24 results on '"Hulmi, J. J."'
Search Results
2. Substantial fat mass loss reduces low-grade inflammation and induces positive alteration in cardiometabolic factors in normal-weight individuals
- Author
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Sarin, H. V., Lee, J. H., Jauhiainen, M., Joensuu, A., Borodulin, K., Männistö, S., Jin, Z., Terwilliger, J. D., Isola, V., Ahtiainen, J. P., Häkkinen, K., Kristiansson, K., Hulmi, J. J., and Perola, M.
- Published
- 2019
- Full Text
- View/download PDF
3. NAD⁺ repletion with niacin counteracts cancer cachexia
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Beltrà, M. (Marc), Pöllänen, N. (Noora), Fornelli, C. (Claudia), Tonttila, K. (Kialiina), Hsu, M. Y. (Myriam Y.), Zampieri, S. (Sandra), Moletta, L. (Lucia), Corrà, S. (Samantha), Porporato, P. E. (Paolo E.), Kivelä, R. (Riikka), Viscomi, C. (Carlo), Sandri, M. (Marco), Hulmi, J. J. (Juha J.), Sartori, R. (Roberta), Pirinen, E. (Eija), Penna, F. (Fabio), Beltrà, M. (Marc), Pöllänen, N. (Noora), Fornelli, C. (Claudia), Tonttila, K. (Kialiina), Hsu, M. Y. (Myriam Y.), Zampieri, S. (Sandra), Moletta, L. (Lucia), Corrà, S. (Samantha), Porporato, P. E. (Paolo E.), Kivelä, R. (Riikka), Viscomi, C. (Carlo), Sandri, M. (Marco), Hulmi, J. J. (Juha J.), Sartori, R. (Roberta), Pirinen, E. (Eija), and Penna, F. (Fabio)
- Abstract
Cachexia is a debilitating wasting syndrome and highly prevalent comorbidity in cancer patients. It manifests especially with energy and mitochondrial metabolism aberrations that promote tissue wasting. We recently identified nicotinamide adenine dinucleotide (NAD⁺) loss to associate with muscle mitochondrial dysfunction in cancer hosts. In this study we confirm that depletion of NAD⁺ and downregulation of Nrk2, an NAD⁺ biosynthetic enzyme, are common features of severe cachexia in different mouse models. Testing NAD⁺ repletion therapy in cachectic mice reveals that NAD⁺ precursor, vitamin B3 niacin, efficiently corrects tissue NAD⁺ levels, improves mitochondrial metabolism and ameliorates cancer- and chemotherapy-induced cachexia. In a clinical setting, we show that muscle NRK2 is downregulated in cancer patients. The low expression of NRK2 correlates with metabolic abnormalities underscoring the significance of NAD⁺ in the pathophysiology of human cancer cachexia. Overall, our results propose NAD⁺ metabolism as a therapy target for cachectic cancer patients.
- Published
- 2023
4. Effect of diet composition on acid–base balance in adolescents, young adults and elderly at rest and during exercise
- Author
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Hietavala, E-M, Stout, J R, Hulmi, J J, Suominen, H, Pitkänen, H, Puurtinen, R, Selänne, H, Kainulainen, H, and Mero, A A
- Published
- 2015
- Full Text
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5. Mimicking exercise in vitro: effects of myotube contractions and mechanical stretch on omics.
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Lautaoja, J. H., Turner, D. C., Sharples, A. P., Kivelä, R., Pekkala, S., Hulmi, J. J., and Ylä-Outinen, L.
- Abstract
The number of studies using skeletal muscle (SkM) cell culture models to study exercise in vitro are rapidly expanding. Progressively, more comprehensive analysis methods, such as different omics approaches including transcriptomics, proteomics, and metabolomics have been used to examine the intra- and extracellular molecular responses to exercise mimicking stimuli in cultured myotubes. Among other techniques, exercise-like electrical pulse stimulation (EL-EPS) and mechanical stretch of SkM cells are the two most commonly used methods to mimic exercise in vitro. In this mini-review, we focus on these two approaches and their effects on the omics of myotubes and/or cell culture media. Furthermore, besides traditional two-dimensional (2-D) methods, the use of three-dimensional (3-D) SkM approaches are increasing in the field of in vitro exercise mimicry. Our aim with this mini-review is to provide the reader with an up-to-date overview of the 2-D and 3-D models and the use of omics approaches to study the molecular response to exercise in vitro. [ABSTRACT FROM AUTHOR]
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- 2023
- Full Text
- View/download PDF
6. Resistance training induced increase in muscle fiber size in young and older men
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Mero, A. A., Hulmi, J. J., Salmijärvi, H., Katajavuori, M., Haverinen, M., Holviala, J., Ridanpää, T., Häkkinen, K., Kovanen, V., Ahtiainen, J. P., and Selänne, H.
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- 2013
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7. Vitamin C and E supplementation alters protein signalling after a strength training session, but not muscle growth during 10 weeks of training
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Paulsen, G., Hamarsland, H., Cumming, K. T., Johansen, R. E., Hulmi, J. J., Børsheim, E., Wiig, H., Garthe, I., and Raastad, T.
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- 2014
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8. Exercise and milk-protein supplements: Effects on skeletal muscle sirtuins in rats with elevated risk factors for metabolic disorders: P9.8
- Author
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Kainulainen, H., Lensu, S., Pekkala, S., Mäkinen, A., Hulmi, J. J., Turpeinen, A., Kujala, U. M., Koch, L. G., and Britton, S. L.
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- 2014
9. Effect of strength training session on plasma amino acid concentration following oral ingestion of arginine or taurine in men
- Author
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Mero, A., Leikas, A., Rinkinen, N., Huhta, P., Hulmi, J. J., Pitkänen, H., and Knuutinen, J.
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- 2008
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10. Molecular signaling in muscle is affected by the specificity of resistance exercise protocol
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Hulmi, J. J., Walker, S., Ahtiainen, J. P., Nyman, K., Kraemer, W. J., and Häkkinen, K.
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- 2012
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11. Systemic blockade of ACVR2B ligands attenuates muscle wasting in ischemic heart failure without compromising cardiac function
- Author
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Szabó, Z. (Zoltán), Vainio, L. (Laura), Lin, R. (Ruizhu), Swan, J. (Julia), Hulmi, J. J. (Juha J.), Rahtu‐Korpela, L. (Lea), Serpi, R. (Raisa), Laitinen, M. (Mika), Pasternack, A. (Arja), Ritvos, O. (Olli), Kerkelä, R. (Risto), Magga, J. (Johanna), Szabó, Z. (Zoltán), Vainio, L. (Laura), Lin, R. (Ruizhu), Swan, J. (Julia), Hulmi, J. J. (Juha J.), Rahtu‐Korpela, L. (Lea), Serpi, R. (Raisa), Laitinen, M. (Mika), Pasternack, A. (Arja), Ritvos, O. (Olli), Kerkelä, R. (Risto), and Magga, J. (Johanna)
- Abstract
Signaling through activin receptors regulates skeletal muscle mass and activin receptor 2B (ACVR2B) ligands are also suggested to participate in myocardial infarction (MI) pathology in the heart. In this study, we determined the effect of systemic blockade of ACVR2B ligands on cardiac function in experimental MI, and defined its efficacy to revert muscle wasting in ischemic heart failure (HF). Mice were treated with soluble ACVR2B decoy receptor (ACVR2B‐Fc) to study its effect on post‐MI cardiac remodeling and on later HF. Cardiac function was determined with echocardiography, and myocardium analyzed with histological and biochemical methods for hypertrophy and fibrosis. Pharmacological blockade of ACVR2B ligands did not rescue the heart from ischemic injury or alleviate post‐MI remodeling and ischemic HF. Collectively, ACVR2B‐Fc did not affect cardiomyocyte hypertrophy, fibrosis, angiogenesis, nor factors associated with cardiac regeneration except modification of certain genes involved in metabolism or cell growth/survival. ACVR2B‐Fc, however, was able to reduce skeletal muscle wasting in chronic ischemic HF, accompanied by reduced LC3II as a marker of autophagy and increased mTOR signaling and Cited4 expression as markers of physiological hypertrophy in quadriceps muscle. Our results ascertain pharmacological blockade of ACVR2B ligands as a possible therapy for skeletal muscle wasting in ischemic HF. Pharmacological blockade of ACVR2B ligands preserved myofiber size in ischemic HF, but did not compromise cardiac function nor exacerbate cardiac remodeling after ischemic injury.
- Published
- 2020
12. Autophagy is induced by resistance exercise in young men, but unfolded protein response is induced regardless of age
- Author
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Hentilä, J., primary, Ahtiainen, J. P., additional, Paulsen, G., additional, Raastad, T., additional, Häkkinen, K., additional, Mero, A. A., additional, and Hulmi, J. J., additional
- Published
- 2018
- Full Text
- View/download PDF
13. Erratum to: Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition) (Autophagy, 12, 1, 1-222, 10.1080/15548627.2015.1100356
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Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Arozena, A. A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., Adhihetty, P. J., Adler, S. G., Agam, G., Agarwal, R., Aghi, M. K., Agnello, M., Agostinis, P., Aguilar, P. V., Aguirre-Ghiso, J., Airoldi, E. M., Ait-Si-Ali, S., Akematsu, T., Akporiaye, E. T., Al-Rubeai, M., Albaiceta, G. M., Albanese, C., Albani, D., Albert, M. L., Aldudo, J., Algül, H., Alirezaei, M., Alloza, I., Almasan, A., Almonte-Beceril, M., Alnemri, E. S., Alonso, C., Altan-Bonnet, N., Altieri, D. C., Alvarez, S., Alvarez-Erviti, L., Alves, S., Amadoro, G., Amano, A., Amantini, C., Ambrosio, S., Amelio, I., Amer, A. O., Amessou, M., Amon, A., An, Z., Anania, F. A., Andersen, S. U., Andley, U. P., Andreadi, C. K., Andrieu-Abadie, N., Anel, A., Ann, D. K., Anoopkumar-Dukie, S., Antonioli, M., Aoki, H., Apostolova, N., Aquila, S., Aquilano, K., Araki, K., Arama, E., Aranda, A., Araya, J., Arcaro, A., Arias, E., Arimoto, H., Ariosa, A. R., Armstrong, J. L., Arnould, T., Arsov, I., Asanuma, K., Askanas, V., Asselin, E., Atarashi, R., Atherton, S. S., Atkin, J. D., Attardi, L. D., Auberger, P., Auburger, G., Aurelian, L., Autelli, R., Avagliano, L., Avantaggiati, M. L., Avrahami, L., Azad, N., Awale, S., Bachetti, T., Backer, J. M., Bae, D. -H., Bae, J. -S., Bae, O. -N., Bae, S. H., Baehrecke, E. H., Baek, S. -H., Baghdiguian, S., Bagniewska-Zadworna, A., Bai, H., Bai, J., Bai, X. -Y., Bailly, Y., Balaji, K. N., Balduini, W., Ballabio, A., Balzan, R., Banerjee, R., Bánhegyi, G., Bao, H., Barbeau, B., Barrachina, M. D., Barreiro, E., Bartel, B., Bartolomé, A., Bassham, D. C., Bassi, M. T., Bast, R. C., J, R., Basu, A., Batista, M. T., Batoko, H., Battino, M., Bauckman, K., Baumgarner, B. L., Bayer, K. U., Beale, R., Beaulieu, J. -F., Beck, G. R., Becker, C., Beckham, J. D., Bédard, P. -A., Bednarski, P. J., Begley, T. J., Behl, C., Behrends, C., Behrens, G. M. N., Behrns, K. E., Bejarano, E., Belaid, A., Belleudi, F., Bénard, G., Berchem, G., Bergamaschi, D., Bergami, M., Berkhout, B., Berliocchi, L., Bernard, A., Bernard, M., Bernassola, F., Bertolotti, A., Bess, A. S., Besteiro, S., Bettuzzi, S., Bhalla, S., Bhattacharyya, S., Bhutia, S. K., Biagosch, C., Bianchi, M. W., Biard-Piechaczyk, M., Billes, V., Bincoletto, C., Bingol, B., Bird, S. W., Bitoun, M., Bjedov, I., Blackstone, C., Blanc, L., Blanco, G. A., Blomhoff, H. K., Boada-Romero, E., Böckler, S., Boes, M., Boesze-Battaglia, K., Boise, L. H., Bolino, A., Boman, A., Bonaldo, P., Bordi, M., Bosch, J., Botana, L. M., Botti, J., Bou, G., Bouché, M., Bouchecareilh, M., Boucher, M. -J., Boulton, M. E., Bouret, S. G., Boya, P., Boyer-Guittaut, M., Bozhkov, P. V., Brady, N., Braga, V. M. M., Brancolini, C., Braus, G. H., Bravo-San-Pedro, J. M., Brennan, L. A., Bresnick, E. H., Brest, P., Bridges, D., Bringer, M. -A., Brini, M., Brito, G. C., Brodin, B., Brookes, P. S., Brown, E. J., Brown, K., Broxmeyer, H. E., Bruhat, A., Brum, P. C., Brumell, J. H., Brunetti-Pierri, N., Bryson-Richardson, R. J., Buch, S., Buchan, A. M., Budak, H., Bulavin, D. V., Bultman, S. J., Bultynck, G., Bumbasirevic, V., Burelle, Y., Burke, R. E., Burmeister, M., Bütikofer, P., Caberlotto, L., Cadwell, K., Cahova, M., Cai, D., Cai, J., Cai, Q., Calatayud, S., Camougrand, N., Campanella, M., Campbell, G. R., Campbell, M., Campello, S., Candau, R., Caniggia, I., Cantoni, L., Cao, L., Caplan, A. B., Caraglia, M., Cardinali, C., Cardoso, S. M., Carew, J. S., Carleton, L. A., Carlin, C. R., Carloni, S., Carlsson, S. R., Carmona-Gutierrez, D., Carneiro, L. A. M., Carnevali, O., Carra, S., Carrier, A., Carroll, B., Casas, C., Casas, J., Cassinelli, G., Castets, P., Castro-Obregon, S., Cavallini, G., Ceccherini, I., Cecconi, F., Cederbaum, A. I., Ceña, V., Cenci, S., Cerella, C., Cervia, D., Cetrullo, S., Chaachouay, H., Chae, H. -J., Chagin, A. S., Chai, C. -Y., Chakrabarti, G., Chamilos, G., Chan, E. Y. W., Chan, M. T. V., Chandra, D., Chandra, P., Chang, C. -P., Chang, R. C. -C., Chang, T. Y., Chatham, J. C., Chatterjee, S., Chauhan, S., Che, Y., Cheetham, M. E., Cheluvappa, R., Chen, C. -J., Chen, G., Chen, G. -C., Chen, H., Chen, J. W., Chen, J. -K., Chen, M., Chen, P., Chen, Q., Chen, S. -D., Chen, S., Chen, S. S. -L., Chen, W., Chen, W. -J., Chen, W. Q., Chen, X., Chen, Y. -H., Chen, Y. -G., Chen, Y., Chen, Y. -J., Chen, Y. -Q., Chen, Z., Cheng, A., Cheng, C. H. K., Cheng, H., Cheong, H., Cherry, S., Chesney, J., Cheung, C. H. A., Chevet, E., Chi, H. C., Chi, S. -G., Chiacchiera, F., Chiang, H. -L., Chiarelli, R., Chiariello, M., Chieppa, M., Chin, L. -S., Chiong, M., Chiu, G. N. C., Cho, D. -H., Cho, S. -G., Cho, W. C., Cho, Y. -Y., Cho, Y. -S., Choi, A. M. K., Choi, E. -J., Choi, E. -K., Choi, J., Choi, M. E., Choi, S. -I., Chou, T. -F., Chouaib, S., Choubey, D., Choubey, V., Chow, K. -C., Chowdhury, K., Chu, C. T., Chuang, T. -H., Chun, T., Chung, H., Chung, T., Chung, Y. -L., Chwae, Y. -J., Cianfanelli, V., Ciarcia, R., Ciechomska, I. A., Ciriolo, M. R., Cirone, M., Claerhout, S., Clague, M. J., Cl� ria, J., Clarke, P. G. H., Clarke, R., Clementi, E., Cleyrat, C., Cnop, M., Coccia, E. M., Cocco, T., Codogno, P., Coers, J., Cohen, E. E. W., Colecchia, D., Coletto, L., Coll, N. S., Colucci-Guyon, E., Comincini, S., Condello, M., Cook, K. L., Coombs, G. H., Cooper, C. D., Cooper, J. M., Coppens, I., Corasaniti, M. T., Corazzari, M., Corbalan, R., Corcelle-Termeau, E., Cordero, M. D., Corral-Ramos, C., Corti, O., Cossarizza, A., Costelli, P., Costes, S., Cotman, S. L., Coto-Montes, A., Cottet, S., Couve, E., Covey, L. R., Cowart, L. A., Cox, J. S., Coxon, F. P., Coyne, C. B., Cragg, M. S., Craven, R. J., Crepaldi, T., Crespo, J. L., Criollo, A., Crippa, V., Cruz, M. T., Cuervo, A. M., Cuezva, J. M., Cui, T., Cutillas, P. R., Czaja, M. J., Czyzyk-Krzeska, M. F., Dagda, R. K., Dahmen, U., Dai, C., Dai, W., Dai, Y., Dalby, K. N., Valle, L. D., Dalmasso, G., D'Amelio, M., Damme, M., Darfeuille-Michaud, A., Dargemont, C., Darley-Usmar, V. M., Dasarathy, S., Dasgupta, B., Dash, S., Dass, C. R., Davey, H. M., Davids, L. M., Dávila, D., Davis, R. J., Dawson, T. M., Dawson, V. L., Daza, P., de Belleroche, J., de Figueiredo, P., de Figueiredo, R. C. B. Q., de la Fuente, J., De Martino, L., De Matteis, A., De Meyer, G. R. Y., De Milito, A., De Santi, M., de Souza, W., De Tata, V., De Zio, D., Debnath, J., Dechant, R., Decuypere, J. -P., Deegan, S., Dehay, B., Del Bello, B., Del Re, D. P., Delage-Mourroux, R., Delbridge, L. M. D., Deldicque, L., Delorme-Axford, E., Deng, Y., Dengjel, J., Denizot, M., Dent, P., Der, C. J., Deretic, V., Derrien, B., Deutsch, E., Devarenne, T. P., Devenish, R. J., Di Bartolomeo, S., Di Daniele, N., Di Domenico, F., Di Nardo, A., Di Paola, S., Di Pietro, A., Di Renzo, L., Di Antonio, A., Díaz-Araya, G., Díaz-Laviada, I., Diaz-Meco, M. T., Diaz-Nido, J., Dickey, C. A., Dickson, R. C., Diederich, M., Digard, P., Dikic, I., Dinesh-Kumar, S. P., Ding, C., Ding, W. -X., Ding, Z., Dini, L., Distler, J. H. W., Diwan, A., Djavaheri-Mergny, M., Dmytruk, K., Dobson, R. C. J., Doetsch, V., Dokladny, K., Dokudovskaya, S., Donadelli, M., Dong, X. C., Dong, X., Dong, Z., Donohue, T. M., Donohue-Jr, T. M., Doran, K. S., D'Orazi, G., Dorn, G. W., Dosenko, V., Dridi, S., Drucker, L., Du, J., L. -L., Du, Du, L., du Toit, A., Dua, P., Duan, L., Duann, P., Dubey, V. K., Duchen, M. R., Duchosal, M. A., Duez, H., Dugail, I., Dumit, V. I., Duncan, M. C., Dunlop, E. A., Dunn, W. A., Dupont, N., Dupuis, L., Durán, R. V., Durcan, T. M., Duvezin-Caubet, S., Duvvuri, U., Eapen, V., Ebrahimi-Fakhari, D., Echard, A., Eckhart, L., Edelstein, C. L., Edinger, A. L., Eichinger, L., Eisenberg, T., Eisenberg-Lerner, A., Eissa, N. T., El-Deiry, W. S., El-Khoury, V., Elazar, Z., Eldar-Finkelman, H., Elliott, C. J. H., Emanuele, E., Emmenegger, U., Engedal, N., Engelbrecht, A. -M., Engelender, S., Enserink, J. M., Erdmann, R., Erenpreisa, J., Eri, R., Eriksen, J. L., Erman, A., Escalante, R., Eskelinen, E. -L., Espert, L., Esteban-Martínez, L., Evans, T. J., Fabri, M., Fabrias, G., Fabrizi, C., Facchiano, A., Færgeman, N. J., Faggioni, A., Fairlie, W. D., Fan, C., Fan, D., Fan, J., Fang, S., Fanto, M., Fanzani, A., Farkas, T., Faure, M., Favier, F. B., Fearnhead, H., Federici, M., Fei, E., Felizardo, T. C., Feng, H., Feng, Y., Ferguson, T. A., Fernández, Á. F., Fernandez-Barrena, M. G., Fernandez-Checa, J. C., Fernández-López, A., Fernandez-Zapico, M. E., Feron, O., Ferraro, E., Ferreira-Halder, C. V., Fesus, L., Feuer, R., Fiesel, F. C., Filippi-Chiela, E. C., Filomeni, G., Fimia, G. M., Fingert, J. H., Finkbeiner, S., Finkel, T., Fiorito, F., Fisher, P. B., Flajolet, M., Flamigni, F., Florey, O., Florio, S., Floto, R. A., Folini, M., Follo, C., Fon, E. A., Fornai, F., Fortunato, F., Fraldi, A., Franco, R., Francois, A., François, A., Frankel, L. B., Fraser, I. D. C., Frey, N., Freyssenet, D. G., Frezza, C., Friedman, S. L., Frigo, D. E., Fu, D., Fuentes, J. M., Fueyo, J., Fujitani, Y., Fujiwara, Y., Fujiya, M., Fukuda, M., Fulda, S., Fusco, C., Gabryel, B., Gaestel, M., Gailly, P., Gajewska, M., Galadari, S., Galili, G., Galindo, I., Galindo, M. F., Galliciotti, G., Galluzzi, L., Galy, V., Gammoh, N., Gandy, S., Ganesan, A. K., Ganesan, S., Ganley, I. G., Gannagé, M., Gao, F. -B., Gao, F., Gao, J. -X., Nannig, L. G., Véscovi, E. G., Garcia-Macía, M., Garcia-Ruiz, C., Garg, A. D., Garg, P. K., Gargini, R., Gassen, N. C., Gatica, D., Gatti, E., Gavard, J., Gavathiotis, E., Ge, L., Ge, P., Ge, S., Gean, P. -W., Gelmetti, V., Genazzani, A. A., Geng, J., Genschik, P., Gerner, L., Gestwicki, J. E., Gewirtz, D. A., Ghavami, S., Ghigo, E., Ghosh, D., Giammarioli, A. M., Giampieri, F., Giampietri, C., Giatromanolaki, A., Gibbings, D. J., Gibellini, L., Gibson, S. B., Ginet, V., Giordano, A., Giorgini, F., Giovannetti, E., Girardin, S. E., Gispert, S., Giuliano, S., Gladson, C. L., Glavic, A., Gleave, M., Godefroy, N., Gogal, R. M., Gokulan, K., Goldman, G. H., Goletti, D., Goligorsky, M. S., Gomes, A. V., Gomes, L. C., Gomez, H., Gomez-Manzano, C., Gómez-Sánchez, R., Gonçalves, D. A. P., Goncu, E., Gong, Q., Gongora, C., Gonzalez, C. B., Gonzalez-Alegre, P., Gonzalez-Cabo, P., González-Polo, R. A., Goping, I. S., Gorbea, C., Gorbunov, N. V., Goring, D. R., Gorman, A. M., Gorski, S. M., Goruppi, S., Goto-Yamada, S., Gotor, C., Gottlieb, R. A., Gozes, I., Gozuacik, D., Graba, Y., Graef, M., Granato, G. E., Grant, G. D., Grant, S., Gravina, G. L., Green, D. R., Greenhough, A., Greenwood, M. T., Grimaldi, B., Gros, F., Grose, C., Groulx, J. -F., Gruber, F., Grumati, P., Grune, T., Guan, J. -L., Guan, K. -L., Guerra, B., Guillen, C., Gulshan, K., Gunst, J., Guo, C., Guo, L., Guo, M., Guo, W., Guo, X. -G., Gust, A. A., Gustafsson, Å. B., Gutierrez, E., Gutierrez, M. G., Gwak, H. -S., Haas, A., Haber, J. E., Hadano, S., Hagedorn, M., Hahn, D. R., Halayko, A. J., Hamacher-Brady, A., Hamada, K., Hamai, A., Hamann, A., Hamasaki, M., Hamer, I., Hamid, Q., Hammond, E. M., Han, F., Han, W., Handa, J. T., Hanover, J. A., Hansen, M., Harada, M., Harhaji-Trajkovic, L., Harper, J. W., Harrath, A. H., Harris, A. L., Harris, J., Hasler, U., Hasselblatt, P., Hasui, K., Hawley, R. G., Hawley, T. S., He, C., C. Y., He, He, F., He, G., R. -R., He, X. -H., He, Y. -W., He, Y. -Y., He, Heath, J. K., Hébert, M. -J., Heinzen, R. A., Helgason, G. V., Hensel, M., Henske, E. P., Her, C., Herman, P. K., Hernández, A., Hernandez, C., Hernández-Tiedra, S., Hetz, C., Hiesinger, P. 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Robin, Higaki, Katsumi, Hilfiker, Sabine, Hill, Bradford G., Hill, Joseph A., Hill, William D., Hino, Keisuke, Hofius, Daniel, Hofman, Paul, Höglinger, Günter U., Höhfeld, Jörg, Holz, Marina K., Hong, Yonggeun, Hood, David A., Hoozemans, Jeroen J.M., Hoppe, Thorsten, Hsu, Chin, Hsu, Chin-Yuan, Hsu, Li-Chung, Hu, Dong, Hu, Guochang, Hu, Hong-Ming, Hu, Hongbo, Hu, Ming Chang, Hu, Yu-Chen, Hu, Zhuo-Wei, Hua, Fang, Hua, Ya, Huang, Canhua, Huang, Huey-Lan, Huang, Kuo-How, Huang, Kuo-Yang, Huang, Shile, Huang, Shiqian, Huang, Wei-Pang, Huang, Yi-Ran, Huang, Yong, Huang, Yunfei, Huber, Tobias B., Huebbe, Patricia, Huh, Won-Ki, Hulmi, Juha J., Hur, Gang Min, Hurley, James H., Husak, Zvenyslava, Hussain, Sabah N.A., Hussain, Salik, Hwang, Jung Jin, Hwang, Seungmin, Hwang, Thomas I.S., Ichihara, Atsuhiro, Imai, Yuzuru, Imbriano, Carol, Inomata, Megumi, Into, Takeshi, Iovane, Valentina, Iovanna, Juan L., Iozzo, Renato V., Ip, Nancy Y., Irazoqui, Javier E., Iribarren, Pablo, Isaka, Yoshitaka, Isakovic, Aleksandra J., Ischiropoulos, Harry, Isenberg, Jeffrey S., Ishaq, Mohammad, Ishida, Hiroyuki, Ishii, Isao, Ishmael, Jane E., Isidoro, Ciro, Isobe, Ken-Ichi, Isono, Erika, Issazadeh-Navikas, Shohreh, Itahana, Koji, Itakura, Eisuke, Ivanov, Andrei I., Iyer, Anand Krishnan V., Izquierdo, José M., Izumi, Yotaro, Izzo, Valentina, Jäättelä, Marja, Jaber, Nadia, Jackson, Daniel John, Jackson, William T., Jacob, Tony George, Jacques, Thomas S., Jagannath, Chinnaswamy, Jain, Ashish, Jana, Nihar Ranjan, Jang, Byoung Kuk, Jani, Alkesh, Janji, Bassam, Jannig, Paulo Roberto, Jansson, Patric J., Jean, Steve, Jendrach, Marina, Jeon, Ju-Hong, Jessen, Niel, Jeung, Eui-Bae, Jia, Kailiang, Jia, Lijun, Jiang, Hong, Jiang, Hongchi, Jiang, Liwen, Jiang, Teng, Jiang, Xiaoyan, Jiang, Xuejun, Jiang, Ying, Jiang, Yongjun, Jiménez, Alberto, Jin, Cheng, Jin, Hongchuan, Jin, Lei, Jin, Meiyan, Jin, Shengkan, Jinwal, Umesh Kumar, Jo, Eun-Kyeong, Johansen, Terje, Johnson, Daniel E., Johnson, Gail V.W., Johnson, James D., Jonasch, Eric, Jones, Chri, Joosten, Leo A.B., Jordan, Joaquin, Joseph, Anna-Maria, Joseph, Bertrand, Joubert, Annie M., Ju, Dianwen, Ju, Jingfang, Juan, Hsueh-Fen, Juenemann, Katrin, Juhász, Gábor, Jung, Hye Seung, Jung, Jae U., Jung, Yong-Keun, Jungbluth, Heinz, Justice, Matthew J., Jutten, Barry, Kaakoush, Nadeem O., Kaarniranta, Kai, Kaasik, Allen, Kabuta, Tomohiro, Kaeffer, Bertrand, Kågedal, Katarina, Kahana, Alon, Kajimura, Shingo, Kakhlon, Or, Kalia, Manjula, Kalvakolanu, Dhan V., Kamada, Yoshiaki, Kambas, Konstantino, Kaminskyy, Vitaliy O., Kampinga, Harm H., Kandouz, Mustapha, Kang, Chanhee, Kang, Rui, Kang, Tae-Cheon, Kanki, Tomotake, Kanneganti, Thirumala-Devi, Kanno, Haruo, Kanthasamy, Anumantha G., Kantorow, Marc, Kaparakis-Liaskos, Maria, Kapuy, Orsolya, Karantza, Vassiliki, Karim, Md Razaul, Karmakar, Parimal, Kaser, Arthur, Kaushik, Susmita, Kawula, Thoma, Kaynar, A. Murat, Ke, Po-Yuan, Ke, Zun-Ji, Kehrl, John H., Keller, Kate E., Kemper, Jongsook Kim, Kenworthy, Anne K., Kepp, Oliver, Kern, Andrea, Kesari, Santosh, Kessel, David, Ketteler, Robin, Kettelhut, Isis do Carmo, Khambu, Bilon, Khan, Muzamil Majid, Khandelwal, Vinoth K.M., Khare, Sangeeta, Kiang, Juliann G., Kiger, Amy A., Kihara, Akio, Kim, Arianna L., Kim, Cheol Hyeon, Kim, Deok Ryong, Kim, Do-Hyung, Kim, Eung Kweon, Kim, Hye Young, Kim, Hyung-Ryong, Kim, Jae-Sung, Kim, Jeong Hun, Kim, Jin Cheon, Kim, Jin Hyoung, Kim, Kwang Woon, Kim, Michael D., Kim, Moon-Moo, Kim, Peter K., Kim, Seong Who, Kim, Soo-Youl, Kim, Yong-Sun, Kim, Yonghyun, Kimchi, Adi, Kimmelman, Alec C., Kimura, Tomonori, King, Jason S., Kirkegaard, Karla, Kirkin, Vladimir, Kirshenbaum, Lorrie A., Kishi, Shuji, Kitajima, Yasuo, Kitamoto, Katsuhiko, Kitaoka, Yasushi, Kitazato, Kaio, Kley, Rudolf A., Klimecki, Walter T., Klinkenberg, Michael, Klucken, Jochen, Knævelsrud, Helene, Knecht, Erwin, Knuppertz, Laura, Ko, Jiunn-Liang, Kobayashi, Satoru, Koch, Jan C., Koechlin-Ramonatxo, Christelle, Koenig, Ulrich, Koh, Young Ho, Köhler, Katja, Kohlwein, Sepp D., Koike, Masato, Komatsu, Masaaki, Kominami, Eiki, Kong, Dexin, Kong, Hee Jeong, Konstantakou, Eumorphia G., Kopp, Benjamin T., Korcsmaros, Tama, Korhonen, Laura, Korolchuk, Viktor I., Koshkina, Nadya V., Kou, Yanjun, Koukourakis, Michael I., Koumenis, Constantino, Kovács, Attila L., Kovács, Tibor, Kovacs, Werner J., Koya, Daisuke, Kraft, Claudine, Krainc, Dimitri, Kramer, Helmut, Kravic-Stevovic, Tamara, Krek, Wilhelm, Kretz-Remy, Carole, Krick, Roswitha, Krishnamurthy, Malathi, Kriston-Vizi, Jano, Kroemer, Guido, Kruer, Michael C., Kruger, Rejko, Ktistakis, Nicholas T., Kuchitsu, Kazuyuki, Kuhn, Christian, Kumar, Addanki Pratap, Kumar, Anuj, Kumar, Ashok, Kumar, Deepak, Kumar, Dhiraj, Kumar, Rakesh, Kumar, Sharad, Kundu, Mondira, Kung, Hsing-Jien, Kuno, Atsushi, Kuo, Sheng-Han, Kuret, Jeff, Kurz, Tino, Kwok, Terry, Kwon, Taeg Kyu, Kwon, Yong Tae, Kyrmizi, Irene, La Spada, Albert R., Lafont, Frank, Lahm, Tim, Lakkaraju, Aparna, Lam, Truong, Lamark, Trond, Lancel, Steve, Landowski, Terry H., Lane, Darius J.R., Lane, Jon D., Lanzi, Cinzia, Lapaquette, Pierre, Lapierre, Louis R., Laporte, Jocelyn, Laukkarinen, Johanna, Laurie, Gordon W., Lavandero, Sergio, Lavie, Lena, Lavoie, Matthew J., Law, Betty Yuen Kwan, Law, Helen Ka-Wai, Law, Kelsey B., Layfield, Robert, Lazo, Pedro A., Le Cam, Laurent, Le Roch, Karine G., Le Stunff, Hervé, Leardkamolkarn, Vijittra, Lecuit, Marc, Lee, Byung-Hoon, Lee, Che-Hsin, Lee, Erinna F., Lee, Gyun Min, Lee, He-Jin, Lee, Hsinyu, Lee, Jae Keun, Lee, Jongdae, Lee, Ju-Hyun, Lee, Jun Hee, Lee, Michael, Lee, Myung-Shik, Lee, Patty J., Lee, Sam W., Lee, Seung-Jae, Lee, Shiow-Ju, Lee, Stella Y., Lee, Sug Hyung, Lee, Sung Sik, Lee, Sung-Joon, Lee, Sunhee, Lee, Ying-Ray, Lee, Yong J., Lee, Young H., Leeuwenburgh, Christiaan, Lefort, Sylvain, Legouis, Renaud, Lei, Jinzhi, Lei, Qun-Ying, Leib, David A., Leibowitz, Gil, Lekli, Istvan, Lemaire, Stéphane D., Lemasters, John J., Lemberg, Marius K., Lemoine, Antoinette, Leng, Shuilong, Lenz, Guido, Lenzi, Paola, Lerman, Lilach O., Barbato, Daniele Lettieri, Leu, Julia I. 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Sue, Menna-Barreto, Rubem F.S., Menon, Manoj B., Meraz-Ríos, Marco A., Merla, Giuseppe, Merlini, Luciano, Merlot, Angelica M., Meryk, Andrea, Meschini, Stefania, Meyer, Joel N., Mi, Man-Tian, Miao, Chao-Yu, Micale, Lucia, Michaeli, Simon, Michiels, Carine, Migliaccio, Anna Rita, Mihailidou, Anastasia Susie, Mijaljica, Dalibor, Mikoshiba, Katsuhiko, Milan, Enrico, Miller-Fleming, Leonor, Mills, Gordon B., Mills, Ian G., Minakaki, Georgia, Minassian, Berge A., Ming, Xiu-Fen, Minibayeva, Farida, Minina, Elena A., Mintern, Justine D., Minucci, Saverio, Miranda-Vizuete, Antonio, Mitchell, Claire H., Miyamoto, Shigeki, Miyazawa, Keisuke, Mizushima, Noboru, Mnich, Katarzyna, Mograbi, Baharia, Mohseni, Simin, Moita, Luis Ferreira, Molinari, Marco, Molinari, Maurizio, Møller, Andreas Buch, Mollereau, Bertrand, Mollinedo, Faustino, Mongillo, Marco, Monick, Martha M., Montagnaro, Serena, Montell, Craig, Moore, Darren J., Moore, Michael N., Mora-Rodriguez, Rodrigo, Moreira, Paula I., Morel, Etienne, Morelli, Maria Beatrice, Moreno, Sandra, Morgan, Michael J., Moris, Arnaud, Moriyasu, Yuji, Morrison, Janna L., Morrison, Lynda A., Morselli, Eugenia, Moscat, Jorge, Moseley, Pope L., Mostowy, Serge, Motori, Elisa, Mottet, Deni, Mottram, Jeremy C., Moussa, Charbel E.-H., Mpakou, Vassiliki E., Mukhtar, Hasan, Levy, Jean M. 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Javier, Ollinger, Karin, Olsson, Stefan, Orban, Daniel P., Ordonez, Paulina, Orhon, Idil, Orosz, Laszlo, O'rourke, Eyleen J., Orozco, Helena, Ortega, Angel L., Ortona, Elena, Osellame, Laura D., Oshima, Junko, Oshima, Shigeru, Osiewacz, Heinz D., Otomo, Takanobu, Otsu, Kinya, Ou, Jing-Hsiung Jame, Outeiro, Tiago F., Ouyang, Dong-Yun, Ouyang, Hongjiao, Overholtzer, Michael, Ozbun, Michelle A., Ozdinler, P. 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- Subjects
Molecular Biology ,Cell Biology ,Settore BIO/06 - Anatomia Comparata E Citologia - Abstract
non presente
- Published
- 2016
14. Systemic blockade of ACVR2B ligands prevents chemotherapy-induced muscle wasting by restoring muscle protein synthesis without affecting oxidative capacity or atrogenes
- Author
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University of Helsinki, Research Programs Unit, University of Helsinki, Medicum, University of Helsinki, Physiology, Nissinen, T. A., Degerman, J., Räsänen, M., Poikonen, A. R., Koskinen, S., Mervaala, E., Pasternack, A., Ritvos, O., Kivela, R., Hulmi, J. J., University of Helsinki, Research Programs Unit, University of Helsinki, Medicum, University of Helsinki, Physiology, Nissinen, T. A., Degerman, J., Räsänen, M., Poikonen, A. R., Koskinen, S., Mervaala, E., Pasternack, A., Ritvos, O., Kivela, R., and Hulmi, J. J.
- Abstract
Doxorubicin is a widely used and effective chemotherapy drug. However, cardiac and skeletal muscle toxicity of doxorubicin limits its use. Inhibiting myostatin/activin signalling can prevent muscle atrophy, but its effects in chemotherapy-induced muscle wasting are unknown. In the present study we investigated the effects of doxorubicin administration alone or combined with activin receptor ligand pathway blockade by soluble activin receptor IIB (sACVR2B-Fc). Doxorubicin administration decreased body mass, muscle size and bone mineral density/content in mice. However, these effects were prevented by sACVR2B-Fc administration. Unlike in many other wasting situations, doxorubicin induced muscle atrophy without markedly increasing typical atrogenes or protein degradation pathways. Instead, doxorubicin decreased muscle protein synthesis which was completely restored by sACVR2B-Fc. Doxorubicin administration also resulted in impaired running performance without effects on skeletal muscle mitochondrial capacity/function or capillary density. Running performance and mitochondrial function were unaltered by sACVR2B-Fc administration. Tumour experiment using Lewis lung carcinoma cells demonstrated that sACVR2B-Fc decreased the cachectic effects of chemotherapy without affecting tumour growth. These results demonstrate that blocking ACVR2B signalling may be a promising strategy to counteract chemotherapy-induced muscle wasting without damage to skeletal muscle oxidative capacity or cancer treatment.
- Published
- 2016
15. Systemic blockade of ACVR2B ligands prevents chemotherapy-induced muscle wasting by restoring muscle protein synthesis without affecting oxidative capacity or atrogenes
- Author
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Nissinen, T. A., primary, Degerman, J., additional, Räsänen, M., additional, Poikonen, A. R., additional, Koskinen, S., additional, Mervaala, E., additional, Pasternack, A., additional, Ritvos, O., additional, Kivelä, R., additional, and Hulmi, J. J., additional
- Published
- 2016
- Full Text
- View/download PDF
16. Effect of diet composition on acid–base balance in adolescents, young adults and elderly at rest and during exercise
- Author
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Hietavala, E-M, primary, Stout, J R, additional, Hulmi, J J, additional, Suominen, H, additional, Pitkänen, H, additional, Puurtinen, R, additional, Selänne, H, additional, Kainulainen, H, additional, and Mero, A A, additional
- Published
- 2014
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17. Resistance training induced increase in muscle fiber size in young and older men
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Mero, A. A., primary, Hulmi, J. J., additional, Salmijärvi, H., additional, Katajavuori, M., additional, Haverinen, M., additional, Holviala, J., additional, Ridanpää, T., additional, Häkkinen, K., additional, Kovanen, V., additional, Ahtiainen, J. P., additional, and Selänne, H., additional
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- 2012
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18. Molecular signaling in muscle is affected by the specificity of resistance exercise protocol
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Hulmi, J. J., primary, Walker, S., additional, Ahtiainen, J. P., additional, Nyman, K., additional, Kraemer, W. J., additional, and Häkkinen, K., additional
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- 2010
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19. Stength, Endurance or Combined Training Elicit Diverse Skeletal Muscle Myosin Heavy Chain Isoform Proportion but Unaltered Androgen Receptor Concentration in Older Men
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Ahtiainen, J. P., primary, Hulmi, J. J., additional, Kraemer, W. J., additional, Lehti, M., additional, Pakarinen, A., additional, Mero, A. A., additional, Karavirta, L., additional, Sillanpää, E., additional, Selänne, H., additional, Alen, M., additional, Komulainen, J., additional, Kovanen, V., additional, Nyman, K., additional, and Häkkinen, K., additional
- Published
- 2009
- Full Text
- View/download PDF
20. Cellular and tissue expression of DAPIT, a phylogenetically conserved peptide.
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Kontro, H., Hulmi, J. J., Rahkila, P., and Kainulainen, H.
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- 2012
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21. Are FNDC5 gene expression and irisin release regulated by exercise?
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Pekkala, S., Wiklund, P. K., Hulmi, J. J., Ahtiainen, J. P., Horttanainen, M., Pöllänen, E., Mäkelä, K., Kainulainen, H., Häkkinen, K., Nyman, K., Alen, M., Herzig, K., and Cheng, S.
- Subjects
PROTEASE inhibitors ,PHYSICAL fitness ,GENETIC regulation - Abstract
Irisin, a proteolytic derivative of muscle integral membrane protein FNDC5 is released into the bloodstream after endurance exercise in mice and humans. The gene is regulated by PGC-1α to activate thermogenic programs in white adipose tissue. We wanted to test the hypothesis if FNDC5 and irisin are link to exercise type and duration and if these are age-dependent. Methods: Middle-aged, non-diabetic and non-athlete men performed a 1-hour low-intensity (50% VOmax) aerobic exercise (AE) with bicycle ergometer (n=17), 21-weeks of endurance exercise (EE, n=9) and a combined endurance and resistance exercise (EE+RE, n=9), and in age matched non-exercised controls (Con, n=2). Vastus lateralis biopsies and blood samples were taken at 3-hours post-exercise. Furthermore, skeletal muscle mRNA fold changes of PGC1α and FNDC5 are investigated after 1-hour and 48-hours of single resistance exercise bout (5 x 10 RM leg press) in (a) young (n=10) and (b) old (n=11) men. FNDC5 mRNA was quantified using Taqman primers by Real-Time quantitative PCR System. PGC1α and GAPDH were quantified using in-house designed primers, iQ SYBR supermix and CFX96 Real-time PCR Detection System. Relative expression levels for FNDC5 and PGC-1α were calculated with the deltaCt method and normalized to the expression of GAPDH. Serum irisin levels were measured from serum samples using a commercial EIA kit. Results: In non-diabetic and non-athlete middle-aged men no significant changes were observed in skeletal muscle PGC-1α, FNDC5 and serum irisin after 1-hour low-intensity aerobic exercise, 21-week endurance training or 21-week endurance training combined with resistance exercise (RE) training, whereas a single RE bout increased significantly FNDC5 mRNA by 1.4-fold post-RE in young, but not in old previously untrained men. Moreover, while the increase in PGC-1α mRNA at 1-hour post-RE in old men was significant, no significant changes in FNDC5 were detected. Apart from the single RE-bout, large intra and inter-individual variations in PGC-1α, FNDC5 and serum irisin in response to endurance exercise and RE training were observed. Importantly, changes in skeletal muscle PGC-1α gene expression were not consistently accompanied by corresponding changes in FNDC5. Our findings indicate that 1) for the most part, exercise does not increase FNDC5 expression in skeletal muscle; 2) factor(s) other than PGC-1αmay be involved in the regulation of FNDC5 expression. In conclusion, the large intra and inter-individual variation in FNDC5 and irisin in response to different types of exercise indicate that exercise does not seem to increase FNDC5 in skeletal muscle or circulating irisin levels. However, the increase in a subset of young individuals in acute RE warrants further studies to determine whether the effects of exercise on FNDC5 and irisin are collection time, exercise type, protocol, intensity and age-dependent. [ABSTRACT FROM AUTHOR]
- Published
- 2013
22. Muscle NAD + depletion and Serpina3n as molecular determinants of murine cancer cachexia-the effects of blocking myostatin and activins.
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Hulmi JJ, Penna F, Pöllänen N, Nissinen TA, Hentilä J, Euro L, Lautaoja JH, Ballarò R, Soliymani R, Baumann M, Ritvos O, Pirinen E, and Lalowski M
- Subjects
- Activin Receptors antagonists & inhibitors, Activin Receptors drug effects, Activin Receptors metabolism, Activins metabolism, Activins pharmacology, Acute-Phase Proteins physiology, Animals, Cachexia metabolism, Cachexia physiopathology, Cell Line, Tumor, Disease Models, Animal, Male, Mice, Mitochondria metabolism, Muscle, Skeletal physiology, Muscular Atrophy metabolism, Myostatin metabolism, Oxidative Phosphorylation, Serpins physiology, Acute-Phase Proteins metabolism, Muscle, Skeletal metabolism, NAD metabolism, Serpins metabolism
- Abstract
Objective: Cancer cachexia and muscle loss are associated with increased morbidity and mortality. In preclinical animal models, blocking activin receptor (ACVR) ligands has improved survival and prevented muscle wasting in cancer cachexia without an effect on tumour growth. However, the underlying mechanisms are poorly understood. This study aimed to identify cancer cachexia and soluble ACVR (sACVR) administration-evoked changes in muscle proteome., Methods: Healthy and C26 tumour-bearing (TB) mice were treated with recombinant sACVR. The sACVR or PBS control were administered either prior to the tumour formation or by continued administration before and after tumour formation. Muscles were analysed by quantitative proteomics with further examination of mitochondria and nicotinamide adenine dinucleotide (NAD
+ ) metabolism. To complement the first prophylactic experiment, sACVR (or PBS) was injected as a treatment after tumour cell inoculation., Results: Muscle proteomics in TB cachectic mice revealed downregulated signatures for mitochondrial oxidative phosphorylation (OXPHOS) and increased acute phase response (APR). These were accompanied by muscle NAD+ deficiency, alterations in NAD+ biosynthesis including downregulation of nicotinamide riboside kinase 2 (Nrk2), and decreased muscle protein synthesis. The disturbances in NAD+ metabolism and protein synthesis were rescued by treatment with sACVR. Across the whole proteome and APR, in particular, Serpina3n represented the most upregulated protein and the strongest predictor of cachexia. However, the increase in Serpina3n expression was associated with increased inflammation rather than decreased muscle mass and/or protein synthesis., Conclusions: We present evidence implicating disturbed muscle mitochondrial OXPHOS proteome and NAD+ homeostasis in experimental cancer cachexia. Treatment of TB mice with a blocker of activin receptor ligands restores depleted muscle NAD+ and Nrk2, as well as decreased muscle protein synthesis. These results indicate putative new treatment therapies for cachexia and that although acute phase protein Serpina3n may serve as a predictor of cachexia, it more likely reflects a condition of elevated inflammation., (Copyright © 2020 The Author(s). Published by Elsevier GmbH.. All rights reserved.)- Published
- 2020
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23. Beneficial effects of running and milk protein supplements on Sirtuins and risk factors of metabolic disorders in rats with low aerobic capacity.
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Lensu S, Pekkala SP, Mäkinen A, Karstunen N, Turpeinen AT, Hulmi JJ, Silvennoinen MM, Ma H, Kujala UM, Karvinen S, Koch LG, Britton SL, and Kainulainen H
- Abstract
Background: Physical activity and dietary intake of dairy products are associated with improved metabolic health. Dairy products are rich with branched chain amino acids that are essential for energy production. To gain insight into the mechanisms underlying the benefit of the sub-chronic effects of running and intake of milk protein supplements, we studied Low Capacity Runner rats (LCR), a rodent exercise model with risk for metabolic disorders. We especially focused on the role of Sirtuins, energy level dependent proteins that affect many cellular metabolic processes., Methods: Forty-seven adult LCR female rats sedentary or running voluntarily in wheels were fed normal chow and given supplements of either whey or milk protein drink (PD)-supplemented water, or water only for 21 weeks. Physiological responses were measured in vivo. Blood lipids were determined from serum. Mitochondrial markers and Sirtuins (Sirt1-7) including downstream targets were measured in plantaris muscle by western blotting., Results: For the first 10 weeks whey-drinking rats ran about 50% less compared to other groups; still, in all runners glucose tolerance improved and triglycerides decreased. Generally, running induced a ∼six-fold increase in running capacity and a ∼8% decrease in % body fat. Together with running, protein supplements increased the relative lean mass of the total body weight by ∼11%. In comparison with sedentary controls, running and whey increased HDL (21%) and whey, with or without running, lowered LDL (-34%). Running increased mitochondrial biogenesis and Sirtuins 3 and 4. When combined with exercise, both whey and milk protein drink induced about a 4-fold increase in Sirt3, compared to runners drinking water only, and about a 2-fold increase compared to the respective sedentary group. Protein supplements, with or without running, enhanced the phosphorylation level of the acetyl-coA-carboxylase, suggesting increased fat oxidation. Both supplemented diets increased Sirt5 and Sirt7 without an additional effect from exercise. Running diminished and PD supplement increased Sirt6., Conclusion: We demonstrate in rats new sub-chronic effects of milk proteins on metabolism that involve Sirtuins and their downstream targets in skeletal muscle. The results show that running and milk proteins act on reducing the risk factors of metabolic disorders and suggest that the underlying mechanisms may involve Sirtuins. Notably, we found that milk protein supplements have some favorable effects on metabolism even without running., Competing Interests: Anu T. Turpeinen is an employee of Valio Ltd, which provided the whey protein and milk protein drinks, but ATT and/or Valio Ltd had no role in the collection and analysis of the data. All other authors have no conflicts of interest., (© 2019 The Author(s).)
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- 2019
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24. Strength, [corrected] endurance or combined training elicit diverse skeletal muscle myosin heavy chain isoform proportion but unaltered androgen receptor concentration in older men.
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Ahtiainen JP, Hulmi JJ, Kraemer WJ, Lehti M, Pakarinen A, Mero AA, Karavirta L, Sillanpää E, Selänne H, Alen M, Komulainen J, Kovanen V, Nyman K, and Häkkinen K
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- Aged, Exercise physiology, Humans, Isometric Contraction physiology, Male, Middle Aged, Muscle, Skeletal metabolism, Oxygen Consumption physiology, Physical Endurance physiology, Quadriceps Muscle metabolism, RNA, Messenger metabolism, Testosterone blood, Myosin Heavy Chains metabolism, Receptors, Androgen metabolism, Resistance Training methods
- Abstract
We investigated whether the myosin heavy chain (MyHC) proportion and androgen receptor (AR) concentration in skeletal muscle differ following 21 weeks of strength, endurance and combined training in untrained older men. Strength (S) and endurance (E) groups trained twice per week and combined (S+E) group trained four times per week (two strength and two endurance). Muscle biopsies were obtained before and after the training period from m. vastus lateralis (VL) and AR mRNA and protein concentration and MyHC proportion were determined. 1RM increased during the training period in S, S+E and E but the changes were greater in S and S+E than in E. Statistically significant increases were observed only in S and S+E in maximal isometric force as well as in VL thickness. VO (2max) increased significantly only in E. MyHCIIa proportion increased in S, while MyHCIIa proportion decreased and MyHCI increased (p<0.05) in E. No statistically significant changes were observed in serum testosterone and in AR mRNA or protein concentrations. The present results indicate that 21 weeks of strength, endurance or combined training changed MyHC proportion according to the training method but did not have an effect on AR mRNA or protein expression in skeletal muscle at rest.
- Published
- 2009
- Full Text
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