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1.
PLoS One ; 17(8): e0273056, 2022.
Artigo em Inglês | MEDLINE | ID: mdl-35998179

RESUMO

Substantial evidence suggests an important role of liver function in brain health. Liver function is clinically assessed by measuring the activity of hepatic enzymes in the peripheral blood. Brain-derived neurotrophic factor (BDNF) is an important regulator of brain function. Therefore, we hypothesized that blood BDNF levels are associated with liver function and fibrosis. To test this hypothesis, in this cross-sectional study, we investigated whether serum BDNF concentration is associated with liver enzyme activity, aspartate aminotransferase (AST)/ alanine aminotransferase (ALT) ratio, and fibrosis-4 (FIB-4) index in middle-aged and older women. We found that serum BDNF level showed a significant positive association with ALT and γ-glutamyltranspeptidase (GGT) activity and negative association with FIB-4 index, and a trend of negative association with the AST/ALT ratio after adjustment for age. Additionally, these associations remained statistically significant even after adjustment for body mass index (BMI) and fasting blood glucose level. These results demonstrate associations of serum BDNF levels with liver enzymes and hepatic fibrosis-related indices, which may underlie liver-brain interactions.


Assuntos
Fator Neurotrófico Derivado do Encéfalo/sangue , Fígado , Idoso , Alanina Transaminase , Aspartato Aminotransferases , Estudos Transversais , Feminino , Humanos , Cirrose Hepática/diagnóstico , Pessoa de Meia-Idade
2.
Nutrients ; 10(10)2018 Oct 18.
Artigo em Inglês | MEDLINE | ID: mdl-30340425

RESUMO

Dietary protein intake is critical for the maintenance of skeletal muscle mass. Plasma amino acid concentrations increase with protein intake and increases in muscle protein synthesis are dependent on leucine concentrations. We aimed to investigate the effect of a mixed meal and free amino acids intake on plasma leucine concentrations. In this randomized crossover study, 10 healthy young men (age 25 ± 1 years, height 1.73 ± 0.02 m, weight 65.8 ± 1.5 kg) underwent tests under different conditions-intake of 2 g of leucine (LEU), intake of a mixed meal (protein 27.5 g, including 2.15 g of leucine, protein: fat: carbohydrate ratio-22:25:53) only (MEAL), intake of 2 g of leucine immediately after a mixed meal (MEAL-LEU) and intake of 2 g of leucine 180 min after a mixed meal (MEAL-LEU180). Blood samples were collected within 420 min (240 min for LEU only) after intake and changes in amino acid concentrations were evaluated. Although the maximum plasma leucine concentration increased to 442 ± 24 µM for LEU, it was lower at 347 ± 16 µM (p < 0.05 vs. LEU) for MEAL-LEU, 205 ± 8 µM (p < 0.05 vs. LEU) for MEAL. The maximum plasma leucine concentration for MEAL-LEU180 increased to 481 ± 27 µM and compared to LEU there was no significant difference (p > 0.1). The observation that rapid elevations in plasma leucine concentrations are suppressed when leucine is ingested at the same time as a meal suggests that the timing of its intake must be considered to maximize the anabolic response.


Assuntos
Aminoácidos/sangue , Proteínas Alimentares/administração & dosagem , Suplementos Nutricionais , Leucina/farmacologia , Refeições/fisiologia , Adulto , Estudos Cross-Over , Humanos , Masculino , Proteínas Musculares/metabolismo , Músculo Esquelético , Período Pós-Prandial , Biossíntese de Proteínas , Fatores de Tempo
3.
Physiol Rep ; 5(15)2017 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-28778992

RESUMO

Previous studies have reported that different modes of muscle contraction (i.e., eccentric or concentric contraction) with similar contraction times can affect muscle proteolytic responses. However, the effect of different contraction modes on muscle proteolytic response under the same force-time integral (FTI: contraction force × time) has not been investigated. The purpose of this study was to investigate the effect of different contraction modes, with the same FTI, on acute proteolytic signaling responses. Eleven-week-old male Sprague-Dawley rats were randomly assigned to eccentric (EC), concentric (CC), or isometric contraction (IC) groups. Different modes of muscle contraction were performed on the right gastrocnemius muscle using electrical stimulation, with the left muscle acting as a control. In order to apply an equivalent FTI, the number of stimulation sets was modified between the groups. Muscle samples were taken immediately and three hours after exercise. Phosphorylation of FoxO3a at Ser253 was significantly increased immediately after exercise compared to controls irrespective of contraction mode. The mRNA levels of the ubiquitin ligases, MuRF1, and MAFbx mRNA were unchanged by contraction mode or time. Phosphorylation of ULK1 at Ser317 (positive regulatory site) and Ser757 (negative regulatory site) was significantly increased compared to controls, immediately or 3 h after exercise, in all contraction modes. The autophagy markers (LC3B-II/I ratio and p62 expression) were unchanged, regardless of contraction mode. These data suggest that differences in contraction mode during resistance exercise with a constant FTI, are not factors in regulating proteolytic signaling in the early phase of skeletal muscle contraction.


Assuntos
Contração Muscular , Músculo Esquelético/metabolismo , Proteólise , Transdução de Sinais , Animais , Proteína Homóloga à Proteína-1 Relacionada à Autofagia/genética , Proteína Homóloga à Proteína-1 Relacionada à Autofagia/metabolismo , Proteína Forkhead Box O3/genética , Proteína Forkhead Box O3/metabolismo , Masculino , Proteínas Associadas aos Microtúbulos/genética , Proteínas Associadas aos Microtúbulos/metabolismo , Proteínas Musculares/genética , Proteínas Musculares/metabolismo , Músculo Esquelético/fisiologia , Condicionamento Físico Animal/fisiologia , Ratos , Ratos Sprague-Dawley , Proteínas Ligases SKP Culina F-Box/genética , Proteínas Ligases SKP Culina F-Box/metabolismo , Proteínas com Motivo Tripartido/genética , Proteínas com Motivo Tripartido/metabolismo , Ubiquitina-Proteína Ligases/genética , Ubiquitina-Proteína Ligases/metabolismo
4.
J Nutr Sci Vitaminol (Tokyo) ; 63(6): 379-388, 2017.
Artigo em Inglês | MEDLINE | ID: mdl-29332899

RESUMO

Dietary protein intake is critical for maintaining an optimal muscle mass, especially among older individuals. Although protein supplementation during resistance training (RT) has been shown to further augment training-induced muscle mass in older individuals, the impact of daily variations in protein intake on training-induced muscle mass has not been explored thus far. Therefore, this study aimed to investigate the relationship between the dietary protein and amino acid intake and RT-induced muscle hypertrophy among older individuals. Ten healthy older men (n=10; mean age=69±2 y; body weight (BW)=61.5±2.2 kg; height=1.65±0.02 m) participated in progressive RT performed 3 times/wk for 12 wk. Body composition (using DXA) and nutritional assessments (using a 3-d dietary record) were performed before and after the training period. Leg lean mass (LLM) increased significantly (15.0±0.8 vs. 15.4±0.8 kg, p<0.05) after RT, with no change in dietary nutrient intake. The average dietary protein intake was 1.62±0.11 g/kg BW/d, while essential amino acids was 600±51 mg/kg BW/d. Although the correlation between the increase in LLM and dietary protein intake was not significant, a significant correlation was found between the increase in LLM and dietary essential amino acid (EAA) intake. Furthermore, there were significant correlations between the increase in LLM and protein as well as EAA (especially leucine) intake at breakfast among subjects with suboptimal protein intake (p<0.05). Our study findings indicate that dietary protein as well as EAA intake may be significant contributing factors in muscle hypertrophic response during RT among healthy older men.


Assuntos
Aminoácidos Essenciais/administração & dosagem , Composição Corporal , Proteínas Alimentares/administração & dosagem , Músculo Esquelético/fisiologia , Treinamento Resistido , Idoso , Ingestão de Energia , Exercício Físico , Humanos , Leucina/administração & dosagem , Masculino , Proteínas Musculares/biossíntese , Força Muscular , Músculo Esquelético/crescimento & desenvolvimento , Avaliação Nutricional
5.
Nutr Res ; 36(11): 1193-1201, 2016 11.
Artigo em Inglês | MEDLINE | ID: mdl-27865617

RESUMO

Resistance exercise activates muscle protein synthesis via the mammalian target of rapamycin complex 1 (mTORC1) pathway and subsequent muscle hypertrophy. Upstream components of the mTORC1 pathway are widely known to be involved in Akt and extracellular signal-regulated kinase 1/2 (ERK1/2) signaling. Previous studies have shown that ginseng stimulated Akt and ERK1/2 signaling. Therefore, we hypothesized that panaxatriol (PT) derived from ginseng triggers mTORC1 signaling and muscle protein synthesis by activating both the Akt and ERK1/2 signaling pathways, and that PT additively stimulates muscle protein synthesis when combined with resistance exercise. The study included male Sprague-Dawley rats. The legs of the rats were divided into control, PT-only, exercise-only, and exercise + PT groups. The right legs were subjected to isometric resistance exercise using percutaneous electrical stimulation, whereas the left legs were used as controls. PT (0.2 g/kg) was administered immediately after exercise. The Akt and ERK1/2 phosphorylation levels were significantly higher in the exercise + PT group than in the exercise-only group 0.5 hour after exercise. The phosphorylation of p70S6K was significantly increased at both 0.5 and 3 hours after exercise, and it was higher in the exercise + PT group than in the exercise-only group at both 0.5 and 3 hours after exercise. Muscle protein synthesis was significantly increased 3 hours after exercise, and it was higher in the exercise + PT group than in the exercise-only group 3 hours after exercise. Our results suggest that PT derived from ginseng enhances resistance exercise-induced protein synthesis via mTORC1 signaling in rat skeletal muscle.


Assuntos
Ginsenosídeos/farmacologia , Alvo Mecanístico do Complexo 1 de Rapamicina/metabolismo , Proteínas Musculares/biossíntese , Músculo Esquelético/efeitos dos fármacos , Panax/química , Preparações de Plantas/farmacologia , Animais , Masculino , Alvo Mecanístico do Complexo 1 de Rapamicina/genética , Proteína Quinase 1 Ativada por Mitógeno/genética , Proteína Quinase 1 Ativada por Mitógeno/metabolismo , Proteínas Musculares/genética , Músculo Esquelético/metabolismo , Fosforilação , Condicionamento Físico Animal , Raízes de Plantas/química , Biossíntese de Proteínas/efeitos dos fármacos , Ratos , Ratos Sprague-Dawley , Proteínas Quinases S6 Ribossômicas 70-kDa/genética , Proteínas Quinases S6 Ribossômicas 70-kDa/metabolismo , Transdução de Sinais
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