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1. Magnetic circular dichroism in X-ray fluorescence of Heusler alloys at threshold excitation

Author

Yablonskikh, M. V., Ezhov, A. V., Grebennikov, V. I., Yarmoshenko, Yu. M., Kurmaev, E. Z., Butorin, S. M., Duda, L. -C., Sothe, C., Kaambre, T., Magnuson, M., Nordgren, J., Plogmann, S., and Neumann, M.

Subjects
Condensed Matter - Materials Science
Abstract

The results of fluorescence measurements of magnetic circular dichroism (MCD) in Mn L_2,L_3 X-ray emission and absorption for Heusler alloys NiMnSb and Co2MnSb are presented. Very intense resonance Mn L_3 emission is found at the Mn 2p_3/2 threshold and is attributed to a peculiarity of the threshold excitation in materials with the half-metallic character of the electronic structure. A theoretical model for the description of resonance scattering of polarized x-rays is suggested., Comment: 3 pages, 2 figures. Discussed at conferences, submitting process in progress

Published
1999
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4. Cardiac metabolism as a driver and therapeutic target of myocardial infarction

Author

Zuurbier, C.J. Bertrand, L. Beauloye, C.R. Andreadou, I. Ruiz-Meana, M. Jespersen, N.R. Kula-Alwar, D. Prag, H.A. Eric Botker, H. Dambrova, M. Montessuit, C. Kaambre, T. Liepinsh, E. Brookes, P.S. Krieg, T.

Abstract

Reducing infarct size during a cardiac ischaemic-reperfusion episode is still of paramount importance, because the extension of myocardial necrosis is an important risk factor for developing heart failure. Cardiac ischaemia-reperfusion injury (IRI) is in principle a metabolic pathology as it is caused by abruptly halted metabolism during the ischaemic episode and exacerbated by sudden restart of specific metabolic pathways at reperfusion. It should therefore not come as a surprise that therapy directed at metabolic pathways can modulate IRI. Here, we summarize the current knowledge of important metabolic pathways as therapeutic targets to combat cardiac IRI. Activating metabolic pathways such as glycolysis (eg AMPK activators), glucose oxidation (activating pyruvate dehydrogenase complex), ketone oxidation (increasing ketone plasma levels), hexosamine biosynthesis pathway (O-GlcNAcylation; administration of glucosamine/glutamine) and deacetylation (activating sirtuins 1 or 3; administration of NAD+-boosting compounds) all seem to hold promise to reduce acute IRI. In contrast, some metabolic pathways may offer protection through diminished activity. These pathways comprise the malate-aspartate shuttle (in need of novel specific reversible inhibitors), mitochondrial oxygen consumption, fatty acid oxidation (CD36 inhibitors, malonyl-CoA decarboxylase inhibitors) and mitochondrial succinate metabolism (malonate). Additionally, protecting the cristae structure of the mitochondria during IR, by maintaining the association of hexokinase II or creatine kinase with mitochondria, or inhibiting destabilization of FOF1-ATPase dimers, prevents mitochondrial damage and thereby reduces cardiac IRI. Currently, the most promising and druggable metabolic therapy against cardiac IRI seems to be the singular or combined targeting of glycolysis, O-GlcNAcylation and metabolism of ketones, fatty acids and succinate. © 2020 The Authors. Journal of Cellular and Molecular Medicine published by Foundation for Cellular and Molecular Medicine and John Wiley & Sons Ltd

Published
2020

5. Generating reference values on mitochondrial respiration in permeabilized muscle fibers

Author

Béatrice, Chabi, Ost, M, Gama-Perez, P, Dahdah, N, Lemieux, H, Holody, CD, Carpenter, RG, Tepp, K, Puurand, M, Kaambre, T, Dubouchaud, H, Cortade, F, Pesta, D, Calabria, E, Casado, M, Fernandez-Ortiz, M, Acuña-Castroviejo, D, Villena, JA, Grefte, S, Keijer, J, O'Brien, K, Sowton, A, Murray, AJ, Campbell, MD, Marcinek, DJ, Wüst, R, Dayanidhi, S, Gnaiger, E, Doerrier, C, Garcia-Roves PM, PM, Nollet, E, Dynamique Musculaire et Métabolisme (DMEM), Université de Montpellier (UM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), German Institute of Human Nutrition Potsdam-Rehbrücke (DIfE), Institut d'Investigació Biomèdica de Bellvitge [Barcelone] (IDIBELL), University of Alberta, National Institute of Chemical Physics and Biophysics = Keemilise ja bioloogilise füüsika instituut [Estonie] (NICPB | KBFI), Laboratoire de bioénergétique fondamentale et appliquée (LBFA), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut National de la Recherche Agronomique (INRA)-Université de Montpellier (UM), German Diabetes Center, Section of Neurology, Department of Neurological and Vision Sciences, University of Verona, Policlin, Instituto de biomedicina [Valencia] (IBV), Consejo Superior de Investigaciones Científicas [Madrid] (CSIC), University of Granada [Granada], Vall d’Hebron Research Institute (VHIR), Human and Animal Physiology [Wageningen, The Netherlands], Wageningen University [The Netherlands], University of Cambridge [UK] (CAM), Department of Radiology, University of Washington, Faculty of Behavioural and Movement Sciences [Amsterdam, The Netherlands], Rehabilitation Institute of Chicago (RIC), Rehabilitation Institute of Chicago [USA], Oroboros Instruments, Mitochondrial Physiology Society, Laboratory of Fundamental and Applied Bioenergetics = Laboratoire de bioénergétique fondamentale et appliquée (LBFA), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Università degli studi di Verona = University of Verona (UNIVR), Universidad de Granada = University of Granada (UGR), Wageningen University and Research [Wageningen] (WUR), and Raynaud, Christelle

Subjects
[SDV] Life Sciences [q-bio], mitochondrial respiration, [SDV]Life Sciences [q-bio], ComputingMilieux_MISCELLANEOUS
Abstract

Permeabilized muscle fibers (pfi) are widely used to assess mitochondrial (mt) respiratory function in skeletal muscle of various models in different physiological and pathological conditions. Facing the numerous data available for mt-respiration from the literature, it remains challenging to determine what the right values are for a specific respiratory protocol. Moreover, mt-respiration values are highly dependent on pfi preparation, which required good technical skills. In the frame of COST Action MITOEAGLE, one of the objectives of WG2 is the generation of reference values for mitochondrial respirometry in permeabilized skeletal muscle sample preparations. The idea is that new researchers in the field follow a reference protocol and check if their values are in an acceptable range. This approach could serve to test researchers’ technical skills and therefore determine if they are proficient enough to perform their own experiments with confidence.

Published
2019

6. 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

7. 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
Full Text
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8. 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

10. 2102Ep embryonal carcinoma cells have compromised respiration and shifted bioenergetic profile distinct from H9 human embryonic stem cells

Author

Ounpuu, L., Klepinin, A., Pook, M., Teino, I., Peet, N., Paju, K., Tepp, K., Chekulayev, V., Shevchuk, I., Kõks, S., Maimets, T., Kaambre, T., Ounpuu, L., Klepinin, A., Pook, M., Teino, I., Peet, N., Paju, K., Tepp, K., Chekulayev, V., Shevchuk, I., Kõks, S., Maimets, T., and Kaambre, T.

Abstract

Recent studies have shown that cellular bioenergetics may be involved in stem cell differentiation. Considering that during cancerogenesis cells acquire numerous properties of stem cells, it is possible to assume that the energy metabolism in tumorigenic cells might be differently regulated. The aim of this study was to compare the mitochondrial bioenergetic profile of normal pluripotent human embryonic stem cells (hESC) and relatively nullipotent embryonal carcinoma cells (2102Ep cell line). We examined three parameters related to cellular bioenergetics: phosphotransfer system, aerobic glycolysis, and oxygen consumption. Activities and expression levels of main enzymes that facilitate energy transfer were measured. The oxygen consumption rate studies were performed to investigate the respiratory capacity of cells. 2102Ep cells showed a shift in energy distribution towards adenylate kinase network. The total AK activity was almost 3 times higher in 2102Ep cells compared to hESCs (179.85±5.73 vs 64.39±2.55mU/mg of protein) and the expression of AK2 was significantly higher in these cells, while CK was downregulated. 2102Ep cells displayed reduced levels of oxygen consumption and increased levels of aerobic glycolysis compared to hESCs. The compromised respiration of 2102Ep cells is not the result of increased mitochondrial mass, increased proton leak, and reduced respiratory reserve capacity of the cells or impairment of respiratory chain complexes. Our data showed that the bioenergetic profile of 2102Ep cells clearly distinguishes them from normal hESCs. This should be considered when this cell line is used as a reference, and highlight the importance of further research concerning energy metabolism of stem cells.

Published
2017

11. Systems level regulation via metabolic cycles: role of creatine and phosphotransfer cycles

Author

Saks, V., Schlattner, Uwe, Tokarska-Schlattner, Malgorzata, Wallimann, T., Bagur Quetglas, Rafaela, Zorman, Sarah, Pelosse, Martin, Dos, P., Boucher, F., Kaambre, T., Guzun, Rita, Laboratoire de bioénergétique fondamentale et appliquée (LBFA), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Santé et de la Recherche Médicale (INSERM), Physiologie cardio-Respiratoire Expérimentale Théorique et Appliquée (TIMC-IMAG-PRETA), Techniques de l'Ingénierie Médicale et de la Complexité - Informatique, Mathématiques et Applications, Grenoble - UMR 5525 (TIMC-IMAG), VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF), M. Aon, V. Saks, U. Schlattner, Hamant, Sarah, and M. Aon, V. Saks, U. Schlattner

Subjects
[SDV] Life Sciences [q-bio], [SDV]Life Sciences [q-bio], ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2013

12. The creatine kinase phosphotransfer network: thermodynamic and kinetic considerations, the impact of the mitochondrial outer membrane and modelling approaches

Author

Saks, V., Kaambre, T., Guzun, R., Anmann, T., Sikk, P., Schlattner, U., Wallimann, T., Aliev, M., Marko Vendelin, Hamant, Sarah, Laboratory of Bioenergetics, National Institute of Chemical Physics and Biophysics = Keemilise ja bioloogilise füüsika instituut [Estonie] (NICPB | KBFI), Laboratoire de bioénergétique fondamentale et appliquée (LBFA), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Santé et de la Recherche Médicale (INSERM), Department of Biology, Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] (ETH Zürich)-Institute of Cell Biology, Institute of Experimental Cardiology, and Cardiology Research Center

Subjects
MESH: Myocardium, Phosphocreatine, MESH: Phosphocreatine, Models, Biological, Mitochondria, Heart, Adenosine Triphosphate, Oxygen Consumption, MESH: Adenosine Triphosphate, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Animals, Humans, MESH: Animals, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH: Oxygen Consumption, Creatine Kinase, MESH: Creatine Kinase, MESH: Humans, MESH: Adenosine Diphosphate, MESH: Kinetics, Myocardium, MESH: Energy Metabolism, MESH: Models, Biological, Adenosine Diphosphate, Kinetics, Thermodynamics, MESH: Mitochondria, Heart, MESH: Thermodynamics, MESH: Mitochondrial ADP, ATP Translocases, Energy Metabolism, Mitochondrial ADP, ATP Translocases
Abstract

International audience; In this review, we summarize the main structural and functional data on the role of the phosphocreatine (PCr)--creatine kinase (CK) pathway for compartmentalized energy transfer in cardiac cells. Mitochondrial creatine kinase, MtCK, fixed by cardiolipin molecules in the vicinity of the adenine nucleotide translocator, is a key enzyme in this pathway. Direct transfer of ATP and ADP between these proteins has been revealed both in experimental studies on the kinetics of the regulation of mitochondrial respiration and by mathematical modelling as a main mechanism of functional coupling of PCr production to oxidative phosphorylation. In cells in vivo or in permeabilized cells in situ, this coupling is reinforced by limited permeability of the outer membrane of the mitochondria for adenine nucleotides due to the contacts with cytoskeletal proteins. Due to these mechanisms, at least 80% of total energy is exported from mitochondria by PCr molecules. Mathematical modelling of intracellular diffusion and energy transfer shows that the main function of the PCr-CK pathway is to connect different pools (compartments) of ATP and, by this way, to overcome the local restrictions and diffusion limitation of adenine nucleotides due to the high degree of structural organization of cardiac cells.

Published
2007

13. Bulk and surface charge states of K3C60

Author

Schiessling, J, Kjeldgaard, L, Kaambre, T, Marenne, [No Value], O'Shea, JN, Schnadt, J, Glover, CJ, Nagasono, M, Nordlund, D, Garnier, MG, Qian, L, Rubensson, JE, Rudolf, P, Martensson, N, Nordgren, J, Bruhwiler, PA, Marenne, I., Käämbre, T., O’Shea, J.N., Mårtensson, N., Surfaces and Thin Films, and Zernike Institute for Advanced Materials

Subjects
PHOTOEMISSION SPECTRA, BAND-STRUCTURE, PHASE-TRANSITION, SOLID C-60, RAY-ABSORPTION-SPECTROSCOPY, COULOMB INTERACTION, DOPED C-60 MONOLAYER, ENERGY-ELECTRON-DIFFRACTION, MEAN FREE PATHS, FULLERIDES
Abstract

We detect a significant angle-dependence in the core level and valence line shapes of photoelectron spectra of single crystal K3C60. This allows the identification of bulk and surface components in the data, and allows us to explain the anomalous line shapes observed for this system. The states near the Fermi level are associated with the bulk of the sample. There is strong evidence of an insulating surface layer, which we ascribe to intermolecular electron correlations. These results simplify the interpretation of previous, apparently conflicting observations.

Published
2005

14. Insulating surface layer on single crystal K3C60

Author

Schiessling, J., Kjeldgaard, L., Kaambre, T., Marenne, I., Qian, L., O'Shea, J.N., Schnadt, J., Garnier, M.G., Nordlund, D., Nagasono, M., Glover, C.J., Rubensson, J.E., Martensson, N., Rudolf, Petra, Nordgren, J., Bruhwiler, P.A., Käämbre, T., O’Shea, J.N., Mårtensson, N., Marenne, [No Value], Oppervlakken en Dunne Lagen, and Zernike Institute for Advanced Materials

Subjects
PHASES, PHOTOEMISSION SPECTRA, ELECTRONIC STATES, SUPERCONDUCTIVITY, METAL, BAND-STRUCTURE, ComputingMethodologies_DOCUMENTANDTEXTPROCESSING, DOPED C-60, FILMS, GeneralLiterature_REFERENCE(e.g.,dictionaries,encyclopedias,glossaries), FULLERIDES, KXC60
Published
2004

15. Modular organization of cardiac energy metabolism: energy conversion, transfer and feedback regulation

Author

Guzun, R., primary, Kaambre, T., additional, Bagur, R., additional, Grichine, A., additional, Usson, Y., additional, Varikmaa, M., additional, Anmann, T., additional, Tepp, K., additional, Timohhina, N., additional, Shevchuk, I., additional, Chekulayev, V., additional, Boucher, F., additional, Dos Santos, P., additional, Schlattner, U., additional, Wallimann, T., additional, Kuznetsov, A. V., additional, Dzeja, P., additional, Aliev, M., additional, and Saks, V., additional

Published
2014
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16. Intracellular energetic units in red muscle cells

Author

Saks, V A, Kaambre, T, Sikk, P, Eimre, M, Orlova, E, Paju, K, Piirsoo, A, Appaix, F, Kay, L, Regitz-Zagrosek, V, Fleck, E, Seppet, E, Bioénergétique fondamentale et appliquée, Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratory of Bioenergetics, National Institute of Chemical Physics and Biophysics = Keemilise ja bioloogilise füüsika instituut [Estonie] (NICPB | KBFI), Department of Pathophysiology, University of Tartu, Department of Human Biology and Genetics, Deutsche Herzzentrum, and Hamant, Sarah

Subjects
Male, MESH: Myocardium, MESH: Rats, MESH: Microscopy, Electron, In Vitro Techniques, Models, Biological, Biochemistry, Mitochondria, Heart, 03 medical and health sciences, 0302 clinical medicine, Animals, MESH: Animals, Rats, Wistar, Muscle, Skeletal, Molecular Biology, 030304 developmental biology, 0303 health sciences, MESH: Muscle, Skeletal, MESH: Adenosine Diphosphate, MESH: Creatine, MESH: Kinetics, Myocardium, MESH: Energy Metabolism, MESH: Models, Biological, MESH: Mitochondria, Muscle, Heart, Cell Biology, MESH: Rats, Wistar, Creatine, MESH: Male, Mitochondria, Muscle, Rats, Adenosine Diphosphate, MESH: Heart, Kinetics, Microscopy, Electron, MESH: Mitochondria, Heart, Energy Metabolism, 030217 neurology & neurosurgery, Research Article
Abstract

International audience; The kinetics of regulation of mitochondrial respiration by endogenous and exogenous ADP in muscle cells in situ was studied in skinned cardiac and skeletal muscle fibres. Endogenous ADP production was initiated by addition of MgATP; under these conditions the respiration rate and ADP concentration in the medium were dependent on the calcium concentration, and 70-80% of maximal rate of respiration was achieved at ADP concentration below 20 microM in the medium. In contrast, when exogenous ADP was added, maximal respiration rate was observed only at millimolar concentrations. An exogenous ADP-consuming system consisting of pyruvate kinase (PK; 20-40 units/ml) and phosphoenolpyruvate (PEP; 5 mM), totally suppressed respiration activated by exogenous ADP, but the respiration maintained by endogenous ADP was not suppressed by more than 20-40%. Creatine (20 mM) further activated respiration in the presence of ATP and PK+PEP. Short treatment with trypsin (50-500 nM for 5 min) decreased the apparent K(m) for exogenous ADP from 300-350 microM to 50-60 microM, increased inhibition of respiration by PK+PEP system up to 70-80%, with no changes in MgATPase activity and maximal respiration rates. Electron-microscopic observations showed detachment of mitochondria and disordering of the regular structure of the sarcomere after trypsin treatment. Two-dimensional electrophoresis revealed a group of at least seven low-molecular-mass proteins in cardiac skinned fibres which were very sensitive to trypsin and not present in glycolytic fibres, which have low apparent K(m) for exogenous ADP. It is concluded that, in oxidative muscle cells, mitochondria are incorporated into functional complexes ('intracellular energetic units') with adjacent ADP-producing systems in myofibrils and in sarcoplasmic reticulum, probably due to specific interaction with cytoskeletal elements responsible for mitochondrial distribution in the cell. It is suggested that these complexes represent the basic pattern of organization of muscle-cell energy metabolism.

Published
2001

17. Angle dependent photoemission study of distilled K3C60

Author

Schiessling, J., Bruhwiler, P. A., Kjeldgaard, L., Kaambre, T., Marenne, I., Quian, L., Shea, J. N. O., Garnier, M. G., Nordlund, D., Nagasono, M., Petra Rudolf, Rubensson, J. E., Martensson, N., Nordgren, J., and Surfaces and Thin Films

Published
2001

19. Closed source experimental system for soft x-ray spectroscopy of radioactive materials

Author

Modin, A., Butorin, S. M., Vegelius, J., Olsson, Anders, Englund, C. -J., Andersson, J., Werme, L., Nordgren, J., Kaambre, T., Skarnemark, G., Burakov, B. E., Modin, A., Butorin, S. M., Vegelius, J., Olsson, Anders, Englund, C. -J., Andersson, J., Werme, L., Nordgren, J., Kaambre, T., Skarnemark, G., and Burakov, B. E.

Abstract

An instrumental and experimental setup for soft x-ray spectroscopy meeting the requirements of a closed source for radioactivity is described. The system consists of a vacuum sealed cell containing the sample, mounted on a tubing system to ensure compatibility with most standard manipulators. The soft x rays penetrate a thin x-ray window separating the interior of the cell from the vacuum in the experimental chamber. Our first results for single crystal PuO2 confirm the feasibility of experiments using the setup. The results are consistent with results of first principles calculations and previously recorded spectra obtained using a standard open source setup. The results show that the closed source experimental system can be used to collect valuable experimental data from radioactive materials.

Published
2008
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20. Adsorption-induced gap states of h-BN on metal surfaces

Author

Preobrajenski, A. B., Krasnikov, S. A., Vinogradov, A. S., Ng, May Ling, Kaambre, T., Cafolla, A. A., Mårtensson, N., Preobrajenski, A. B., Krasnikov, S. A., Vinogradov, A. S., Ng, May Ling, Kaambre, T., Cafolla, A. A., and Mårtensson, N.

Abstract

The formation of hexagonal boron nitride (h-BN) monolayers on Ni(111), Rh(111), and Pt(111) has been studied by a combination of x-ray emission, angle-resolved valence band photoemission, and x-ray absorption in search for interface-induced gap states of h-BN. A significant density of both occupied and unoccupied gap states with N 2p and B 2p characters is observed for h-BN/Ni(111), somewhat less for h-BN/Rh(111) and still less for h-BN/Pt(111). X-ray emission shows that the h-BN monolayer is chemisorbed strongly on Ni(111) and very weakly on Pt(111). We associate the gap states of h-BN adsorbed on the transition metal surfaces with the orbital mixing and electron sharing at the interface because their density increases with the growing strength of chemisorption.

Published
2008
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21. Resonant inelastic X-ray scattering at the Be 1s edge in BeO

Author

Kaambre, T., Kikas, A., Kooser, K., Kisand, V., Kirm, M., Saar, A., Nommiste, E., Ivanov, V., Pustovarov, V., Martinson, I., Пустоваров, В. А., Kaambre, T., Kikas, A., Kooser, K., Kisand, V., Kirm, M., Saar, A., Nommiste, E., Ivanov, V., Pustovarov, V., Martinson, I., and Пустоваров, В. А.

Published
2007

24. Resonant inelastic x-ray scattering at the F 1s photoabsorption edge in LiF : Interplay of excitonic and conduction states, and Stokes' doubling

Author

Kikas, A., Kaambre, T., Saar, A., Kooser, K., Nommiste, E., Martinson, I., Kimberg, Victor, Polyutov, Sergey, Gel'mukhanov, Faris, Kikas, A., Kaambre, T., Saar, A., Kooser, K., Nommiste, E., Martinson, I., Kimberg, Victor, Polyutov, Sergey, and Gel'mukhanov, Faris

Abstract

The excitation-decay processes at the F 1s photoabsorption edge in LiF crystal are studied using resonant inelastic x-ray scattering spectroscopy. The Raman-type linear dispersion and the narrowing of the x-ray fluorescence peak are observed at resonant excitation. A theoretical model based on the Kramers-Heisenberg formula describes well the main features in fluorescence spectra and allows one to separate the contributions of the exciton and the conduction states in the scattering spectra. At the same time, the role of the shape of the spectral distribution within the incident radiation is emphasized as being critically sensitive to the number, kind, and onset of the spectral features which finally appear in the scattering spectra at a particular incident photon energy, particularly in the subthreshold excitation region., QC 20110926

Published
2004
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26. Bond formation in titanium fulleride compounds studied through x-ray emission spectroscopy

Author

Nyberg, M., Luo, Yi, Qian, L., Rubensson, J. E., Sathe, C., Ding, D., Guo, J. H., Kaambre, T., Nordgren, J., Nyberg, M., Luo, Yi, Qian, L., Rubensson, J. E., Sathe, C., Ding, D., Guo, J. H., Kaambre, T., and Nordgren, J.

Abstract

The geometric and electronic structures of titanium fulleride complexes have been studied at the gradient corrected density-functional theory level by using various C60Tix (x=1,2) clusters. The cluster with the Ti atom binding on the six-ring site (eta (6)) Of the fullerene is shown to be lower in energy than those with Ti atom adsorbed on either five-ring (eta (5)) Or bridge(eta (2)) sites. The bond formation for titanium fulleride has further been examined by calculated nonresonant, resonant, and off-resonant . x-ray emission spectra of the clusters, and a comparison to the experimental counterpart. The examination shows that only the theoretical spectra of clusters with a six-ring adsorption site are in close agreement with the experimental x-ray emission spectra of titanium fulleride films. Our results indicate that off-resonant x-ray emission spectra provide an excellent basis for the probing of the bonding between metals and organic molecules., QC 20100525

Published
2001
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27. Magnetic circular dichroism in X-ray fluorescence of Heusler alloys at threshold excitation

Author

Yablonskikh, MV, Grebennikov, VI, Yarmoshenko, YM, Kurmaev, EZ, Butorin, SM, Duda, LC, Sathe, C, Kaambre, T, Magnuson, Martin, Nordgren, J, Plogmann, S, Neumann, M, Yablonskikh, MV, Grebennikov, VI, Yarmoshenko, YM, Kurmaev, EZ, Butorin, SM, Duda, LC, Sathe, C, Kaambre, T, Magnuson, Martin, Nordgren, J, Plogmann, S, and Neumann, M

Abstract

The results of fluorescence measurements of magnetic circular dichroism (MCD) in Mn L-2,L-3 X-ray emission and absorption for Heusler alloys NiMnSb and Co2MnSb are presented. Very intense resonance Mn L-3 emission is found at the Mn 2P(3/2) threshold and, Addresses: Yablonskikh MV, Russian Acad Sci, Inst Met Phys, GSP-170, Yekaterinburg 620219, Russia. Russian Acad Sci, Inst Met Phys, Yekaterinburg 620219, Russia. Univ Uppsala, Dept Phys, S-75121 Uppsala, Sweden. Univ Osnabruck, Fachbereich Phys, D-49069 O

Published
2001

28. Bond formation in titanium fulleride compounds studied through x-ray emission spectroscopy - art. no. 115117

Author

Nyberg, M, Luo, Yi, Qian, L, Rubensson, JE, Sathe, C, Ding, D, Guo, JH, Kaambre, T, Nordgren, J, Nyberg, M, Luo, Yi, Qian, L, Rubensson, JE, Sathe, C, Ding, D, Guo, JH, Kaambre, T, and Nordgren, J

Abstract

The geometric and electronic structures of titanium fulleride complexes have been studied at the gradient corrected density-functional theory level by using various C60Tix (x=1,2) clusters. The cluster with the Ti atom binding on the six-ring site (eta (6, Addresses: Nyberg M, Stockholm Univ, Dept Phys, POB 6730, S-11385 Stockholm, Sweden. Stockholm Univ, Dept Phys, S-11385 Stockholm, Sweden. Univ Uppsala, Dept Phys, S-75121 Uppsala, Sweden. Jilin Univ, Inst Atom & Mol Phys, State Key Lab Superhard Mat, Cha

Published
2001

29. Resonant photoemission of CoCl2

Author

Kikas, A, Ruus, R, Saar, A, Nommiste, E, Kaambre, T, Sundin, S, Kikas, A, Ruus, R, Saar, A, Nommiste, E, Kaambre, T, and Sundin, S

Abstract

We present the results of a study of the resonant photoemission from polycrystalline in situ evaporated thin him of CoCl2 excited at 2p photoabsorption edges of Co and Cl. At the Co 2p-->3d resonance strong enhancement was observed for the Co 3p, valence, Addresses: Kikas A, Tartu State Univ, Inst Phys, Riia 142, EE-2400 Tartu, Estonia. Tartu State Univ, Inst Phys, EE-2400 Tartu, Estonia. Univ Oulu, Dept Phys Sci, FIN-90570 Oulu, Finland. Univ Uppsala, Dept Phys, S-75121 Uppsala, Sweden.

Published
1999

30. Non-destructive chemical analysis of sandwich structures by means of soft X-ray emission

Author

Galnander, B, Kaambre, T, Blomquist, P, Nilsson, E, Guo, J, Rubensson, JE, Nordgren, J, Galnander, B, Kaambre, T, Blomquist, P, Nilsson, E, Guo, J, Rubensson, JE, and Nordgren, J

Abstract

Soft X-ray emission spectroscopy provides information about elemental composition, including the light elements, as well as the chemical bonding. The probe depth reaches hundreds of nanometers but under certain conditions considerable surface sensitivity, Addresses: Galnander B, Univ Uppsala, Dept Mat Sci, Box 534, S-75121 Uppsala, Sweden. Univ Uppsala, Dept Mat Sci, S-75121 Uppsala, Sweden. Univ Uppsala, Dept Phys, S-75121 Uppsala, Sweden.

Published
1999

32. Mapping of molecular C-17 indandione-1,3 pyridinium betaine adsorbates on fused silica by surface second harmonic generation

Author

Ding, D, Kaambre, T, Ljungstrom, S, Chen, Y, Siegbahn, K, Wistus, E, Swensson, P, Mukhtar, E, Ding, D, Kaambre, T, Ljungstrom, S, Chen, Y, Siegbahn, K, Wistus, E, Swensson, P, and Mukhtar, E

Abstract

Surface second harmonic generation (SHG) has been utilized to obtain information such as orientation, concentration distribution and desorption of C-17 indandione-1,3 pyridinium betaine (IPB) thin films prepared by the Langmuir-Blodgett (LB) technique on, Addresses: UNIV UPPSALA, ESCA, LASER LAB, S-75121 UPPSALA, SWEDEN. UNIV UPPSALA, DEPT CHEM PHYS, S-75121 UPPSALA, SWEDEN.

Published
1996

33. Metabolic consequences of functional complexes of mitochondria, myofibrils and sarcoplasmic reticulum in muscle cells.

Author

Andrienko, T., Kuznetsov, A.V., Kaambre, T., Usson, Y., Orosco, A., Appaix, F., Tiivel, T., Sikk, P., Vendelin, M., Margreiter, R., and Saks, V.A.

Subjects
MUSCLE cells, MITOCHONDRIA, SARCOPLASMIC reticulum
Abstract

Regulation of mitochondrial respiration both by endogenous and exogenous ADP in the cells in situ was studied in isolated and permeabilized cardiomyocytes, permeabilized cardiac fibers and 'ghost' fibers (all with a diameter of 10-20 µm) at different (0-3 µmol 1[sup -1]) free Ca[sup 2+] concentrations in the medium. In all these preparations, the apparent K[sub m] of mitochondrial respiration for exogenous ADP at free Ca[sup 2+] concentrations of 0-0.1 µmol l[sup -1] was very high, in the range of 250-350 µmol 1[sup -1], in contrast to isolated mitochondria in vitro (apparent K[sub m] for ADP is approximately 20 µmol l[sup -1]). An increase in the free Ca[sup 2+] concentration (up to 3 µmol l[sup -1], which is within physiological range), resulted in a very significant decrease of the apparent K[sub m] value to 20-30 µmol l[sup -1], a decrease of V[sub max] of respiration in permeabilized intact fibers and a strong contraction of sarcomeres. In ghost cardiac fibers, from which myosin was extracted but mitochondria were intact, neither the high apparent K[sub m] for ADP (300-350 µmol 1[sup -1]) nor V[sub max] of respiration changed in the range of free Ca[sup 2+] concentration studied, and no sarcomere contraction was observed. The exogenous-ADP-trapping system (pyruvate kinase + phosphoenolpyruvate) inhibited endogenous-ADP-supported respiration in permeabilized cells by no more than 40%, and this inhibition was reversed by creatine due to activation of mitochondrial creatine kinase. These results are taken to show strong structural associations (functional complexes) among mitochondria, sarcomeres and sarcoplasmic reticulum. Inside these complexes, mitochondrial functional state is controlled by channeling of ADP, mostly via energy- and phosphoryltransfer networks, and apparently depends on the state of sarcomere structures. [ABSTRACT FROM AUTHOR]

Published
2003
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43. Combined luminescence and X-ray emission study of self-trapped excitons in oxides

Author

Ivanov, V, Kikas, A, Kaambre, T, Kirm, M, Kuusik, I, and Pustovarov, V

Abstract

The experimental study of relaxation of anion and cation excitons at the selective VUV-(valence) and soft X-ray (inner-shell) excitations for binary BeO crystal and multicomponent oxide crystals Be2SiO4, Al2Be3Si6O18 and Y2SiO5 is presented. Results show that the relaxation during the time-scale of decay of short-living anion and cation excitations leads to creation of self-trapped excitons at the corresponding low-symmetry (tetrahedral) local structural units of crystalline lattice. This can be caused by increase of dynamical instability of such a local structural units (in comparison with high symmetry ones), which facilitates self-trapping processes in these systems.

Published
2010

44. Energy Metabolism Behavior and Response to Microenvironmental Factors of the Experimental Cancer Cell Models Differ From That of Actual Human Tumors.

Author

Moreno-Sanchez R, Vargas-Navarro JL, Padilla-Flores JA, Robledo-Cadena DX, Granados-Rivas JC, Taba R, Terasmaa A, Auditano GL, Kaambre T, and Rodríguez-Enríquez S

Abstract

Analysis of the biochemical differences in the energy metabolism among bi-dimensional (2D) and tri-dimensional (3D) cultured cancer cell models and actual human tumors was undertaken. In 2D cancer cells, the oxidative phosphorylation (OxPhos) fluxes range is 2.5-19 nmol O2/min/mg cellular protein. Hypoxia drastically decreased OxPhos flux by 2-3 times in 2D models, similar to what occurs in mature multicellular tumor spheroids (MCTS), a representative 3D cancer cell model. However, mitochondrial protein contents and enzyme activities were significantly different between both models. Moreover, glycolytic fluxes were also significantly different between 2D and MCTS. The glycolytic flux range in 2D models is 1-34 nmol lactate/min/mg cellular protein, whereas in MCTS the range of glycolysis fluxes is 60-80 nmol lactate/min/mg cellular. In addition, sensitivity to anticancer canonical and metabolic drugs was greater in MCTS than in 2D. Actual solid human tumor samples show lower (1.6-4.5 times) OxPhos fluxes compared to normoxic 2D cancer cell cultures. These observations indicate that tridimensional organization provides a unique microenvironment affecting tumor physiology, which has not been so far faithfully reproduced by the 2D environment. Thus, the analysis of the resemblances and differences among cancer cell models undertaken in the present study raises caution on the interpretation of results derived from 2D cultured cancer cells when they are extended to clinical settings. It also raises awareness about detecting which biological and environmental factors are missing in 2D and 3D cancer cell models to be able to reproduce the actual human tumor behavior., (Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.net.)

Published
2024
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45. Synergistic celecoxib and dimethyl-celecoxib combinations block cervix cancer growth through multiple mechanisms.

Author

Robledo-Cadena DX, Pacheco-Velázquez SC, Vargas-Navarro JL, Padilla-Flores JA, López-Marure R, Pérez-Torres I, Kaambre T, Moreno-Sánchez R, and Rodríguez-Enríquez S

Subjects
Humans, Female, HeLa Cells, Cisplatin pharmacology, Cell Line, Tumor, Paclitaxel pharmacology, Mitochondria metabolism, Mitochondria drug effects, Cell Survival drug effects, Antineoplastic Agents pharmacology, Glycolysis drug effects, Celecoxib pharmacology, Uterine Cervical Neoplasms metabolism, Uterine Cervical Neoplasms drug therapy, Uterine Cervical Neoplasms pathology, Cell Proliferation drug effects, Drug Synergism, Reactive Oxygen Species metabolism, Mitophagy drug effects, Apoptosis drug effects
Abstract

Objective: The synergistic inhibitory effect of celecoxib (CXB) and dimethyl-celecoxib (DMC) plus paclitaxel (PA) or cisplatin (CP) on human cervix HeLa and SiHa cells was assessed at multiple cellular levels in order to elucidate the biochemical mechanisms triggered by the synergistic drug combinations., Methods: The effect of CXB (5 μM)/CP (2 μM) or CXB (5 μM)/PA (15 μM) and DMC (15 μM)/CP (5 μM) or DMC (15 μM)/PA (20 μM) for 24 h was assayed on cancer cell proliferation, energy metabolism, mitophagy, ROS production, glycoprotein-P activity, DNA stability and apoptosis/necrosis., Results: Drug combinations synergistically decreased HeLa and SiHa cell proliferation (>75%) and arrested cellular cycle by decreasing S and G2/M phases as well as the Ki67 content (HeLa) by 7.5-30 times. Cell viability was preserved (>90%) and no apparent effects on non-cancer cell growth were observed. Mitochondrial and glycolytic protein contents (44-95%) and ΔΨm (45-50%) in HeLa cells and oxidative phosphorylation and glycolysis fluxes (70-90%) in HeLa and SiHa cells were severely decreased, which in turn promoted a drastic fall in the ATP supply (85-88%). High levels of mitophagy proteins in HeLa cells and active mitochondrial digestion in HeLa and SiHa cells was observed. Mitochondrial fission and microtubule proteins were also affected. Intracellular ROS content (2-2.3-fold) and ROS production was stimulated (2.3-4 times), whereas content and activity of glycoprotein-P (45-85%) were diminished. DNA fragmentation was not observed and apoptosis/necrosis was not detected suggesting that cell death could be mainly associated to mitophagy induction., Conclusions: CXB or DMC combination with canonical chemotherapy may be a promising chemotherapy strategy against cervical cancer growth, because it can selectively block multiple cell processes including inhibition of energy pathways and in consequence ATP-dependent processes such as cell proliferation, glycoprotein-P activity, ROS production and mitophagy, with no apparent effects on non-cancer cells., Competing Interests: The authors have declared that no competing interests exist., (Copyright: © 2024 Robledo-Cadena et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.)

Published
2024
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46. Repurposing auranofin and meclofenamic acid as energy-metabolism inhibitors and anti-cancer drugs.

Author

Rodríguez-Enríquez S, Robledo-Cadena DX, Pacheco-Velázquez SC, Vargas-Navarro JL, Padilla-Flores JA, Kaambre T, and Moreno-Sánchez R

Subjects
Humans, Cell Line, Tumor, Cell Movement drug effects, HeLa Cells, Mitophagy drug effects, Glycolysis drug effects, Oxygen Consumption drug effects, Auranofin pharmacology, Drug Repositioning, Antineoplastic Agents pharmacology, Cell Proliferation drug effects, Energy Metabolism drug effects, Mitochondria drug effects, Mitochondria metabolism, Meclofenamic Acid pharmacology, Oxidative Phosphorylation drug effects
Abstract

Objective: Cytotoxicity of the antirheumatic drug auranofin (Aur) and the non-steroidal anti-inflammatory drug meclofenamic acid (MA) on several cancer cell lines and isolated mitochondria was examined to assess whether these drugs behave as oxidative phosphorylation inhibitors., Methods: The effect of Aur or MA for 24 h was assayed on metastatic cancer and non-cancer cell proliferation, energy metabolism, mitophagy and metastasis; as well as on oxygen consumption rates of cancer and non-cancer mitochondria., Results: Aur doses in the low micromolar range were required to decrease proliferation of metastatic HeLa and MDA-MB-231 cells, whereas one or two orders of magnitude higher levels were required to affect proliferation of non-cancer cells. MA doses required to affect cancer cell growth were one order of magnitude higher than those of Aur. At the same doses, Aur impaired oxidative phosphorylation in isolated mitochondria and intact cells through mitophagy induction, as well as glycolysis. Consequently, cell migration and invasiveness were severely affected. The combination of Aur with very low cisplatin concentrations promoted that the effects on cellular functions were potentiated., Conclusion: Aur surges as a highly promising anticancer drug, suggesting that efforts to establish this drug in the clinical treatment protocols are warranted and worthy to undertake., Competing Interests: The authors have declared that no competing interests exist., (Copyright: © 2024 Rodríguez-Enríquez et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.)

Published
2024
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47. Diving into cancer OXPHOS - The application of metabolic control analysis to cell and tissue research.

Author

Puurand M, Tepp K, and Kaambre T

Abstract

Knowing how the oxidative phosphorylation (OXPHOS) system in cancer cells operates differently from that of normal cells would help find compounds that specifically paralyze the energy metabolism of cancer cells. The first experiments in the study of mitochondrial respiration using the metabolic control analysis (MCA) method were done with isolated liver mitochondria in the early 80s of the last century. Subsequent studies have shown that the regulation of mitochondrial respiration by ADP in isolated mitochondria differs significantly from a model of mitochondria in situ, where the contacts with components in the cytoplasm are largely preserved. The method of selective permeabilization of the outer membrane of the cells allows the application of MCA to evaluate the contribution of different components of the OXPHOS system to its functioning while mitochondria are in a natural state. In this review, we summarize the use of MCA to study OXPHOS in cancer using permeabilized cells and tissues. In addition, we give examples of how this data fits into cancer research with a completely different approach and methodology., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023 Elsevier B.V. All rights reserved.)

Published
2023
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48. Colorectal polyps increase the glycolytic activity.

Author

Rebane-Klemm E, Reinsalu L, Puurand M, Shevchuk I, Bogovskaja J, Suurmaa K, Valvere V, Moreno-Sanchez R, and Kaambre T

Abstract

In colorectal cancer (CRC) energy metabolism research, the precancerous stage of polyp has remained rather unexplored. By now, it has been shown that CRC has not fully obtained the glycolytic phenotype proposed by O. Warburg and rather depends on mitochondrial respiration. However, the pattern of metabolic adaptations during tumorigenesis is still unknown. Understanding the interplay between genetic and metabolic changes that initiate tumor development could provide biomarkers for diagnosing cancer early and targets for new cancer therapeutics. We used human CRC and polyp tissue material and performed high-resolution respirometry and qRT-PCR to detect changes on molecular and functional level with the goal of generally describing metabolic reprogramming during CRC development. Colon polyps were found to have a more glycolytic bioenergetic phenotype than tumors and normal tissues. This was supported by a greater GLUT1 , HK , LDHA , and MCT expression. Despite the increased glycolytic activity, cells in polyps were still able to maintain a highly functional OXPHOS system. The mechanisms of OXPHOS regulation and the preferred substrates are currently unclear and would require further investigation. During polyp formation, intracellular energy transfer pathways become rearranged mainly by increasing the expression of mitochondrial adenylate kinase ( AK ) and creatine kinase ( CK ) isoforms. Decreased glycolysis and maintenance of OXPHOS activity, together with the downregulation of the CK system and the most common AK isoforms ( AK1 and AK2 ), seem to play a relevant role in CRC development., Competing Interests: The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest., (Copyright © 2023 Rebane-Klemm, Reinsalu, Puurand, Shevchuk, Bogovskaja, Suurmaa, Valvere, Moreno-Sanchez and Kaambre.)

Published
2023
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50. Stable Isotope Tracing Uncovers Reduced γ/β-ATP Turnover and Metabolic Flux Through Mitochondrial-Linked Phosphotransfer Circuits in Aggressive Breast Cancer Cells.

Author

Klepinin A, Miller S, Reile I, Puurand M, Rebane-Klemm E, Klepinina L, Vija H, Zhang S, Terzic A, Dzeja P, and Kaambre T

Abstract

Changes in dynamics of ATP γ- and β-phosphoryl turnover and metabolic flux through phosphotransfer pathways in cancer cells are still unknown. Using 18 O phosphometabolite tagging technology, we have discovered phosphotransfer dynamics in three breast cancer cell lines: MCF7 (non-aggressive), MDA-MB-231 (aggressive), and MCF10A (control). Contrary to high intracellular ATP levels, the 18 O labeling method revealed a decreased γ- and β-ATP turnover in both breast cancer cells, compared to control. Lower β-ATP[ 18 O] turnover indicates decreased adenylate kinase (AK) flux. Aggressive cancer cells had also reduced fluxes through hexokinase (HK) G-6-P[ 18 O], creatine kinase (CK) [CrP[ 18 O], and mitochondrial G-3-P[ 18 O] substrate shuttle. Decreased CK metabolic flux was linked to the downregulation of mitochondrial MTCK1A in breast cancer cells. Despite the decreased overall phosphoryl flux, overexpression of HK2, AK2, and AK6 isoforms within cell compartments could promote aggressive breast cancer growth., Competing Interests: The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest., (Copyright © 2022 Klepinin, Miller, Reile, Puurand, Rebane-Klemm, Klepinina, Vija, Zhang, Terzic, Dzeja and Kaambre.)

Published
2022
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