Search

Your search keyword '"Trivigno, C."' showing total 9 results
Start Over Author "Trivigno, C."
9 results on '"Trivigno, C."'

1. 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

2. 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
View/download PDF

3. 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

4. Dark chocolate's impact on low-grade endotoxemia in metabolic dysfunction-associated steatohepatitis.

Author

Pannunzio A, Baratta F, Maggio E, Palumbo IM, Magna A, Trivigno C, Carnevale R, Simona B, Cammisotto V, Vidili G, Pignatelli P, Ben MD, Violi F, and Loffredo L

Subjects
Humans, Male, Female, Middle Aged, Adult, Cholera Toxin blood, Fatty Liver blood, Fatty Liver etiology, Prebiotics, Cacao, Endotoxemia blood, Cross-Over Studies, Chocolate, Haptoglobins metabolism, Lipopolysaccharides blood, Protein Precursors blood
Abstract

Background and Aims: Cocoa may have prebiotic effects and improve gut barrier function. However, it remains unclear whether dark chocolate can reduce lipopolysaccharide (LPS) levels in patients with metabolic dysfunction-associated steatohepatitis (MASH). This study aims to evaluate the effect of dark chocolate compared to milk chocolate on endotoxemia in patients with MASH., Methods and Results: Nineteen patients with MASH were randomly assigned in a crossover design to consume either 40 g/d of dark chocolate (>85% cocoa) or 40 g/d of milk chocolate (<35% cocoa) for 2 weeks to evaluate circulating levels of LPS and zonulin. A significant difference between treatments was observed in LPS (P = 0.04) and zonulin (P = 0.02) levels based on the ANOVA conducted on the crossover study data. Pairwise comparisons revealed that, compared to baseline, after 14 days of dark chocolate consumption, LPS levels decreased from 22 ± 4 to 19 ± 4 pg/dL (-15%), and zonulin levels decreased from 3.2 ± 0.9 to 2.5 ± 0.8 pg/mL (-20%). Linear correlation analysis indicated that the change (Δ) in LPS values before and after chocolate intake correlated with the change (Δ) in zonulin levels (R = 0.340, P = 0.03)., Conclusions: This study demonstrates that dark chocolate reduces circulating levels of LPS and zonulin in patients with MASH., 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 article., (Copyright © 2024 Elsevier Inc. All rights reserved.)

Published
2025
Full Text
View/download PDF

5. Choroidal and Retinal Imaging Biomarkers in Different Types of Macular Neovascularization.

Author

Toto L, Ruggeri ML, Evangelista F, Trivigno C, D'Aloisio R, De Nicola C, Viggiano P, Doronzo E, Di Nicola M, Porreca A, and Mastropasqua R

Abstract

Background: The aim of this study was to investigate optical coherence tomography (OCT) and OCT angiography (OCTA) parameters in patients with neovascular age-related macular degeneration (nAMD) and macular neovascularization (MNV) type 1, type 2, and type 3., Methods: In this retrospective study, 105 treatment-naïve eyes of 105 patients (60 men and 45 women) with a definite diagnosis of active nAMD and MNV of different types and 105 frequency-matched age and gender healthy subjects were evaluated (61 men and 44 women). All subjects underwent a full ophthalmic examination and multimodal imaging assessment, including spectral domain (SD) OCT and OCTA. The main outcome measures were choroidal vascularity index (CVI), subfoveal choroidal thickness (SFCT), central macular thickness (CMT), and outer retina to choriocapillaris (ORCC) MNV flow area (ORCCFA)., Results: Significant differences were found in terms of CVI, CMT, and ORCCFA between MNV 1 and the two other groups. CVI was significantly different between MNV 1 and healthy control patients ( p < 0.001) and between MNV 1 and MNV 2 ( p < 0.001). ORCCFA and CMT were significantly different between MNV1 and MNV2 ( p < 0.005). The difference in subfoveal CT between the three groups was not statistically significant ( p = 0.458). A significant negative correlation was found between CVI and ORCCFA. Furthermore, CVI showed a positive correlation with subfoveal CT.

Published
2023
Full Text
View/download PDF

6. Brolucizumab Intravitreal Injection in Macular Neovascularization Type 1: VA, SD-OCT, and OCTA Parameter Changes during a 16-Week Follow-Up.

Author

Toto L, Ruggeri ML, D'Aloisio R, De Nicola C, Trivigno C, Cerino L, Di Marzio G, Di Nicola M, Porreca A, and Mastropasqua R

Subjects
Humans, Angiogenesis Inhibitors therapeutic use, Follow-Up Studies, Tomography, Optical Coherence, Intravitreal Injections, Prospective Studies, Macular Degeneration drug therapy, Choroidal Neovascularization diagnosis, Choroidal Neovascularization drug therapy, Retinal Detachment
Abstract

Introduction: The aim of this study was to assess early anatomical and functional changes after brolucizumab intravitreal injection (BIVI) in patients with age-related macular degeneration (AMD) and macular neovascularization type 1 (MNV1)., Methods: A total of 24 eyes of 24 patients suffering from naïve AMD with MNV1 candidates to BIVI as per label with q12/q8 dosing regimen after the loading dose were enrolled in this prospective study. Main outcome measures during a 16-week follow-up period included changes in best corrected visual acuity (BCVA), central macular thickness (CMT), subfoveal subretinal fluid (SSRF) thickness (SSRFT), subfoveal sub-retinal pigment epithelium (RPE) fluid thickness (SSRPEFT), subfoveal choroidal thickness (SFCT), and pigment epithelial detachment (PED) maximum height (PED-MH). In addition, MNV1 flow area; percentages of eyes with intraretinal fluid (IRF), subretinal fluid, and sub-RPE fluid at different time points; and percentages of eyes candidates to a q8 or q12 injection interval after disease activity assessment at week 16 were evaluated., Results: BCVA improved significantly from baseline (T0) to week 12 (T3) (p = 0.028). CMT showed a significant reduction from 456 ± 123 µm at T0 to 265 ± 85 µm at T3 (p < 0.001). SSRFT and SSRPEFT reduced significantly as well (p < 0.001 and p = 0.049, respectively). PED-MH and SFCT reduced significantly at the different time points (p = 0.020; p = 0.006, respectively). IRF presence changed significantly from 41.7% of eyes at T0 to 20.8% at T3 (p = 0.045). SSRF reduced significantly during follow-up, being present in 62.5% of eyes at T0 and 4.2% of eyes at T3 (p < 0.001). Subfoveal sub-RPE fluid decreased significantly during time, being present in 20.8% of eyes at T0 and 0% at T3 (p = 0.013). Most of the eyes (18 eyes, 75%) at week 16 after disease activity assessment were shifted in the q12 interval, and only a minority of eyes shifted in a q8 interval (6 eyes, 25%)., Conclusion: Brolucizumab is efficient in AMD patients with MNV1 by reducing all retinal fluids during the loading phase and shows reduction of macular thickness, choroidal thickness, and PED height. Most eyes at disease activity assessment (75%) fall into 12-week interval and the minority (25%) into the 8-week interval., (© 2022 The Author(s). Published by S. Karger AG, Basel.)

Published
2023
Full Text
View/download PDF

7. Halofuginone-induced amino acid starvation regulates Stat3-dependent Th17 effector function and reduces established autoimmune inflammation.

Author

Carlson TJ, Pellerin A, Djuretic IM, Trivigno C, Koralov SB, Rao A, and Sundrud MS

Subjects
Animals, Encephalomyelitis, Autoimmune, Experimental genetics, Encephalomyelitis, Autoimmune, Experimental pathology, Inflammation chemically induced, Inflammation genetics, Inflammation immunology, Inflammation pathology, Interleukin-23 genetics, Interleukin-23 immunology, Mice, Mice, Inbred BALB C, Mice, Knockout, Phosphorylation genetics, Phosphorylation immunology, Piperidines, Quinazolinones, Receptors, CCR6 genetics, Receptors, CCR6 immunology, Receptors, Interleukin genetics, Receptors, Interleukin immunology, STAT3 Transcription Factor genetics, STAT3 Transcription Factor metabolism, Th17 Cells pathology, Amino Acids deficiency, Encephalomyelitis, Autoimmune, Experimental immunology, Lymphocyte Activation, STAT3 Transcription Factor immunology, Th17 Cells immunology
Abstract

The IL-23 pathway is genetically linked to autoimmune disease in humans and is required for pathogenic Th17 cell function in mice. However, because IL-23R-expressing mature Th17 cells are rare and poorly defined in mice at steady-state, little is known about IL-23 signaling. In this study, we show that the endogenous CCR6(+) memory T cell compartment present in peripheral lymphoid organs of unmanipulated mice expresses Il23r ex vivo, displays marked proinflammatory responses to IL-23 stimulation in vitro, and is capable of transferring experimental autoimmune encephalomyelitis. The prolyl-tRNA synthetase inhibitor halofuginone blocks IL-23-induced Stat3 phosphorylation and IL-23-dependent proinflammatory cytokine expression in endogenous CCR6(+) Th17 cells via activation of the amino acid starvation response (AAR) pathway. In vivo, halofuginone shows therapeutic efficacy in experimental autoimmune encephalomyelitis, reducing both established disease progression and local Th17 cell effector function within the CNS. Mechanistically, AAR activation impairs Stat3 responses downstream of multiple cytokine receptors via selective, posttranscriptional suppression of Stat3 protein levels. Thus, our study reveals latent pathogenic functions of endogenous Th17 cells that are regulated by both IL-23 and AAR pathways and identifies a novel regulatory pathway targeting Stat3 that may underlie selective immune regulation by the AAR.

Published
2014
Full Text
View/download PDF

8. Identity crisis of Th17 cells: many forms, many functions, many questions.

Author

Sundrud MS and Trivigno C

Subjects
Animals, Humans, Phenotype, T-Lymphocyte Subsets immunology, T-Lymphocyte Subsets metabolism, Th17 Cells immunology, Th17 Cells metabolism
Abstract

Th17 cells are a subset of CD4(+) effector T cells characterized by expression of the IL-17-family cytokines, IL-17A and IL-17F. Since their discovery nearly a decade ago, Th17 cells have been implicated in the regulation of dozens of immune-mediated inflammatory diseases and cancer. However, attempts to clarify the development and function of Th17 cells in human health and disease have generated as many questions as answers. On one hand, cytokine expression in Th17 cells appears to be remarkably dynamic and is subject to extensive regulation (both positive and negative) in tissue microenvironments. On the other hand, accumulating evidence suggests that the human Th17 subset is a heterogeneous population composed of several distinct pro- and anti-inflammatory subsets. Clearly, Th17 cells as originally conceived no longer neatly fit the long-standing paradigm of stable and irrepressible effector T cell function. Here we review current concepts surrounding human Th17 cells, with an emphasis on their plasticity, heterogeneity, and their many, tissue-specific functions. In spite of the challenges ahead, a comprehensive understanding of Th17 cells and their relationship to human disease is key to ongoing efforts to develop safer and more selective anti-inflammatory medicines., (Copyright © 2013 Elsevier Ltd. All rights reserved.)

Published
2013
Full Text
View/download PDF

9. The Drosophila mitochondrial translation elongation factor G1 contains a nuclear localization signal and inhibits growth and DPP signaling.

Author

Trivigno C and Haerry TE

Subjects
Amino Acid Sequence, Animals, Animals, Genetically Modified, Down-Regulation genetics, Drosophila growth & development, Drosophila metabolism, Drosophila Proteins genetics, Embryo, Nonmammalian, Female, Gene Expression Regulation, Developmental, Genes, Lethal, Humans, Male, Mitochondrial Proteins chemistry, Mitochondrial Proteins genetics, Mitochondrial Proteins metabolism, Mitochondrial Proteins physiology, Molecular Sequence Data, Peptide Elongation Factor G metabolism, Peptide Elongation Factors genetics, Peptide Elongation Factors metabolism, Sequence Homology, Amino Acid, Signal Transduction genetics, Drosophila embryology, Drosophila genetics, Drosophila Proteins chemistry, Drosophila Proteins metabolism, Drosophila Proteins physiology, Nuclear Localization Signals chemistry, Nuclear Localization Signals genetics, Nuclear Localization Signals physiology, Peptide Elongation Factor G chemistry, Peptide Elongation Factor G genetics, Peptide Elongation Factor G physiology, Peptide Elongation Factors chemistry, Peptide Elongation Factors physiology
Abstract

Mutations in the human mitochondrial elongation factor G1 (EF-G1) are recessive lethal and cause death shortly after birth. We have isolated mutations in iconoclast (ico), which encodes the highly conserved Drosophila orthologue of EF-G1. We find that EF-G1 is essential during fly development, but its function is not required in every tissue. In contrast to null mutations, missense mutations exhibit stronger, possibly neomorphic phenotypes that lead to premature death during embryogenesis. Our experiments show that EF-G1 contains a secondary C-terminal nuclear localization signal. Expression of missense mutant forms of EF-G1 can accumulate in the nucleus and cause growth and patterning defects and animal lethality. We find that transgenes that encode mutant human EF-G1 proteins can rescue ico mutants, indicating that the underlying problem of the human disease is not just the loss of enzymatic activity. Our results are consistent with a model where EF-G1 acts as a retrograde signal from mitochondria to the nucleus to slow down cell proliferation if mitochondrial energy output is low.

Published
2011
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results