, W., Jaskiewicz, A., Jedlicka, J., Jespersen, NR., Jha, RK., Jurczak, MJ., Jurk, D., Kaambre, T., Kaczor, JJ., Kainulainen, H., Kampa, RP., Kandel, SM., Kane, DA., Kapferer, W., Kappler, L., Karabatsiakis, A., Karavaeva, I., Karkucinska-Wieckowska, A., Kaur, S., Keijer, J., Keller, MA., Keppner, G., Khamoui, AV., Kidere, D., Kilbaugh, T., Kim, HK., Kim, JKS., Klepinin, A., Klepinina, L., Klingenspor, M., Klocker, H., Komlodi, T., Koopman, WJH., Kopitar-Jerala, N., Kowaltowski, AJ., Kozlov, AV., Krajcova, A., Krako Jakovljevic, N., Kristal, BS., Krycer, JR., Kuang, J., Kucera, O., Kuka, J., Kwak, HB., Kwast, K., Laasmaa, M., Labieniec-Watala, M., Lagarrigue, S., Lai, N., Land, JM., Lane, N., Laner, V., Lanza, IR., Laranjinha, J., Larsen, TS., Lavery, GG., Lazou, A., Lee, HK., Leeuwenburgh, C., Lehti, M., Lemieux, H., Lenaz, G., Lerfall, J., Li, PA., Li Puma, L., Liepins, E., Liu, J., Lopez, LC., Lucchinetti, E., Ma, T., Macedo, MP., Maciej, S., MacMillan-Crow, LA., Majtnerova, P., Makarova, E., Makrecka-Kuka, M., Malik, AN., Markova, M., Martin, DS., Martins, AD., Martins, JD., Maseko, TE., Maull, F., Mazat, JP., McKenna, HT., McKenzie, M., Menze, MA., Merz, T., Meszaros, AT., Methner, A., Michalak, S., Moellering, DR., Moisoi, N., Molina, AJA., Montaigne, D., Moore, AL., Moreau, K., Moreira, BP., Moreno-Sanchez, R., Mracek, T., Muccini, AM., Munro, D., Muntane, J., Muntean, DM., Murray, AJ., Musiol, E., Nabben, M., Nair, KS., Nehlin, JO., Nemec, M., Neufer, PD., Neuzil, J., Neviere, R., Newsom, SA., Nozickova, K., O'Brien, KA., O'Gorman, D., Olgar, Y., Oliveira, B., Oliveira, MF., Oliveira, MT., Oliveira, PF., Oliveira, PJ., Orynbayeva, Z., Osiewacz, HD., Pak, YK., Pallotta, ML., Palmeira, CM., Parajuli, N., Passos, JF., Passrugger, M., Patel, HH., Pavlova, N., Pecina, P., Pedersen, TM., Pereira da Silva Grilo da Silva, F., Pereira, SP., Perez Valencia, JA., Perks, KL., Pesta, D., Petit, PX., Pettersen, IKN., Pichaud, N., Pichler, I., Piel, S., Pietka, TA., Pino, MF., Pirkmajer, S., Plangger, M., Porter, C., Porter, RK., Procaccio, V., Prochownik, EV., Prola, A., Pulinilkunnil, T., Puskarich, MA., Puurand, M., Radenkovic, F., Ramzan, R., Rattan, SIS., Reboredo, P., Renner-Sattler, K., Rial, E., Robinson, MM., Roden, M., Rodriguez, E., Rodriguez-Enriquez, S., Roesland, GV., Rohlena, J., Rolo, AP., Ropelle, ER., Rossignol, R., Rossiter, HB., Rubelj, I., Rybacka-Mossakowska, J., Saada, A., Safaei, Z., Saharnaz, S., Salin, K., Salvadego, D., Sandi, C., Saner, N., Sanz, A., Sazanov, LA., Scatena, R., Schartner, M., Scheibye-Knudsen, M., Schilling, JM., Schlattner, U., Schoenfeld, P., Schots, PC., Schulz, R., Schwarzer, C., Scott, GR., Selman, C., Shabalina, IG., Sharma, P., Sharma, V., Shevchuk, I., Shirazi, R., Shiroma, JG., Siewiera, K., Silber, AM., Silva, AM., Sims, CA., Singer, D., Singh, BK., Skolik, R., Smenes, BT., Smith, J., Soares, FAA., Sobotka, O., Sokolova, I., Sonkar, VK., Sowton, AP., Sparagna, GC., Sparks, LM., Spinazzi, M., Stankova, P., Starr, J., Stary, C., Stelfa, G., Stepto, NK., Stiban, J., Stier, A., Stocker, R., Storder, J., Sumbalova, Z., Suomalainen, A., Suravajhala, P., Svalbe, B., Swerdlow, RH., Swiniuch, D., Szabo, I., Szewczyk, A., Szibor, M., Tanaka, M., Tandler, B., Tarnopolsky, MA., Tausan, D., Tavernarakis, N., Tepp, K., Thakkar, H., Thapa, M., Thyfault, JP., Tomar, D., Ton, R., Torp, MK., Towheed, A., Tretter, L., Trewin, AJ., Trifunovic, A., Trivigno, C., Tronstad, KJ., Trougakos, IP., Truu, L., Tuncay, E., Turan, B., Tyrrell, DJ., Urban, T., Valentine, JM., Van Bergen, NJ., Van Hove, J., Varricchio, F., Vella, J., Vendelin, M., Vercesi, AE., Victor, VM., Vieira Ligo Teixeira, C., Vidimce, J., Viel, C., Vieyra, A., Vilks, K., Villena, JA., Vincent, V., Vinogradov, AD., Viscomi, C., Vitorino, RMP., Vogt, S., Volani, C., Volska, K., Votion, DM., Vujacic-Mirski, K., Wagner, BA., Ward, ML., Warnsmann, V., Wasserman, DH., Watala, C., Wei, YH., Whitfield, J., Wickert, A., Wieckowski, MR., Wiesner, RJ., Williams, CM., Winwood-Smith, H., Wohlgemuth, SE., Wohlwend, M., Wolff, JN., Wrutniak-Cabello, C., Wuest, RCI., Yokota, T., Zablocki, K., Zanon, A., Zanou, N., Zaugg, K., Zaugg, M., Zdrazilova, L., Zhang, Y., Zhang, YZ., Zikova, A., Zischka, H., Zorzano, A., and Zvejniece, L.

Subjects
Mitochondrial respiratory control, coupling control, mitochondrial preparations, protonmotive force, uncoupling, oxidative phosphorylation, OXPHOS, efficiency, electron transfer, ET, proton leak, LEAK, residual oxygen consumption, ROX, State 2, State 3, State 4, normalization, flow, flux, O2
Abstract

As the knowledge base and importance of mitochondrial physiology to human health expands, the necessity for harmonizing the terminologyconcerning mitochondrial respiratory states and rates has become increasingly apparent. Thechemiosmotic theoryestablishes the mechanism of energy transformationandcoupling in oxidative phosphorylation. Theunifying concept of the protonmotive force providestheframeworkfordeveloping a consistent theoretical foundation ofmitochondrial physiology and bioenergetics.We followguidelines of the International Union of Pure and Applied Chemistry(IUPAC)onterminology inphysical chemistry, extended by considerationsofopen systems and thermodynamicsof irreversible processes.Theconcept-driven constructive terminology incorporates the meaning of each quantity and alignsconcepts and symbols withthe nomenclature of classicalbioenergetics. We endeavour to provide a balanced view ofmitochondrial respiratory control and a critical discussion on reporting data of mitochondrial respiration in terms of metabolic flows and fluxes.Uniform standards for evaluation of respiratory states and rates will ultimatelycontribute to reproducibility between laboratories and thussupport the development of databases of mitochondrial respiratory function in species, tissues, and cells.Clarity of concept and consistency of nomenclature facilitate effective transdisciplinary communication, education, and ultimately further discovery.

Published
2019

15. Bi-allelic Mutations in NDUFA6 Establish Its Role in Early-Onset Isolated Mitochondrial Complex I Deficiency

Author

Alston, CL, Heidler, J, Dibley, MG, Kremer, LS, Taylor, LS, Fratter, C, French, CE, Glasgow, RIC, Feichtinger, RG, Delon, I, Pagnamenta, AT, Dolling, H, Lemonde, H, Aiton, N, Bjørnstad, A, Henneke, L, Gärtner, J, Thiele, H, Tauchmannova, K, Quaghebeur, G, Houstek, J, Sperl, W, Raymond, FL, Prokisch, H, Mayr, JA, McFarland, R, Poulton, J, Ryan, MT, Wittig, I, Henneke, M, Taylor, RW, French, Courtney [0000-0001-7620-1544], Dolling, Helen [0000-0001-6279-3622], Raymond, Lucy [0000-0003-2652-3355], and Apollo - University of Cambridge Repository

Subjects
Male, Electron Transport Complex I, Mitochondrial Diseases, complex I, complexome profiling, Infant, Fibroblasts, Mitochondria, Mitochondrial Proteins, Complex I, Complexome Profiling, Mitochondrial Disease, Ndufa6, mitochondrial disease, Genetic Heterogeneity, NDUFA6, Phenotype, Report, Mutation, Humans, Female, ddc:610, Amino Acid Sequence, Sequence Alignment, Alleles
Abstract

Isolated complex I deficiency is a common biochemical phenotype observed in pediatric mitochondrial disease and often arises as a consequence of pathogenic variants affecting one of the similar to 65 genes encoding the complex I structural subunits or assembly factors. Such genetic heterogeneity means that application of next-generation sequencing technologies to undiagnosed cohorts has been a catalyst for genetic diagnosis and gene-disease associations. We describe the clinical and molecular genetic investigations of four unrelated children who presented with neuroradiological findings and/or elevated lactate levels, highly suggestive of an underlying mitochondrial diagnosis. Next-generation sequencing identified bi-allelic variants in NDUFA6, encoding a 15 kDa LYR-motif-containing complex I subunit that forms part of the Q-module. Functional investigations using subjects' fibroblast cell lines demonstrated complex I assembly defects, which were characterized in detail by mass-spectrometry-based complexome profiling. This confirmed a marked reduction in incorporated NDUFA6 and a concomitant reduction in other Q-module subunits, including NDUFAB1, NDUFA7, and NDUFA12. Lentiviral transduction of subjects' fibroblasts showed normalization of complex I. These data also support supercomplex formation, whereby the similar to 830 kDa complex I intermediate (consisting of the P- and Q-modules) is in complex with assembled complex III and IV holoenzymes despite lacking the N-module. Interestingly, RNA-sequencing data provided evidence that the consensus RefSeq accession number does not correspond to the predominant transcript in clinically relevant tissues, prompting revision of the NDUFA6 RefSeq transcript and highlighting not only the importance of thorough variant interpretation but also the assessment of appropriate transcripts for analysis.

Published
2018

16. Mitochondrial respiratory states and rates: Building blocks of mitochondrial physiology (Part 1)

Author

Gnaiger, E., Ahn, B., Alves, M. G., Amati, F., Aral, C., Arandarčikaitė, O., Åsander Frostner, E., Bailey, David M., Bastos Sant'Anna Silva, A. C., Battino, M., Beard, D. A., Newsom, S., Robinson, M. M., Patel, H. H., Buettner, G. R., Pecina, P., Shevchuk, I., Pereira da Silva Grilo da Silva, F., Ben-Shachar, D., Pesta, D., Goodpaster, B. H., Zorzano, Antonio, Petit, P. X., Pichaud, N., Pirkmajer, S., Porter, R. K., Wagner, B. A., Pranger, F., Rohlena, J., Prochownik, E. V., Siewiera, K., Røsland, G. V., Ehinger, J., Rossiter, H. B., Towheed, A., Rybacka-Mossakowska, J., Dias, T., Salvadego, D., Jansen-Dürr, P., Scatena, R., Schartner, M., Scheibye-Knudsen, Morten, Breton, S., Cardoso, L.H.D., Schilling, J. M., Singer, D., Schlattner, U., Brown, R. A., Sobotka, O., Spinazzi, M., Ward, M. L., Brown, G. C., Gonzalo, H., Stankova, P., Labieniec-Watala, M., Stier, A., Stocker, R., Sumbalova, Zuzana, Doerrier, C., Suravajhala, P., Tretter, L., Tanaka, M., Duchen, Michael R., Trivigno, C., Tronstad, K. J., Carvalho, Eugenia, Drahota, Z., Jackson, C. B., Trougakos, I. P., Tyrrell, D. J., Urban, T., Velika, B., Gorr, T. A., Vercesi, A. E., Watala, C., Victor, V. M., Grefte, S., Wei, Y. H., Wieckowski, M. R., O'Gorman, D., Kucera, O., Wohlwend, M., Wolff, J., Wuest, R.C.I., Zaugg, K., Jespersen, N. R., Zaugg, M., Casado, Marta, Calabria, E., Červinková, Zuzana, Chang, S. C., Radenkovic, F., Moisoi, N., Chicco, A. J., Chinopoulos, C., Coen, P. M., Collins, J. L., Lai, N., Crisóstomo, L., Elmer, E., Davis, M. S., Han, J., Endlicher, R., Pak, Y. K., Fell, D. A., Jha, R. K., Ferko, M., Nozickova, K., Ferreira, J.C.B., Scott, G. R., Filipovska, A., Fisar, Z., Fisher, J., García-Rovés, Pablo M., Molina, A.J.A., Garcia-Souza, L. F., Harrison, D. K., Genova, M. L., Kaambre, T., Hellgren, K. T., Hernansanz-Agustín, Pablo, Laner, V., Holland, O., Puurand, M., Hoppel, C. L., Tepp, K., Houstek, J., Hunger, M., Iglesias-Gonzalez, J., Oliveira, P. F., Irving, B. A., Kane, D. A., Iyer, S., Orynbayeva, Z., Kappler, L., Karabatsiakis, A., Montaigne, D., Oliveira, P. J., Schoenfeld, P., Keijer, J., Keppner, G., Komlodi, T., Kopitar-Jerala, N., Reboredo, P., Krako Jakovljevic, N., Larsen, T. S., Kuang, J., Renner-Sattler, K., Lee, H. K., Lemieux, H., Bishop, D., Tandler, B., Lerfall, J., Lucchinetti, E., MacMillan-Crow, L. A., Makrecka-Kuka, M., Shabalina, I. G., Meszaros, A. T., Moore, A. L., Michalak, S., Moreira, B. P., Mracek, T., Distefano, G., Villena, J. A., Muntané, Jordi, Muntean, D. M., Murray, A. J., Nedergaard, J., Tomar, D., Nemec, M., Palmeira, C. M., and European Commission

Subjects
Mitochondrial preparations, Mitochondrial respiratory control, Proton leak, Flux, Flow, Coupling control, Efficiency, State 4, Protonmotive force, State 2, OXPHOS, Residual oxygen consumption, State 3, Electron transfer, Normalization, ROX, Oxidative phosphorylation, LEAK, ET
Abstract

Supporting co-authors: Bakker BM, Bernardi P, Boetker HE, Borsheim E, Borutaitė V, Bouitbir J, Calbet JA, Calzia E, Chaurasia B, Clementi E, Coker RH, Collin A, Das AM, De Palma C, Dubouchaud H, Durham WJ, Dyrstad SE, Engin AB, Fornaro M, Gan Z, Garlid KD, Garten A, Gourlay CW, Granata C, Haas CB, Haavik J, Haendeler J, Hand SC, Hepple RT, Hickey AJ, Hoel F, Jang DH, Kainulainen H, Khamoui AV, Klingenspor M, Koopman WJH, Kowaltowski AJ, Krajcova A, Lane N, Lenaz G, Malik A, Markova M, Mazat JP, Menze MA, Methner A, Neuzil J, Oliveira MT, Pallotta ML, Parajuli N, Pettersen IKN, Porter C, Pulinilkunnil T, Ropelle ER, Salin K, Sandi C, Sazanov LA, Silber AM, Skolik R, Smenes BT, Soares FAA, Sokolova I, Sonkar VK, Swerdlow RH, Szabo I, Trifunovic A, Thyfault JP, Valentine JM, Vieyra A, Votion DM, Williams C, Zischka H, As the knowledge base and importance of mitochondrial physiology to human health expand, the necessity for harmonizing nomenclature concerning mitochondrial respiratory states and rates has become increasingly apparent. Clarity of concept and consistency of nomenclature are key trademarks of a research field. These trademarks facilitate effective transdisciplinary communication, education, and ultimately further discovery. Peter Mitchell’s chemiosmotic theory establishes the link between vectorial and scalar energy transformation and coupling in oxidative phosphorylation. The unifying concept of the protonmotive force provides the framework for developing a consistent theory and nomenclature for mitochondrial physiology and bioenergetics. Herein, we follow IUPAC guidelines on general terms of physical chemistry, extended by considerations on open systems and irreversible thermodynamics. We align the nomenclature and symbols of classical bioenergetics with a concept-driven constructive terminology to express the meaning of each quantity clearly and consistently. In this position statement, in the frame of COST Action MitoEAGLE, we endeavour to provide a balanced view on mitochondrial respiratory control and a critical discussion on reporting data of mitochondrial respiration in terms of metabolic flows and fluxes. Uniform standards for evaluation of respiratory states and rates will ultimately support the development of databases of mitochondrial respiratory function in species, tissues, and cells., We thank M. Beno for management assistance. Supported by COST Action CA15203 MitoEAGLE and K-Regio project MitoFit (E.G.).

Published
2018
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17. 5162Novel insights into desminopathy in the era of next generation sequencing

Author

Kubanek, M, primary, Schimerova, T, additional, Piherova, L, additional, Krebsova, A, additional, Hansikova, H, additional, Zeman, J, additional, Palecek, T, additional, Houstek, J, additional, Zamecnik, J, additional, Macek Jr, M, additional, Ridzon, P, additional, Stranecky, V, additional, Kmoch, S, additional, Melenovsky, V, additional, and Kautzner, J, additional

Published
2019
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18. Mitochondrial respiratory states and rates: Building blocks of mitochondrial physiology (Part 1)

Author

European Commission, Gnaiger, E., Ahn, B., Alves, M. G., Amati, F., Aral, C., Arandarčikaitė, O., Åsander Frostner, E., Bailey, David M., Bastos Sant'Anna Silva, A. C., Battino, M., Beard, D. A., Newsom, S., Robinson, M. M., Patel, H. H., Buettner, G. R., Pecina, P., Shevchuk, I., Pereira da Silva Grilo da Silva, F., Ben-Shachar, D., Pesta, D., Goodpaster, B. H., Zorzano, Antonio, Petit, P. X., Pichaud, N., Pirkmajer, S., Porter, R. K., Wagner, B. A., Pranger, F., Rohlena, J., Prochownik, E. V., Siewiera, K., Røsland, G. V., Ehinger, J., Rossiter, H. B., Towheed, A., Rybacka-Mossakowska, J., Dias, T., Salvadego, D., Jansen-Dürr, P., Scatena, R., Schartner, M., Scheibye-Knudsen, Morten, Breton, S., Cardoso, L.H.D., Schilling, J. M., Singer, D., Schlattner, U., Brown, R. A., Sobotka, O., Spinazzi, M., Ward, M. L., Brown, G. C., Gonzalo, H., Stankova, P., Labieniec-Watala, M., Stier, A., Stocker, R., Sumbalova, Zuzana, Doerrier, C., Suravajhala, P., Tretter, L., Tanaka, M., Duchen, Michael R., Trivigno, C., Tronstad, K. J., Carvalho, Eugenia, Drahota, Z., Jackson, C. B., Trougakos, I. P., Tyrrell, D. J., Urban, T., Velika, B., Gorr, T. A., Vercesi, A. E., Watala, C., Victor, V. M., Grefte, S., Wei, Y. H., Wieckowski, M. R., O'Gorman, D., Kucera, O., Wohlwend, M., Wolff, J., Wuest, R.C.I., Zaugg, K., Jespersen, N. R., Zaugg, M., Casado, Marta, Calabria, E., Červinková, Zuzana, Chang, S. C., Radenkovic, F., Moisoi, N., Chicco, A. J., Chinopoulos, C., Coen, P. M., Collins, J. L., Lai, N., Crisóstomo, L., Elmer, E., Davis, M. S., Han, J., Endlicher, R., Pak, Y. K., Fell, D. A., Jha, R. K., Ferko, M., Nozickova, K., Ferreira, J.C.B., Scott, G. R., Filipovska, A., Fisar, Z., Fisher, J., García-Rovés, Pablo M., Molina, A.J.A., Garcia-Souza, L. F., Harrison, D. K., Genova, M. L., Kaambre, T., Hellgren, K. T., Hernansanz-Agustín, Pablo, Laner, V., Holland, O., Puurand, M., Hoppel, C. L., Tepp, K., Houstek, J., Hunger, M., Iglesias-Gonzalez, J., Oliveira, P. F., Irving, B. A., Kane, D. A., Iyer, S., Orynbayeva, Z., Kappler, L., Karabatsiakis, A., Montaigne, D., Oliveira, P. J., Schoenfeld, P., Keijer, J., Keppner, G., Komlodi, T., Kopitar-Jerala, N., Reboredo, P., Krako Jakovljevic, N., Larsen, T. S., Kuang, J., Renner-Sattler, K., Lee, H. K., Lemieux, H., Bishop, D., Tandler, B., Lerfall, J., Lucchinetti, E., MacMillan-Crow, L. A., Makrecka-Kuka, M., Shabalina, I. G., Meszaros, A. T., Moore, A. L., Michalak, S., Moreira, B. P., Mracek, T., Distefano, G., Villena, J. A., Muntané, Jordi, Muntean, D. M., Murray, A. J., Nedergaard, J., Tomar, D., Nemec, M., Palmeira, C. M., European Commission, Gnaiger, E., Ahn, B., Alves, M. G., Amati, F., Aral, C., Arandarčikaitė, O., Åsander Frostner, E., Bailey, David M., Bastos Sant'Anna Silva, A. C., Battino, M., Beard, D. A., Newsom, S., Robinson, M. M., Patel, H. H., Buettner, G. R., Pecina, P., Shevchuk, I., Pereira da Silva Grilo da Silva, F., Ben-Shachar, D., Pesta, D., Goodpaster, B. H., Zorzano, Antonio, Petit, P. X., Pichaud, N., Pirkmajer, S., Porter, R. K., Wagner, B. A., Pranger, F., Rohlena, J., Prochownik, E. V., Siewiera, K., Røsland, G. V., Ehinger, J., Rossiter, H. B., Towheed, A., Rybacka-Mossakowska, J., Dias, T., Salvadego, D., Jansen-Dürr, P., Scatena, R., Schartner, M., Scheibye-Knudsen, Morten, Breton, S., Cardoso, L.H.D., Schilling, J. M., Singer, D., Schlattner, U., Brown, R. A., Sobotka, O., Spinazzi, M., Ward, M. L., Brown, G. C., Gonzalo, H., Stankova, P., Labieniec-Watala, M., Stier, A., Stocker, R., Sumbalova, Zuzana, Doerrier, C., Suravajhala, P., Tretter, L., Tanaka, M., Duchen, Michael R., Trivigno, C., Tronstad, K. J., Carvalho, Eugenia, Drahota, Z., Jackson, C. B., Trougakos, I. P., Tyrrell, D. J., Urban, T., Velika, B., Gorr, T. A., Vercesi, A. E., Watala, C., Victor, V. M., Grefte, S., Wei, Y. H., Wieckowski, M. R., O'Gorman, D., Kucera, O., Wohlwend, M., Wolff, J., Wuest, R.C.I., Zaugg, K., Jespersen, N. R., Zaugg, M., Casado, Marta, Calabria, E., Červinková, Zuzana, Chang, S. C., Radenkovic, F., Moisoi, N., Chicco, A. J., Chinopoulos, C., Coen, P. M., Collins, J. L., Lai, N., Crisóstomo, L., Elmer, E., Davis, M. S., Han, J., Endlicher, R., Pak, Y. K., Fell, D. A., Jha, R. K., Ferko, M., Nozickova, K., Ferreira, J.C.B., Scott, G. R., Filipovska, A., Fisar, Z., Fisher, J., García-Rovés, Pablo M., Molina, A.J.A., Garcia-Souza, L. F., Harrison, D. K., Genova, M. L., Kaambre, T., Hellgren, K. T., Hernansanz-Agustín, Pablo, Laner, V., Holland, O., Puurand, M., Hoppel, C. L., Tepp, K., Houstek, J., Hunger, M., Iglesias-Gonzalez, J., Oliveira, P. F., Irving, B. A., Kane, D. A., Iyer, S., Orynbayeva, Z., Kappler, L., Karabatsiakis, A., Montaigne, D., Oliveira, P. J., Schoenfeld, P., Keijer, J., Keppner, G., Komlodi, T., Kopitar-Jerala, N., Reboredo, P., Krako Jakovljevic, N., Larsen, T. S., Kuang, J., Renner-Sattler, K., Lee, H. K., Lemieux, H., Bishop, D., Tandler, B., Lerfall, J., Lucchinetti, E., MacMillan-Crow, L. A., Makrecka-Kuka, M., Shabalina, I. G., Meszaros, A. T., Moore, A. L., Michalak, S., Moreira, B. P., Mracek, T., Distefano, G., Villena, J. A., Muntané, Jordi, Muntean, D. M., Murray, A. J., Nedergaard, J., Tomar, D., Nemec, M., and Palmeira, C. M.

Abstract

As the knowledge base and importance of mitochondrial physiology to human health expand, the necessity for harmonizing nomenclature concerning mitochondrial respiratory states and rates has become increasingly apparent. Clarity of concept and consistency of nomenclature are key trademarks of a research field. These trademarks facilitate effective transdisciplinary communication, education, and ultimately further discovery. Peter Mitchell’s chemiosmotic theory establishes the link between vectorial and scalar energy transformation and coupling in oxidative phosphorylation. The unifying concept of the protonmotive force provides the framework for developing a consistent theory and nomenclature for mitochondrial physiology and bioenergetics. Herein, we follow IUPAC guidelines on general terms of physical chemistry, extended by considerations on open systems and irreversible thermodynamics. We align the nomenclature and symbols of classical bioenergetics with a concept-driven constructive terminology to express the meaning of each quantity clearly and consistently. In this position statement, in the frame of COST Action MitoEAGLE, we endeavour to provide a balanced view on mitochondrial respiratory control and a critical discussion on reporting data of mitochondrial respiration in terms of metabolic flows and fluxes. Uniform standards for evaluation of respiratory states and rates will ultimately support the development of databases of mitochondrial respiratory function in species, tissues, and cells.

Published
2018

23. Pharmacological inhibition of fatty-acid oxidation synergistically enhances the effect of l-asparaginase in childhood ALL cells

Author

Hermanova, I, primary, Arruabarrena-Aristorena, A, additional, Valis, K, additional, Nuskova, H, additional, Alberich-Jorda, M, additional, Fiser, K, additional, Fernandez-Ruiz, S, additional, Kavan, D, additional, Pecinova, A, additional, Niso-Santano, M, additional, Zaliova, M, additional, Novak, P, additional, Houstek, J, additional, Mracek, T, additional, Kroemer, G, additional, Carracedo, A, additional, Trka, J, additional, and Starkova, J, additional

Published
2015
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26. Genetic defects of cytochrome c oxidase assembly

Author

Pecina P, Houstková H, Hansíková H, Jiri Zeman, and Houstek J

Subjects
Electron Transport Complex IV, Mitochondrial Proteins, Oxygen, Alkyl and Aryl Transferases, Mitochondrial Diseases, Animals, Cytochrome-c Oxidase Deficiency, Humans, Membrane Proteins, Point Mutation, Proteins, Mitochondria, Molecular Chaperones
Abstract

Cytochrome c oxidase (COX), the terminal enzyme of the mitochondrial respiratory chain, is one of the key functional and regulatory sites of the mammalian energy metabolism. Owing to the importance of the enzyme, pathogenetic mutations affecting COX frequently result in severe, often fatal metabolic disorders. No satisfactory therapy is currently available so that the treatment remains largely symptomatic and does not improve the course of the disease. While only few genetic defects of COX are caused by mutations in mitochondrial genome, during the last five years a large number of pathogenetic mutations in nuclear genes have been discovered. All these mutations are located in genes encoding COX-specific assembly proteins including SURF1, SCO1, SCO2, COX10, and COX15. Despite the identification of increasing number of mutations, their precise etiopathogenetic mechanisms, which are necessary for the development of future therapeutic protocols, still remain to be elucidated. This review summarizes recent developments, including our efforts in elucidation of the molecular basis of human mitochondrial diseases due to specific defects of COX with special focus on SURF1 assembly protein.

Published
2004

27. Optimal conditions for determination of cytochrome c oxidase activity in the rat heart

Author

Stieglerova, A., Zdenek Drahota, Ostadal, B., and Houstek, J.

Subjects
Male, Binding Sites, Potassium Compounds, Myocardium, Detergents, Binding, Competitive, Mitochondria, Heart, Phosphates, Rats, Electron Transport Complex IV, Kinetics, Glucosides, Animals, Rats, Wistar
Abstract

The determination of cytochrome c oxidase (COX) activity represents an important indicator for the evaluation of cell oxidative capacity. However, it has been shown repeatedly that different factors modify the rate of COX activity under various experimental conditions. The most important concern the ionic concentrations of the medium and the application of various detergents for the solubilization of mitochondrial membranes. We found the highest activity of COX in rat heart homogenates and mitochondria at 40-60 mM potassium phosphate. The rate of COX activity is dependent on the detergent/protein (P) ratio. Using n-dodecyl-beta-D-maltoside (lauryl maltoside, LM) as the detergent, we obtained the highest activity at LM/P ratios of (50:100):1. By kinetic measurements of low-affinity binding sites in heart mitochondria, we found Vlim values of 4.3 and 22.2 micromol cytochrome c per min per mg P in the presence or absence of lauryl maltoside, respectively. The Km values were 16.7 micromol in the presence or absence of lauryl maltoside. Our results thus indicate that 1) the exact assessment of COX activity in heart homogenates and mitochondria requires the determination of optimum phosphate concentrations in the medium used, and 2) even small modifications of the experimental procedure may induce significant differences in the maximum values of COX activity.

Published
2000

28. [Leber's hereditary optic nerve neuropathy]

Author

Michalik J, Kurca E, Drobny M, Vosko MR, Malis V, Misovicova N, Jiri Zeman, Konradova V, Stratilova L, and Houstek J

Subjects
Adult, Male, Optic Atrophies, Hereditary, Humans
Abstract

The authors present a case report of 26 years old man with bilateral optic nerve neuropathy. Detection of heteroplasmic mutation of mitochondrial DNA at G3460A site confirmed the suspicion on Lebers hereditary optic nerve neuropathy (LHON). Genetic and environmental factors of the disease and various accompanying neurologic and other symptoms, which can together with the optic nerve defect participate in the development of of the LOHN clinical pattern are discussed. (Ref. 12.)

Published
2000

29. Polyunsaturated fatty acids of marine origin upregulate mitochondrial biogenesis and induce-beta oxidation in white fat

Author

Flachs, P., Horakova, O., Brauner, P., Rossmeisl, M., Pecina, P., van Franssen-Hal, N.L.W., Ruzickova, J., Sponarova, J., Drahota, Z., Vlcek, C., Keijer, J., Houstek, J., Kopecky, J., Flachs, P., Horakova, O., Brauner, P., Rossmeisl, M., Pecina, P., van Franssen-Hal, N.L.W., Ruzickova, J., Sponarova, J., Drahota, Z., Vlcek, C., Keijer, J., Houstek, J., and Kopecky, J.

Abstract

Aims/hypothesis Intake of n-3 polyunsaturated fatty acids reduces adipose tissue mass, preferentially in the abdomen. The more pronounced effect of marine-derived eicosapentaenoic (EPA) and docosahexaenoic (DHA) acids on adiposity, compared with their precursor -linolenic acid, may be mediated by changes in gene expression and metabolism in white fat. Methods The effects of EPA/DHA concentrate (6% EPA, 51% DHA) admixed to form two types of high-fat diet were studied in C57BL/6J mice. Oligonucleotide microarrays, cDNA PCR subtraction and quantitative real-time RT-PCR were used to characterise gene expression. Mitochondrial proteins were quantified using immunoblots. Fatty acid oxidation and synthesis were measured in adipose tissue fragments. Results Expression screens revealed upregulation of genes for mitochondrial proteins, predominantly in epididymal fat when EPA/DHA concentrate was admixed to a semisynthetic high-fat diet rich in -linolenic acid. This was associated with a three-fold stimulation of the expression of genes encoding regulatory factors for mitochondrial biogenesis and oxidative metabolism (peroxisome proliferator-activated receptor gamma coactivator 1 alpha [Ppargc1a, also known as Pgc1] and nuclear respiratory factor-1 [Nrf1] respectively). Expression of genes for carnitine palmitoyltransferase 1A and fatty acid oxidation was increased in epididymal but not subcutaneous fat. In the former depot, lipogenesis was depressed. Similar changes in adipose gene expression were detected after replacement of as little as 15% of lipids in the composite high-fat diet with EPA/DHA concentrate, while the development of obesity was reduced. The expression of Ppargc1a and Nrf1 was also stimulated by n-3 polyunsaturated fatty acids in 3T3-L1 cells. Conclusions/interpretation The anti-adipogenic effect of EPA/DHA may involve a metabolic switch in adipocytes that includes enhancement of -oxidation and upregulation of mitochondrial biogenesis

Published
2005

32. Mitochondrial encephalocardio-myopathy with early neonatal onset due to TMEM70 mutation

Author

Honzik, T., primary, Tesarova, M., additional, Mayr, J. A, additional, Hansikova, H., additional, Jesina, P., additional, Bodamer, O., additional, Koch, J., additional, Magner, M., additional, Freisinger, P., additional, Huemer, M., additional, Kostkova, O., additional, van Coster, R., additional, Kmoch, S., additional, Houstek, J., additional, Sperl, W., additional, and Zeman, J., additional

Published
2010
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40. Activities of cytochrome c oxidase and citrate synthase in lymphocytes of obese and normal-weight subjects.

Author

Capkova, M. and Houstek, J.

Subjects
*CYTOCHROME oxidase, *CITRATES, *LYMPHOCYTES, *OBESITY
Abstract

Analyzes the activities of mitochondrial enzymes cytochrome c oxidase (COX) and citrate synthase (CS) in isolated lymphocytes of obese and normal-weight subjects. Evidence that isolated lymphocytes from peripheral blood contribute very little to the overall metabolic turnover; Marker cells for studying the changes of mitochondrial energy converting systems in obesity.

Published
2002

43. Activity of Cytochrome cOxidase in the Right and Left Ventricular Myocardium of Male and Female Rats Exposed To Intermittent High Altitude Hypoxiaa

Author

STIEGLEROVÁ, A., DRAHOTA, Z., HOUSTEK, J., MILEROVÁ, M., PELOUCH, V., and OSTADAL, B.

Abstract

The aim of the present study was to compare the capacity of the oxidative metabolism (total activity of cytochrome c oxidase, COX) in the right and left ventricular myocardium of adult rats exposed to intermittent high altitude (IHA) hypoxia simulated in a barochamber (5,000 m, 8 hday, 5 dayswk, for a total of 32 exposures). In male and female rats, IHA induced significant increases of the right ventricular (RV) weight and protein content, whereas left ventricular (LV) weight and protein content remained unaffected. Consequently, the RVLV ratio in both sexes markedly increased. Similarly, IHA induce an increase of the total activity of COX in RV in both sexes. The specific activities of COX in homogenate as well as in isolated mitochondria were not changed in IHA-exposed animals, which indicates that the increase of total activity of COX is proportional to the increase of total protein content and RV weight.

Published
1999
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45. Characterization of sulphydryl groups of the mitochondrial phosphate translocator by a maleimide spin label

Author

Houstek, J., Bertoli, E., Stipani, I., Pavelka, S., Megli, f.M., and Palmieri, F.

Abstract

A maleimide spin label strongly inhibits the phosphate/H +symporter of rat liver mitochondria. While inducing half-maximal inhibition of transport, the spin label reacts preferentially with the SH groups of the carrier, which are at least of two types. One type of SH group is localized close to the surface of the membrane and its environment does not significantly influence the mobility of the probe. The second type of SH group is buried in the membrane, is not accessible to ascorbate or chromium oxalate and its environment greatly restricts the motion of the probe.

Published
1983
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