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1. Age‐related decline in murine heart and skeletal muscle performance is attenuated by reduced Ahnak1 expression

Author

Mahmoodzadeh, S., Koch, K., Schriever, C., Xu, J., Steinecker, M., Leber, J., Dworatzek, E., Purfürst, B., Kunz, S., Recchia, D., Canepari, M., Heuser, A., Di Francescantonio, S., and Morano, I.

Subjects
Male, Mice, Knockout, Age‐related mitochondrial dysfunction, Ahnak1, QM1-695, Skeletal muscle, Heart, Original Articles, Diseases of the musculoskeletal system, Mitochondrial Dynamics, Mitochondria, Physical performance, Mice, RC925-935, Cardiovascular and Metabolic Diseases, Human anatomy, Animals, Original Article, Female, Technology Platforms, Function and Dysfunction of the Nervous System, Muscle, Skeletal, Muscle Contraction
Abstract

Background Aging is associated with a progressive reduction in cellular function leading to poor health and loss of physical performance. Mitochondrial dysfunction is one of the hallmarks of aging; hence, interventions targeting mitochondrial dysfunction have the potential to provide preventive and therapeutic benefits to elderly individuals. Meta‐analyses of age‐related gene expression profiles showed that the expression of Ahnak1, a protein regulating several signal‐transduction pathways including metabolic homeostasis, is increased with age, which is associated with low VO2MAX and poor muscle fitness. However, the role of Ahnak1 in the aging process remained unknown. Here, we investigated the age‐related role of Ahnak1 in murine exercise capacity, mitochondrial function, and contractile function of cardiac and skeletal muscles. Methods We employed 15‐ to 16‐month‐old female and male Ahnak1‐knockout (Ahnak1‐KO) and wild‐type (WT) mice and performed morphometric, biochemical, and bioenergetics assays to evaluate the effects of Ahnak1 on exercise capacity and mitochondrial morphology and function in cardiomyocytes and tibialis anterior (TA) muscle. A human left ventricular (LV) cardiomyocyte cell line (AC16) was used to investigate the direct role of Ahnak1 in cardiomyocytes. Results We found that the level of Ahnak1 protein is significantly up‐regulated with age in the murine LV (1.9‐fold) and TA (1.8‐fold) tissues. The suppression of Ahnak1 was associated with improved exercise tolerance, as all aged adult Ahnak1‐KO mice (100%) successfully completed the running programme, whereas approximately 31% male and 8% female WT mice could maintain the required running speed and distance. Transmission electron microscopic studies showed that LV and TA tissue specimens of aged adult Ahnak1‐KO of both sexes have significantly more enlarged/elongated mitochondria and less small mitochondria compared with WT littermates (P

Published
2021

6. Rebalancing expression of HMGB1 redox isoforms to counteract muscular dystrophy

Author

Careccia, G, Saclier, M, Tirone, M, Ruggieri, E, Principi, E, Raffaghello, L, Torchio, S, Recchia, D, Canepari, M, Gorzanelli, A, Ferrara, M, Castellani, P, Rubartelli, A, Rovere-Querini, P, Casalgrandi, M, Preti, A, Lorenzetti, I, Bruno, C, Bottinelli, R, Brunelli, S, Previtali, S, Bianchi, M, Messina, G, Vénéreau, E, Careccia, Giorgia, Saclier, Marielle, Tirone, Mario, Ruggieri, Elena, Principi, Elisa, Raffaghello, Lizzia, Torchio, Silvia, Recchia, Deborah, Canepari, Monica, Gorzanelli, Andrea, Ferrara, Michele, Castellani, Patrizia, Rubartelli, Anna, Rovere-Querini, Patrizia, Casalgrandi, Maura, Preti, Alessandro, Lorenzetti, Isabella, Bruno, Claudio, Bottinelli, Roberto, Brunelli, Silvia, Previtali, Stefano Carlo, Bianchi, Marco Emilio, Messina, Graziella, Vénéreau, Emilie, Careccia, G, Saclier, M, Tirone, M, Ruggieri, E, Principi, E, Raffaghello, L, Torchio, S, Recchia, D, Canepari, M, Gorzanelli, A, Ferrara, M, Castellani, P, Rubartelli, A, Rovere-Querini, P, Casalgrandi, M, Preti, A, Lorenzetti, I, Bruno, C, Bottinelli, R, Brunelli, S, Previtali, S, Bianchi, M, Messina, G, Vénéreau, E, Careccia, Giorgia, Saclier, Marielle, Tirone, Mario, Ruggieri, Elena, Principi, Elisa, Raffaghello, Lizzia, Torchio, Silvia, Recchia, Deborah, Canepari, Monica, Gorzanelli, Andrea, Ferrara, Michele, Castellani, Patrizia, Rubartelli, Anna, Rovere-Querini, Patrizia, Casalgrandi, Maura, Preti, Alessandro, Lorenzetti, Isabella, Bruno, Claudio, Bottinelli, Roberto, Brunelli, Silvia, Previtali, Stefano Carlo, Bianchi, Marco Emilio, Messina, Graziella, and Vénéreau, Emilie

Abstract

Muscular dystrophies (MDs) are a group of genetic diseases characterized by progressive muscle wasting associated to oxidative stress and persistent inflammation. It is essential to deepen our knowledge on the mechanism connecting these two processes because current treatments for MDs have limited efficacy and/or are associated with side effects. Here, we identified the alarmin high-mobility group box 1 (HMGB1) as a functional link between oxidative stress and inflammation in MDs. The oxidation of HMGB1 cysteines switches its extracellular activities from the orchestration of tissue regeneration to the exacerbation of inflammation. Extracellular HMGB1 is present at high amount and undergoes oxidation in patients with MDs and in mouse models of Duchenne muscular dystrophy (DMD) and limb-girdle muscular dystrophy 3 (LGMDR3) compared to controls. Genetic ablation of HMGB1 in muscles of DMD mice leads to an amelioration of the dystrophic phenotype as evidenced by the reduced inflammation and muscle degeneration, indicating that HMGB1 oxidation is a detrimental process in MDs. Pharmacological treatment with an engineered nonoxidizable variant of HMGB1, called 3S, improves functional performance, muscle regeneration, and satellite cell engraftment in dystrophic mice while reducing inflammation and fibrosis. Overall, our data demonstrate that the balance between HMGB1 redox isoforms dictates whether skeletal muscle is in an inflamed or regenerating state, and that the nonoxidizable form of HMGB1 is a possible therapeutic approach to counteract the progression of the dystrophic phenotype. Rebalancing the HMGB1 redox isoforms may also be a therapeutic strategy for other disorders characterized by chronic oxidative stress and inflammation.

Published
2021

15. Abstract

Author

Andries, L. J., Sys, S. U., Meulemans, A. L., Schuurkes, J. A. J., Vanheel, B., Van de Voorde, J., De Smet, P., Li, J., Van Driessche, W., Flamion, B., Foulon, S., Abramow, M., Calders, P., Eechaute, W., Lacroix, E., Weyne, I., Hoeben, D., Burvenich, C., Fransen, P., Andries, L. J., Van Bedaf, D., Demolder, M., Sys, S. U., Ouedraogo, R., Lebrun, P., Herchuelz, A., Antoine, M. -H., Vandenput, S., Votion, D., Anciaux, N., Duvivier, D. H., Art, T., Lekeux, P., Votion, D., Ghafir, Y., Vandenput, S., Art, T., Lekeux, P., Geurts, M., Hermans, E., Maloteaux, J. -M., Perrad, B., Noel, B., Lagache, F., Bister, J. L., Paquay, R., Bister, J. L., Derycke, G., Vandermeir, M. A., Paquay, R., de Brouwer, S., Porret, C. -A., Stergiopulos, N., Meister, J. -J., Verbeke, M., Van de Voorde, J., Lameire, N., De Clerck, N. M., De Schuytter, J., Tytgato, J., Buyse, G., Eggermont, J., Droogmans, G., Nilius, B., Daenens, P., Salomone, S., Feron, O., Dessy, C., Morel, N., Godfraind, T., Aloisi, A. M., Sacerdote, P., Lodi, L., Carli, G., Carobi, C., Garinei, G., Miniaci, U. C., Scotto, P., Sabatino, M., Sardo, P., Iurato, L., La Grutta, V., Bagni, M. A., Cecchi, G., Cecchini, E., Colomo, F., Garzella, P., Bottinelli, R., Harridge, S. D. H., Canepari, M., Reggiani, C., Reggiani, Saltin, Bambagioni, D., Fanò, G., Menchetti, G,, Danieli-Betto, P., Esposito, A., Betto, R., Megighian, A., Midrio, M., Betto, D. Danieli, Esposito, A., Megighian, A., Midrio, M., Orizio, C., Liberati, D., Locatelli, C., De Grandis, D., Veicsteinas, A., Angoli, D., Delia, D., Wanke, E., Bramucci, M., Miano, A., Quassinti, L., Maccari, E., Murri, O., Amici, D., Cibelli, G., Jüngling, S., Schoch, S., Gerdest, H. H., Thiel, G., Demori, I., Bottazzi, C., Voci, A., Fugassa, E., Barreca, A., Minuto, F., Gallo, G., Fulle, S., Belia, S., Menchetti, G., Cacchio, M., Fanò, G., Gastaldi, G., Laforenza, U., Ferrari, G., Rindi, G., Doni, M. G., Padoin, E., Residori, O., Cesaro, M., Toma, L., Rubini, A., Mutinelli, F, Paulesu, L., Romagnolie, R., Cintorino, M., Pippia, P., Meloni, M. A., Sciola, L., Spano, A., Cogoli-Greuter, M., Cogoli, A., Sardini, A., Mintenig, G. M., Valverde, M. A., Sepùlveda, F. V., Gill, D. R., Hyde, S. C., Higgins, C. F., McNaughton, P. A., Spena, A., Arcuri, M. T., Bonofiglio, S., Chimenti, R., Covello, C., De Cicco, T., Mazzulla, S., Martino, G., Tottene, A., Moretti, A., Pietrobon, D., Baccari, M. C., Calamai, F., Staderini, G., Cova, E., Marelli, R., Sommi, P., Ventura, U., Lombardi, A. M., Fabris, R., Pagano, C., Federspil, G., Vettor, R., Mancinelli, R., Tonali, P., Servidei, S., Romani, R., Tringali, A., Azzena, G. B., Mulè, F., Serio, R., Postorino, A., Pagano, C., Rizzato, M., Granzotto, M., Lombardi, A. M., Fabris, R., Vettor, R., Federspil, G., Sommi, P., Ricci, V., Romano, M., Ivey, K. J., Ventura, U., Vacca, G., Papillo, B., Mary, D. A. S. G., Battaglia, A., Grossini, E., Vacca, G., Papillo, B., Battaglia, A., Grossini, E., Accili, E. A., Redaelli, G., DiFrancesco, D., Antoniotti, S., Distasi, C., Lovisolo, D., Munaron, L., Bertaso, F., Assandri, R., Mazzanti, M., Bianchi, L., Arcangeli, A., Faravelli, L., Becchetti, A., Coronello, M., Mini, E., Francini, F., Olivotto, M., Wanke, E., Bigiani, A., Kim, D. -J., Roper, S. D., Carabelli, V., Lovallo, M., Magnelli, V., Zucker, H., Carbone, E., D’Angelo, E., Rossi, P., De Filippi, G., Taglietti, V., Faravelli, L., Bianchi, L., Arcangeli, A., Francini, F., Olivotto, M., Wanke, E., Francini, F., Bencini, C., Squecco, R., Guatteo, E., Bacci, A., Franceschetti, S., Avanzini, G., Wanke, E., Magnelli, V., Carbone, E., Mazzanti, M., Assandri, R., Ferroni, A., DiFrancesco, D., Navangione, A., Vellani, V., Rispoli, G., Peres, A., Centinaio, E., Giovannardi, S., Russo, G., Marcotti, W., Prigioni, I., Trequattrini, C., Harper, A. A., Petris, A., Franciolini, F., Zaza, A., Micheletti, M., Brioschi, A., Antonutto, G., Capelli, C., Girardis, M., Zamparo, P., di Prampero, P. E., Antonutto, G., Girardis, M., Tuniz, D., di Prampero, P. E., Filippi, G. M., Troiani, D., Grassi, B., Poole, D. C., Richardson, R. S., Knight, D. R., Erickson, B. K., Wagner, P. D., Aimi, B., Stilli, D., Gallo, P., Sgoifo, A., Lagrasta, C., Olivetti, G., Reali, N., Casti, A., Musso, E., Alloatti, G., Penna, C., Gallo, M. P., Levi, R. C., Fenoglio, I., Appendino, G., Gallo, P., Sgoifo, A., Medici, D., Aimi, B., Manghi, M., Stilli, D., Musso, E., Sgoifo, A., Pasini, E., Gallo, P., Aimi, B., Stilli, D., Ceconi, C., Musso, E., Baldissera, F., Cavallari, P., Locatelli, M., Bartesaghi, R., Gessi, T., Benfenati, F., Valtorta, F., Onofri, F., Poo, M., Greengard, P., Biagini, G., Sala, D., Viani§, P., Kozlov, A. V., Zini, I., Bravin, M., Tempia, F., Strata, P., Brescia, G., Di Benedetto, C., Corsi, P., Cangiano, G., Buttiglione, M., Ambrosini, M., Gennarini, G., Casadio, A., Levi, R. C., Montarolo, P. G., Cesare, P., Stoughton, R., McNaughton, P. A., D’Arcangelo, G., Dodt, H. U., Brancati, A., Zieglgänsberger, W., Errico, P., Ferraresi, A., Barmack, N. H., Pettorossi, V. E., Gasparini, S., D’Ambrosio, R., Janigro, D., DiFrancesco, D., Gritti, I., Marintti, M., Calcaterra, R., Freddi, R., Mancia, M., Imeri, I., Bianchi, S., Mancia, M., Lui, F., Gregory, K. M., Blanks, R. H. I., Giolli, R. A., Benassi, C., Corazza, R., Magherini, P. C., Bardoni, R., Belluzzi, O., Mancinelli, R., Manni, E., Azzena, G. B., Tringali, A., Romani, R., Diana, M., Fratta, W., Manzoni, D., Andre, P., Pompeiano, O., Mazzocchio, R., Rossi, A., Melis, F., Kitura, A., Caria, M. A., Asanuma, H., Melone, M, De Biasi, S, Minelli, A, Conti, F, Minelli, A, Karschin, C, DeBiasi, S, Brecha, N C, Conti, F, Monda, M., Amaro, S., Sullo, A., De Luca, B., Monda, M., Amaro, S., Sullo, A., De Luca, B., Pantò, M. R., Cicirata, F., Parenti, R., Serapide, M. F., Parenti, R., Wassef, M., Cicirata, F., Podda, M. V., Solinas, A., Chessa, G., Deriu, F., Mameli, O., Tolu, E., Pompeiano, O., Andre, P., Manzoni, D., Porro, C. A., Francescato, M. P., Cettolo, V., Diamond, M. E., Baraldi, P., Bazzocchi, M., Rivosecchi, R., Konnerth, A., Rossi, M. L., Martini, M., Pelucchi, B., Fesce, R., Santarelli, L., Schacher, S., Montarolo, P. G., Santarelli, R., Grassi, C., Valente, A., Nisticò, S., Bagetta, G., Azzena, G. B., Scuri, Rossana, Garcia-Gil, Mercedes, Mozzachiodi, Riccardo, Brunelli, Marcello, Stefani, G., Onofri, F., Vaccaro, P., Nielander, H. B., Benfenati, F., Tancredi, V., D’Antuono, M., Siniscalchi, A., Brancati, A., Avoli, M., Vellani, V., Navangione, A., Rispoli, G., Verzè, L., Buffo, A., Rossi, F., Oestreicher, A. B., Gispen, W. H., Strata, P., Zamboni, G., Amici, R., Jones, C. A., Perez, E., Domeniconi, R., Parmeggiani, P. L., Zoli, Michele, Le Novàre, Nicolas, Changeux, Jean -Pierre, Lafortuna, C. L., Reinach, E., Saibene, F., Scotto, P., Zocchi, L., Agostoni, E., and Cremaschi, D.

Published
1996
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17. Maximum speed of shortening and ATPase activity in atrial and ventricular myocardia of hyperthyroid rats

Author

Bottinelli, R., Canepari, M., Cappelli, V., and Reggiani, C.

Subjects
Hyperthyroidism -- Research, Adenosine triphosphatase -- Physiological aspects, Heart muscle -- Observations, Biological sciences
Abstract

The atrial and ventricular myocardia in hyperthyroid rats demonstrate identical functioning of myofibrillar adenosine triphosphatase at conditions of high and low ionic strengths. This result was predicted for the two myocardia when myosin heavy chain isoforms are involved. The shortening is faster in atrial myocardium than in ventricular myocardium because of tissue-specific isoforms of myosin light chains.

Published
1995

20. High mobility group box 1 orchestrates tissue regeneration via CXCR4

Author

Tirone, M, Tran, N, Ceriotti, C, Gorzanelli, A, Canepari, M, Bottinelli, R, Raucci, A, Di Maggio, S, Santiago, C, Mellado, M, Saclier, M, François, S, Careccia, G, He, M, De Marchis, F, Conti, V, Ben Larbi, S, Cuvellier, S, Casalgrandi, M, Preti, A, Chazaud, B, Al-Abed, Y, Messina, G, Sitia, G, Brunelli, S, Bianchi, M, Vénéreau, E, Tirone, Mario, Tran, Ngoc Lan, Ceriotti, Chiara, Gorzanelli, Andrea, Canepari, Monica, Bottinelli, Roberto, Raucci, Angela, Di Maggio, Stefania, Santiago, César, Mellado, Mario, Saclier, Marielle, François, Stéphanie, Careccia, Giorgia, He, Mingzhu, De Marchis, Francesco, Conti, Valentina, Ben Larbi, Sabrina, Cuvellier, Sylvain, CASALGRANDI, MAURA, Preti, Alessandro, Chazaud, Bénédicte, Al-Abed, Yousef, Messina, Graziella, Sitia, Giovanni, Brunelli, Silvia, Bianchi, Marco Emilio, Vénéreau, Emilie, Tirone, M, Tran, N, Ceriotti, C, Gorzanelli, A, Canepari, M, Bottinelli, R, Raucci, A, Di Maggio, S, Santiago, C, Mellado, M, Saclier, M, François, S, Careccia, G, He, M, De Marchis, F, Conti, V, Ben Larbi, S, Cuvellier, S, Casalgrandi, M, Preti, A, Chazaud, B, Al-Abed, Y, Messina, G, Sitia, G, Brunelli, S, Bianchi, M, Vénéreau, E, Tirone, Mario, Tran, Ngoc Lan, Ceriotti, Chiara, Gorzanelli, Andrea, Canepari, Monica, Bottinelli, Roberto, Raucci, Angela, Di Maggio, Stefania, Santiago, César, Mellado, Mario, Saclier, Marielle, François, Stéphanie, Careccia, Giorgia, He, Mingzhu, De Marchis, Francesco, Conti, Valentina, Ben Larbi, Sabrina, Cuvellier, Sylvain, CASALGRANDI, MAURA, Preti, Alessandro, Chazaud, Bénédicte, Al-Abed, Yousef, Messina, Graziella, Sitia, Giovanni, Brunelli, Silvia, Bianchi, Marco Emilio, and Vénéreau, Emilie

Abstract

Inflammation and tissue regeneration follow tissue damage, but little is known about how these processes are coordinated. High Mobility Group Box 1 (HMGB1) is a nuclear protein that, when released on injury, triggers inflammation. We previously showed that HMGB1 with reduced cysteines is a chemoattractant, whereas a disulfide bond makes it a proinflammatory cytokine. Here we report that fully reduced HMGB1 orchestrates muscle and liver regeneration via CXCR4, whereas disulfide HMGB1 and its receptors TLR4/MD-2 and RAGE (receptor for advanced glycation end products) are not involved. Injection of HMGB1 accelerates tissue repair by acting on resident muscle stem cells, hepatocytes, and infiltrating cells. The nonoxidizable HMGB1 mutant 3S, in which serines replace cysteines, promotes muscle and liver regeneration more efficiently than the wildtype protein and without exacerbating inflammation by selectively interacting with CXCR4. Overall, our results show that the reduced form of HMGB1 coordinates tissue regeneration and suggest that 3S may be used to safely accelerate healing after injury in diverse clinical contexts.

Published
2018

21. Structure and function of human muscle fibres and muscle proteome in physically active older men.

Author

Brocca, L, McPhee, JS, Longa, E, Canepari, M, Seynnes, O, De Vito, G, Pellegrino, MA, Narici, M, Bottinelli, R, Brocca, L, McPhee, JS, Longa, E, Canepari, M, Seynnes, O, De Vito, G, Pellegrino, MA, Narici, M, and Bottinelli, R

Abstract

Contradictory results have been reported on the impact of ageing on structure and functions of skeletal muscle fibres likely due to complex interplay between ageing and other phenomena such as disuse and diseases. Here we recruited healthy, physically and socially active young (YO) and elderly (EL) men in order to study aging per se without the confounding effects of impaired physical function. In vivo analyses of quadriceps and in vitro analyses of vastus lateralis muscle biopsies were performed. In EL subjects, our results show that: (i) quadriceps volume, maximum voluntary torque (MVC), and patellar tendon force (Ft) were significantly lower; (ii) muscle fibres went through significant atrophy and impairment of specific force (Po/CSA) and unloaded shortening velocity (Vo); (iii) myosin/actin ratio and myosin content in individual muscle fibres were not altered; (iv) muscle proteome went through quantitative adaptations, namely an up-regulation of the content of several groups of proteins among which myofibrillar proteins and antioxidant defence systems; (v) muscle proteome went through qualitative adaptations, namely phosphorylation of several proteins, including Myosin Light Chain-2 slow and Troponin T and carbonylation of Myosin Heavy Chains. The present results indicate that impairment of individual muscle fibres structure and function is a major feature of ageing per se and that qualitative adaptations of muscle proteome are likely more involved than quantitative adaptations in determining such phenomenon. This article is protected by copyright. All rights reserved.

Published
2017

22. MITOCHONDRIA AND OXIDATIVE STRESS IN AGE-RELATED MUSCLE LOSS (SARCOPENIA)

Author

LO VERSO, Francesca, CARNIO, S, BARAIBAR, M, LONGA, M, MAFFEI, M, CANEPARI, M, FRIGUET, B, BOTTINELLI, R, and SANDRI, M

Abstract

Muscle wasting is due to an excessive activation of degradative pathways. It occurs in different pathologies such as cancer, AIDS, diabetes but inevitably it occurs in everybody’s life during aging. Sarcopenia is the degenerative loss of skeletal muscle mass and strength associated with aging. The ability to activate compensatory mechanisms in response to environmental stress and physiological changing is an important factor for survival and maintenance of cellular functions. A system that is often activated both in short and prolonged stress conditions is autophagy. Autophagy is required to clear the cell from dysfunctional organelles and altered proteins and is reported to decline during ageing. This reduction might contribute to age-related organ dysfunction and, in general, to ageing. Here we report that specific autophagy inhibition in muscle has a major impact on this tissue that ultimately affect life span of animals. Inhibition of autophagy exacerbates the aging-related features of muscle such as atrophy, mitochondrial dysfunction, oxidative stress and profound weakness. Mitochondrial dysfunction and oxidative stress directly affect acto-myosin interaction and force generation. These results demonstrate that aging-related muscle dysfunction is mainly caused by a failure of the autophagy system. It has been reported that lifestyle adaptations, such as caloric restriction and physical exercise are able to ameliorate several features during ageing process, moreover physical activity has been recently documented to play a fundamental physiological role in the regulation of autophagy in several tissues. Here we address also the role of autophagy during exercise. We reveal that autophagy is critical for the preservation of mitochondrial function during damaging muscle contraction. We establish that basal oxidative stress plays a crucial role in mitochondrial maintenance during normal physical activity. Therefore, autophagy is an adaptive response to exercise that ensures effective mitochondria-quality control during damaging physical activity., Journal of International Society of Antioxidants in Nutrition & Health, Vol 3, No 3 (2016)

Published
2016
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23. Molecular mechanism regulating myosin and cardiac functions by ELC

Author

Lossie, J., Köhncke, C., Mahmoodzadeh, S., Steffen, W., Canepari, M., Maffei, M., Taube, M., Larchevêque, O., Baumert, P., Haase, H., Bottinelli, R., Regitz-Zagrosek, V., and Morano, I.

Subjects
Cardiovascular and Metabolic Diseases, Function and Dysfunction of the Nervous System
Abstract

The essential myosin light chain (ELC) is involved in modulation of force generation of myosin motors and cardiac contraction, while its mechanism of action remains elusive. We hypothesized that ELC could modulate myosin stiffness which subsequently determines its force production and cardiac contraction. We therefore generated heterologous transgenic mouse (TgM) strains with cardiomyocyte-specific expression of ELC with human ventricular ELC (hVLC-1; TgM(hVLC-1)) or E56G-mutated hVLC-1 (hVLC-1(E56G); TgM(E56G)). hVLC-1 or hVLC-1(E56G) expression in TgM was around 39% and 41%, respectively of total VLC-1. Laser trap and in vitro motility assays showed that stiffness and actin sliding velocity of myosin with hVLC-1 prepared from TgM(hVLC-1) (1.67pN/nm and 2.3{my}m/s, respectively) were significantly higher than myosin with hVLC-1(E56G) prepared from TgM(E56G) (1.25pN/nm and 1.7{my}m/s, respectively) or myosin with mouse VLC-1 (mVLC-1) prepared from C57/BL6 (1.41 pN/nm and 1.5+-0.03 {my}m/s, respectively). Maximal left ventricular pressure development of isolated perfused hearts in vitro prepared from TgM(hVLC-1) (80.0mmHg) were significantly higher than hearts from TgM(E56G) (66.2mmHg) or C57/BL6 (59.3+-3.9 mmHg). These findings show that ELCs decreased myosin stiffness, in vitro motility, and thereby cardiac functions in the order hVLC-1 > hVLC-1(E56G) ≈ mVLC-1. They also suggest a molecular pathomechanism of cardiomyopathies caused by hVLC-1 mutations.

Published
2014

25. Skeletal muscle hypertrophy and structure and function of skeletal muscle fibres in male body builders

Author

D'Antona, G, Lanfranconi, F, Pellegrino, M, Brocca, L, Adami, R, Rossi, R, Moro, G, Miotti, D, Canepari, M, Bottinelli, R, Pellegrino, MA, Bottinelli, R., LANFRANCONI, FRANCESCA, D'Antona, G, Lanfranconi, F, Pellegrino, M, Brocca, L, Adami, R, Rossi, R, Moro, G, Miotti, D, Canepari, M, Bottinelli, R, Pellegrino, MA, Bottinelli, R., and LANFRANCONI, FRANCESCA

Abstract

Needle biopsy samples were taken from vastus lateralis muscle (VL) of five male body builders (BB, age 27.4 +/- 0.93 years; mean +/- s.e.m.), who had being performing hypertrophic heavy resistance exercise (HHRE) for at least 2 years, and from five male active, but untrained control subjects (CTRL, age 29.9 +/- 2.01 years). The following determinations were performed: anatomical cross-sectional area and volume of the quadriceps and VL muscles in vivo by magnetic resonance imaging (MRI); myosin heavy chain isoform (MHC) distribution of the whole biopsy samples by SDS-PAGE; cross-sectional area (CSA), force (P-o), specific force (P-o/CSA) and maximum shortening velocity (V-o) of a large population (n= 524) of single skinned muscle fibres classified on the basis of MHC isoform composition by SDS-PAGE; actin sliding velocity (V-f) on pure myosin isoforms by in vitro motility assays. In BB a preferential hypertrophy of fast and especially type 2X fibres was observed. The very large hypertrophy of VL in vivo could not be fully accounted for by single muscle fibre hypertrophy. CSA of VL in vivo was, in fact, 54% larger in BB than in CTRL, whereas mean fibre area was only 14% larger in BB than in CTRL. MHC isoform distribution was shifted towards 2X fibres in BB. P-o/CSA was significantly lower in type 1 fibres from BB than in type 1 fibres from CTRL whereas both type 2A and type 2X fibres were significantly stronger in BB than in CTRL. V-o of type 1 fibres and V-f of myosin 1 were significantly lower in BB than in CTRL, whereas no difference was observed among fast fibres and myosin 2A. The findings indicate that skeletal muscle of BB was markedly adapted to HHRE through extreme hypertrophy, a shift towards the stronger and more powerful fibre types and an increase in specific force of muscle fibres. Such adaptations could not be fully accounted for by well known mechanisms of muscle plasticity, i.e. by the hypertrophy of single muscle fibre (quantitative mechanism) and by

Published
2006

38. Prostatic Abscess

Author

Barozzi, L., primary, Pavlica, P., additional, Menchi, I., additional, De Matteis, M., additional, and Canepari, M., additional

Published
1998
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