Search

Your search keyword '"Gerlinger-Romero, Frederico"' showing total 31 results
Start Over Author "Gerlinger-Romero, Frederico"
31 results on '"Gerlinger-Romero, Frederico"'

1. Changes in Skeletal Muscle Protein Metabolism Signaling Induced by Glutamine Supplementation and Exercise

Author

Rodrigues Junior, Carlos Flores, primary, Murata, Gilson Masahiro, additional, Gerlinger-Romero, Frederico, additional, Nachbar, Renato Tadeu, additional, Marzuca-Nassr, Gabriel Nasri, additional, Gorjão, Renata, additional, Vitzel, Kaio Fernando, additional, Hirabara, Sandro Massao, additional, Pithon-Curi, Tania Cristina, additional, and Curi, Rui, additional

Published
2023
Full Text
View/download PDF

10. Effects of beta-hydroxy-beta-methylbutyrate (HMB) on the expression of ubiquitin ligases, protein synthesis pathways and contractile function in extensor digitorum longus (EDL) of fed and fasting rats

Author

Gerlinger-Romero, Frederico, Guimarães-Ferreira, Lucas, Yonamine, Caio Yogi, Salgueiro, Rafael Barrera, and Nunes, Maria Tereza

Subjects
Body weight, Proteolysis, Ubiquitin, Protein biosynthesis, Ligases, Fasting, Muscles, Psychology and mental health
Abstract

Beta-hydroxy-beta-methylbutyrate (HMB), a leucine metabolite, enhances the gain of skeletal muscle mass by increasing protein synthesis or attenuating protein degradation or both. The aims of this study were to investigate the effect of HMB on molecular factors controlling skeletal muscle protein synthesis and degradation, as well as muscle contractile function, in fed and fasted conditions. Wistar rats were supplied daily with HMB (320 mg/kg body weight diluted in NaCl-0.9%) or vehicle only (control) by gavage for 28 days. After this period, some of the animals were subjected to a 24-h fasting, while others remained in the fed condition. The EDL muscle was then removed, weighed and used to evaluate the genes and proteins involved in protein synthesis (AKT/4E-BP1/S6) and degradation (Fbxo32 and Trim63). A sub-set of rats were used to measure in vivo muscle contractile function. HMB supplementation increased AKT phosphorylation during fasting (three-fold). In the fed condition, no differences were detected in atrogenes expression between control and HMB supplemented group; however, HMB supplementation did attenuate the fasting-induced increase in their expression levels. Fasting animals receiving HMB showed improved sustained tetanic contraction times (one-fold) and an increased muscle to tibia length ratio (1.3-fold), without any cross-sectional area changes. These results suggest that HMB supplementation under fasting conditions increases AKT phosphorylation and attenuates the increased of atrogenes expression, followed by a functional improvement and gain of skeletal muscle weight, suggesting that HMB protects skeletal muscle against the deleterious effects of fasting. Keywords: HMB, Protein synthesis, Protein degradation, EDL, Muscle contraction, Author(s): Frederico Gerlinger-Romero[sup.1,3], Lucas Guimarães-Ferreira[sup.1,2], Caio Yogi Yonamine[sup.1], Rafael Barrera Salgueiro[sup.1] and Maria Tereza Nunes[sup.1] Introduction Among nutritional strategies aiming to preserve skeletal muscle mass and contractile function, hydroxy-beta-methylbutyrate (HMB), [...]

Published
2017
Full Text
View/download PDF

12. List of Contributors

Author

Ali, Asif, primary, Almada, Anthony L., additional, Amsterdam, Ezra A., additional, Aoi, Wataru, additional, Apong, Philip E., additional, Artioli, Guilherme G., additional, Atalay, Mustafa, additional, Augustine, Samuel, additional, Bagchi, Debasis, additional, Bashir, Raza, additional, Blocher, John C., additional, Bloomer, Richard J., additional, Bonifazi, Marco, additional, Botchlett, Rachel, additional, Brioche, Thomas, additional, Campbell, Wayne W., additional, Capelli, Bob, additional, Capelli, Carlo, additional, Connes, Philippe, additional, Cox, Don J., additional, Creighton, Brent C., additional, Culver, Bruce, additional, Curi, Rui, additional, Cysewski, Gerald R., additional, Das, Amitava, additional, Degens, Hans, additional, Deli, Chariklia K., additional, Demetrovics, Zsolt, additional, Druhan, Lawrence J., additional, Dufour, Stéphane, additional, Duncan, Michael J., additional, Dunn-Lewis, Courtenay, additional, Erskine, Robert M., additional, Evers, Brad, additional, Eynon, Nir, additional, Farney, Tyler M., additional, Fatouros, Ioannis G., additional, Favret, Fabrice, additional, de Farias, Maria Lucia Fleiuss, additional, Franchini, Emerson, additional, Freidenreich, Daniel J., additional, Gómez-Cabrera, Mari Carmen, additional, Gaffney, Gary, additional, Galaz, Gustavo A., additional, Georgakouli, Kalliopi, additional, Gerlinger-Romero, Frederico, additional, Griffiths, Mark D., additional, Guimarães-Ferreira, Lucas, additional, Habib, Safia, additional, Hanson, Erik D, additional, Hofmann, Hande, additional, Hulmi, Juha J., additional, Hunter, John, additional, Jamurtas, Athanasios Z., additional, Jenkins, Usha, additional, Jeukendrup, Asker, additional, Kappagoda, C. Tissa, additional, Karila, Tuomo, additional, Keogh, Justin W.L., additional, Kerksick, Chad M., additional, Kinnunen, Susanna, additional, Kirk, Erik P., additional, Kitchens, Edeth K., additional, Knechtle, Beat, additional, Kondo, Masakatsu, additional, Kraemer, William J., additional, Kulovitz, Michelle, additional, Lancha, Antonio H., additional, Lawler, John M., additional, Li, Jia, additional, Lingen, Jan, additional, Lombard, Joel R., additional, Luk, Hui-Ying, additional, Martinez-Bello, Vladimir, additional, McAllister, Matthew J., additional, McCarthy, John J., additional, McFarlin, Brian K., additional, Mero, Antti A., additional, Meyer, Flavia, additional, Midorikawa, Taishi, additional, Miller, Donald W., additional, Moriyama, Hiroyoshi, additional, Murai, Igor, additional, Nair, Sreejayan, additional, Naito, Yuji, additional, Neggers, Yasmin, additional, Nicastro, Humberto, additional, Nodland, Sonja E., additional, Ojala, Tuomo, additional, Okamura, Koji, additional, Oksala, Niku, additional, Panzhinskiy, Evgeniy, additional, Pareja-Galeano, Helios, additional, Pichon, Aurélien, additional, Pietrzkowski, Zbigniew, additional, Pinheiro, Carlos Hermano J., additional, Pogliaghi, Silvia, additional, Pond, Hartley, additional, Ren, Jun, additional, Ribeiro, Beatriz Gonçalves, additional, Robinson, Dennis H., additional, Sakamoto, Shizuo, additional, Sanchis-Gomar, Fabian, additional, Schönfelder, Martin, additional, Schtscherbyna, Annie, additional, Seifert, John, additional, Seixas Chaves, Daniela Fojo, additional, Sen, Chandan K., additional, Seppälä, Timo A., additional, Shiojima, Yoshiaki, additional, Dantas, Wagner Silva, additional, Smith, Bryan K., additional, Smith, JohnEric W., additional, Solis, Marina Y., additional, Stevens, Bruce R., additional, Stohs, Sidney J., additional, Sundell, Jan, additional, Szabo, Attila, additional, Takagi, Tomohisa, additional, Takemasa, Tohru, additional, Talbott, Shawn M., additional, Timmons, Brian Weldon, additional, Tritto, Aline C., additional, Vennerstrom, Jonathan L., additional, Venojärvi, Mika, additional, Vincent, John B., additional, Volek, Jeff S., additional, Volk, Brittanie M., additional, Wagner, Jon C., additional, Wal, Ankita, additional, Wal, Pranay, additional, Wilk, Boguslaw, additional, Wilson, Jacob M., additional, Wu, Guoyao, additional, Yoshikawa, Toshikazu, additional, Zamparo, Paola, additional, Eidy Zanchi, Nelo, additional, and Zhou, Jing, additional

Published
2013
Full Text
View/download PDF

14. Non-invasive assessment of dorsiflexor muscle function in mice

Author

Gerlinger Romero, Frederico, Addinsall, Alex B, Lovering, Richard M, Foletta, Victoria C, van der Poel, Chris, Della Gatta, Paul A, Russell, Aaron P, Gerlinger Romero, Frederico, Addinsall, Alex B, Lovering, Richard M, Foletta, Victoria C, van der Poel, Chris, Della Gatta, Paul A, and Russell, Aaron P

Published
2019

19. Diabetes modulates microRNAs 29b-3p, 29c-3p, 199a-5p and 532-3p expression in muscle: possible role in GLUT4 and HK2 repression

Author

Esteves, João V, Yonamine, Caio Y, Pinto-Junior, Danilo C, Gerlinger Romero, Frederico, Enguita, Francisco J, Machado, Ubiratan F, Esteves, João V, Yonamine, Caio Y, Pinto-Junior, Danilo C, Gerlinger Romero, Frederico, Enguita, Francisco J, and Machado, Ubiratan F

Abstract

The reduced expression of solute carrier family 2, facilitated glucose transporter member 4 (GLUT4) and hexokinase-2 (HK2) in skeletal muscle participates in insulin resistance of diabetes mellitus (DM). MicroRNAs (miRNAs) have emerged as important modulators of mRNA/protein expression, but their role in DM is unclear. We investigated miRNAs hypothetically involved in GLUT4/HK2 expression in soleus muscle of type 1 diabetes-like rats. In silico analysis revealed 651 miRNAs predicted to regulate solute carrier family 2 member 4 (Slc2a4) mRNA, several of them also predicted to regulate Hk2 mRNA, and 16 miRNAs were selected for quantification. Diabetes reduced Slc2a4/GLUT4 and Hk2/HK2 expression (50-77%), upregulated miR-29b-3p and miR-29c-3p (50-100%), and downregulated miR-93-5p, miR-150-5p, miR-199a-5p, miR-345-3p, and miR-532-3p (∼30%) expression. Besides, GLUT4 and HK2 proteins correlated (P < 0.05) negatively with miR-29b-3p and miR-29c-3p and positively with miR-199a-5p and miR-532-3p, suggesting that these miRNAs could be markers of alterations in GLUT4 and HK2 expression. Additionally, diabetes increased the nuclear factor kappa B subunit 1 protein (p50) expression, a repressor of Slc2a4, which was also predicted as a target for miR-199a-5p and miR-532-3p. Correlations were also detected between these miRNAs and blood glucose, 24-h glycosuria and plasma fructosamine, and insulin therapy reversed most of the alterations. In sum, we report that diabetes altered miR-29b-3p, miR-29c-3p, miR-199a-5p and miR-532-3p expression in muscle of male rats, where their predicted targets Slc2a4/GLUT4 and Hk2/HK2 are repressed. These data shed light on these miRNAs as a markers of impaired skeletal muscle glucose disposal, and, consequently, glycemic control in diabetes.

Published
2018

22. Erythropoietin does not enhance skeletal muscle protein synthesis following exercise in young and older adults

Author

Lamon, Severine, Zacharewicz, Evelyn, Arentson-Lantz, Emily, Della Gatta, Paul A., Ghobrial, Lobna, Gerlinger Romero, Frederico, Garnham, Andrew, Paddon-Jones, Douglas, Russell, Aaron P., Lamon, Severine, Zacharewicz, Evelyn, Arentson-Lantz, Emily, Della Gatta, Paul A., Ghobrial, Lobna, Gerlinger Romero, Frederico, Garnham, Andrew, Paddon-Jones, Douglas, and Russell, Aaron P.

Abstract

PURPOSE: Erythropoietin (EPO) is a renal cytokine that is primarily involved in hematopoiesis while also playing a role in non-hematopoietic tissues expressing the EPO-receptor (EPOR). The EPOR is present in human skeletal muscle. In mouse skeletal muscle, EPO stimulation can activate the AKT serine/threonine kinase 1 (AKT) signaling pathway, the main positive regulator of muscle protein synthesis. We hypothesized that a single intravenous EPO injection combined with acute resistance exercise would have a synergistic effect on skeletal muscle protein synthesis via activation of the AKT pathway. METHODS: Ten young (24.2 ± 0.9 years) and 10 older (66.6 ± 1.1 years) healthy subjects received a primed, constant infusion of [ring-13C(6)] L-phenylalanine and a single injection of 10,000 IU epoetin-beta or placebo in a double-blind randomized, cross-over design. 2 h after the injection, the subjects completed an acute bout of leg extension resistance exercise to stimulate skeletal muscle protein synthesis. RESULTS: Significant interaction effects in the phosphorylation levels of the members of the AKT signaling pathway indicated a differential activation of protein synthesis signaling in older subjects when compared to young subjects. However, EPO offered no synergistic effect on vastus lateralis mixed muscle protein synthesis rate in young or older subjects. CONCLUSIONS: Despite its ability to activate the AKT pathway in skeletal muscle, an acute EPO injection had no additive or synergistic effect on the exercise-induced activation of muscle protein synthesis or muscle protein synthesis signaling pathways.

Published
2016

24. Erratum: Short-term creatine supplementation decreases reactive oxygen species content with no changes in expression and activity of antioxidant enzymes in skeletal muscle

Author

Guimaraes-Ferreira, Lucas, Pinheiro, Carlos Hermano J., Gerlinger Romero, Frederico, Vitzel, Kaio F., Nachbar, Renato T., Curi, Rui, Nunes, Maria Tereza, Guimaraes-Ferreira, Lucas, Pinheiro, Carlos Hermano J., Gerlinger Romero, Frederico, Vitzel, Kaio F., Nachbar, Renato T., Curi, Rui, and Nunes, Maria Tereza

Published
2012

26. Effect of glutamine supplementation and resistive training in signaling pathways of protein synthesis and degradation in rat skeletal muscle

Author

Pithon‐Curi, Tania C, primary, Rodrigues, Carlos F, additional, Sousa, Luis G O, additional, Vasconcelos, Diogo A, additional, Vinolo, Marco A, additional, Rodrigues, Alice C, additional, Nachbar, Renato T, additional, Guimarães‐Ferreira, Lucas, additional, Gerlinger‐Romero, Frederico, additional, Sellitti, Donald F, additional, Hirabara, Sandro M, additional, and Curi, Rui, additional

Published
2013
Full Text
View/download PDF

30. MOLECULAR BASIS OF TESTOSTERONE, GROWTH HORMONE, AND INSULIN-LIKE GROWTH FACTOR 1 (IGF-1) ON SKELETAL MUSCLE HYPERTROPHY AND STRENGTH TRAINING RESPONSES.

Author

Gerlinger-Romero, Frederico, Chagas Caperuto, Érico, Fortes Maia, Adriano, and Guimarães-Ferreira, Lucas

Abstract

The hormones testosterone, growth hormone (GH) and insulin-like growth factor 1 (IGF-1) are important regulators of muscle mass, modulating processes of protein synthesis and degradation. This paper aims to discuss the molecular basis of actions of these hormones in skeletal muscle, the responses of acute and chronic, as well as possible influences upon neuromuscular adaptations to strength training. The manipulation of the training variables such as volume, intensity, rest intervals and muscle groups used directly affects the hormonal responses. Increased secretion of anabolic hormones could contribute to chronic adaptations -- muscle hypertrophy -- in response to training. However, the importance of hormonal response to this adaptation is still uncertain and needs further investigation. [ABSTRACT FROM AUTHOR]

Published
2013

31. BASES MOLECULARES DAS AÇÕES DA TESTOSTERONA, HORMÔNIO DO CRESCIMENTO E IGF-1 SOBRE A HIPERTROFIA MUSCULAR ESQUELÉTICA E RESPOSTAS AO TREINAMENTO DE FORÇA.

Author

Gerlinger-Romero, Frederico, Chagas Caperuto, Érico, Fortes Maia, Adriano, and Guimarães-Ferreira, Lucas

Subjects
*SKELETAL muscle physiology, *MUSCLE protein metabolism, *PHYSIOLOGICAL adaptation, *EXERCISE, *EXERCISE physiology, *MOLECULAR biology, *MUSCLE strength, *NEUROPHYSIOLOGY, *SOMATOMEDIN, *TESTOSTERONE, *COOLDOWN, *HUMAN growth hormone, *NEUROMUSCULAR system, *EXERCISE intensity
Abstract

The hormones testosterone, growth hormone (GH) and insulin-like growth factor 1 (IGF-1) are important regulators of muscle mass, modulating processes of protein synthesis and degradation. This paper aims to discuss the molecular basis of actions of these hormones in skeletal muscle, the responses of acute and chronic, as well as possible influences upon neuromuscular adaptations to strength training. The manipulation of the training variables such as volume, intensity, rest intervals and muscle groups used directly affects the hormonal responses. Increased secretion of anabolic hormones could contribute to chronic adaptations -- muscle hypertrophy -- in response to training. However, the importance of hormonal response to this adaptation is still uncertain and needs further investigation. [ABSTRACT FROM AUTHOR]

Published
2013

Catalog

Books, media, physical & digital resources
See catalog results