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1.
J Strength Cond Res ; 32(8): 2233-2242, 2018 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-28399016

RESUMO

Sharp, MH, Lowery, RP, Shields, KA, Lane, JR, Gray, JL, Partl, JM, Hayes, DW, Wilson, GJ, Hollmer, CA, Minivich, JR, and Wilson, JM. The effects of beef, chicken, or whey protein after workout on body composition and muscle performance. J Strength Cond Res 32(8): 2233-2242, 2018-The purpose of this study was to determine the effects of postworkout consumption of beef protein isolate (Beef), hydrolyzed chicken protein (Chx), or whey protein concentrate (WPC), compared with a control on body composition and muscle performance during 8 weeks of resistance training. Forty-one men and women were randomized into 4 groups: WPC (m = 5, f = 5; age [years] = 19 ± 2, height [cm] = 171 ± 10, mass [kg] = 74.60 ± 14.19), Beef (m = 5, f = 5; age [years] = 22 ± 4, height [cm] = 170 ± 7, mass [kg] = 70.13 ± 8.16), Chx (m = 5, f = 6; Age [years] = 21 ± 2, height [cm] = 169 ± 9, mass [kg] = 74.52 ± 13.83), and Maltodextrin (control) (m = 4, f = 6; age [years] = 21 ± 2, height [cm] = 170 ± 9, mass [kg] = 73.18 ± 10.96). Subjects partook in an 8-week periodized resistance training program. Forty-six grams of protein or a control were consumed immediately after training or at similar times on off-days. Dual-energy x-ray absorptiometry was used to determine changes in body composition. Maximum strength was assessed by 1 repetition maximum for bench press (upper body) and deadlift (lower body). Power output was measured using cycle ergometer. Whey protein concentrate (52.48 ± 11.15 to 54.96 ± 11.85 kg), Beef (51.68 ± 7.61 to 54.65 ± 8.67 kg), and Chx (52.97 ± 12.12 to 54.89 ± 13.43 kg) each led to a significant increase in lean body mass compared with baseline (p < 0.0001), whereas the control condition did not (53.14 ± 11.35 to 54.19 ± 10.74 kg). Fat loss was also significantly decreased at 8 weeks compared to baseline for all protein sources (p < 0.0001; WPC: 18.70 ± 7.38 to 17.16 ± 7.18 kg; Beef: 16.43 ± 5.71 to 14.65 ± 5.41 kg; Chx: 17.58 ± 5.57 to 15.87 ± 6.07 kg), but not the control condition (16.29 ± 7.14 to 14.95 ± 7.72 kg). One repetition maximum for both deadlift and bench press was significantly increased for all treatment groups when compared with baseline. No differences in strength were noted between conditions. Overall, the results of this study demonstrate that consuming quality sources of protein from meat or WPC lead to significant benefits in body composition compared with control.


Assuntos
Composição Corporal/efeitos dos fármacos , Suplementos Nutricionais , Força Muscular , Treinamento Resistido , Proteínas do Soro do Leite/farmacologia , Absorciometria de Fóton , Adolescente , Adulto , Animais , Bovinos , Galinhas , Método Duplo-Cego , Feminino , Humanos , Masculino , Músculo Esquelético/efeitos dos fármacos , Músculo Esquelético/fisiologia , Polissacarídeos/farmacologia , Carne Vermelha , Adulto Jovem
2.
J Nutr ; 147(2): 195-201, 2017 02.
Artigo em Inglês | MEDLINE | ID: mdl-27903833

RESUMO

BACKGROUND: Protein quantity and quality at a meal affect muscle protein synthesis (MPS); however, long-term effects of protein distribution at individual meals on adult muscle mass remain unknown. OBJECTIVE: We used a precise feeding protocol in adult rats to determine if optimizing postmeal MPS response by modifying the meal distribution of protein, and the amino acid leucine (Leu), would affect muscle mass. METHODS: Two studies were conducted with the use of male Sprague-Dawley rats (∼300 g) trained to consume 3 meals/d, then assigned to diet treatments with identical macronutrient contents (16% of energy from protein, 54% from carbohydrates, and 30% from fat) but differing in protein quality or meal distribution. Study 1 provided 16% protein at each meal with the use of whey, egg white, soy, or wheat gluten, with Leu concentrations of 10.9%, 8.8%, 7.7%, and 6.8% (wt:wt), respectively. Study 2 used whey protein with 16% protein at each meal [balanced distribution (BD)] or meals with 8%, 8%, and 27% protein [unbalanced distribution (UD)]. MPS and translation factors 4E binding protein 1 (4E-BP1) and ribosomal protein p70S6 (S6K) were determined before and after breakfast meals at 2 and 11 wk. Muscle weights and body composition were measured at 11 wk. RESULTS: In study 1, the breakfast meal increased MPS and S6K in whey and egg treatments but not in wheat or soy treatments. Gastrocnemius weight was greater in the whey group (2.20 ± 0.03 g) than the soy group (1.95 ± 0.04 g) (P < 0.05) and was intermediate in the egg and wheat groups. The wheat group had >20% more body fat than the soy, egg, or whey groups (P < 0.05). Study 2, postmeal MPS and translation factors were 30-45% greater in the BD group than the UD group (P < 0.05), resulting in 6% and 11% greater (P < 0.05) gastrocnemius and soleus weights at 11 wk. CONCLUSION: These studies show that meal distribution of protein and Leu influences MPS and long-term changes in adult muscle mass.


Assuntos
Composição Corporal/efeitos dos fármacos , Proteínas Alimentares/administração & dosagem , Leucina/administração & dosagem , Refeições , Músculo Esquelético/fisiologia , Ração Animal/análise , Animais , Composição Corporal/fisiologia , Masculino , Distribuição Aleatória , Ratos , Ratos Sprague-Dawley
3.
Am J Physiol Endocrinol Metab ; 308(4): E283-93, 2015 Feb 15.
Artigo em Inglês | MEDLINE | ID: mdl-25491724

RESUMO

The antileukemic agent asparaginase triggers the amino acid response (AAR) in the liver by activating the eukaryotic initiation factor 2 (eIF2) kinase general control nonderepressible 2 (GCN2). To explore the mechanism by which AAR induction is necessary to mitigate hepatic lipid accumulation and prevent liver dysfunction during continued asparaginase treatment, wild-type and Gcn2 null mice were injected once daily with asparaginase or phosphate buffered saline for up to 14 days. Asparaginase induced mRNA expression of multiple AAR genes and greatly increased circulating concentrations of the metabolic hormone fibroblast growth factor 21 (FGF21) independent of food intake. Loss of Gcn2 precluded mRNA expression and circulating levels of FGF21 and blocked mRNA expression of multiple genes regulating lipid synthesis and metabolism including Fas, Ppara, Pparg, Acadm, and Scd1 in both liver and white adipose tissue. Furthermore, rates of triglyceride export and protein expression of apolipoproteinB-100 were significantly reduced in the livers of Gcn2 null mice treated with asparaginase, providing a mechanistic basis for the increase in hepatic lipid content. Loss of AAR-regulated antioxidant defenses in Gcn2 null livers was signified by reduced Gpx1 gene expression alongside increased lipid peroxidation. Substantial reductions in antithrombin III hepatic expression and activity in the blood of asparaginase-treated Gcn2 null mice indicated liver dysfunction. These results suggest that the ability of the liver to adapt to prolonged asparaginase treatment is influenced by GCN2-directed regulation of FGF21 and oxidative defenses, which, when lost, corresponds with maladaptive effects on lipid metabolism and hemostasis.


Assuntos
Antineoplásicos/efeitos adversos , Asparaginase/efeitos adversos , Doença Hepática Induzida por Substâncias e Drogas/metabolismo , Fatores de Crescimento de Fibroblastos/agonistas , Fígado/efeitos dos fármacos , Proteínas Serina-Treonina Quinases/metabolismo , Triglicerídeos/metabolismo , Tecido Adiposo Branco/efeitos dos fármacos , Tecido Adiposo Branco/metabolismo , Tecido Adiposo Branco/patologia , Animais , Antineoplásicos/administração & dosagem , Asparaginase/administração & dosagem , Biomarcadores/sangue , Biomarcadores/metabolismo , Doença Hepática Induzida por Substâncias e Drogas/patologia , Proteínas de Escherichia coli/administração & dosagem , Proteínas de Escherichia coli/efeitos adversos , Feminino , Fatores de Crescimento de Fibroblastos/sangue , Regulação da Expressão Gênica/efeitos dos fármacos , Homeostase/efeitos dos fármacos , Injeções Intraperitoneais , Peroxidação de Lipídeos/efeitos dos fármacos , Fígado/metabolismo , Fígado/patologia , Masculino , Camundongos Endogâmicos C57BL , Camundongos Knockout , Proteínas Serina-Treonina Quinases/genética , RNA Mensageiro/metabolismo
4.
Br J Nutr ; 114(4): 519-32, 2015 Aug 28.
Artigo em Inglês | MEDLINE | ID: mdl-26198178

RESUMO

The aim of the present study was to investigate the mechanistic basis of protein deficiency during pregnancy in mother that is transduced to offspring. To this end, timed-pregnant Sprague-Dawley rats were fed either a control (20 % of energy from protein) or low-protein (LP, 8 % of energy from protein) diet during gestation. Tissues were collected after delivery from rat dams, and skeletal muscle was collected at postnatal day 38 from the offspring. Quantitative RT-PCR and Western blot analyses were performed to determine mRNA and protein levels. Histological analysis was performed to evaluate myofibre size. LP dams gained significantly less weight during pregnancy, developed muscle atrophy, and had significantly lower circulating threonine and histidine levels than control dams. The mRNA expression of the well-known amino acid response (AAR) pathway-related target genes was increased only in the skeletal muscle of LP dams, as well as the protein expression levels of activating transcription factor 4 (ATF4) and phosphorylated eukaryotic translation initiation factor 2α (p-eIF2α). The mRNA expression of autophagy-related genes was significantly increased in the skeletal muscle of LP dams. Moreover, the mRNA expression of genes involved in both AAR and autophagy pathways remained elevated and was memorised in the muscle of LP offspring that consumed a post-weaning control diet. Additionally, the LP diet increased an autophagy marker, microtubule-associated proteins 1A/1B light chain 3B (LC3B) protein expression in the skeletal muscle of rat dams, consistent with the initiation of autophagy. The LP diet further increased ATF4 binding at the predicted regions of AAR and autophagy pathway-related genes. Increased binding of ATF4 unveils the crucial role of ATF4 in the activation of autophagy in response to protein restriction. Our data suggest that molecular changes in maternal muscle are memorised in the offspring long after gestational protein restriction, reinforcing the role of maternal signalling in programming offspring health.


Assuntos
Fator 4 Ativador da Transcrição/metabolismo , Aminoácidos/metabolismo , Autofagia , Dieta com Restrição de Proteínas , Proteínas Alimentares/administração & dosagem , Músculo Esquelético/metabolismo , Fenômenos Fisiológicos da Nutrição Pré-Natal , Animais , Autofagia/genética , Proteínas Alimentares/farmacologia , Ingestão de Energia , Fatores de Iniciação em Eucariotos/metabolismo , Feminino , Masculino , Memória , Proteínas Associadas aos Microtúbulos/metabolismo , Gravidez , RNA Mensageiro/metabolismo , Ratos Sprague-Dawley
5.
Am J Physiol Endocrinol Metab ; 305(9): E1124-33, 2013 Nov 01.
Artigo em Inglês | MEDLINE | ID: mdl-24002574

RESUMO

Asparaginase is an important drug in the treatment regimen for acute lymphoblastic leukemia. Asparaginase depletes circulating asparagine and glutamine, activating an amino acid stress response (AAR) involving phosphorylation of eukaryotic initiation factor 2 (eIF2) by general control nonderepressible kinase 2 (GCN2). We hypothesized that GCN2 functions to mitigate hepatic stress during asparaginase therapy by activating the AAR. To test this idea, C57BL/6J wild-type mice (Gcn2(+/+)) and those deleted for Gcn2 (Gcn2(-/-)) were injected with asparaginase or saline excipient one time daily for 1 or 6 days. In liver, increased phosphorylation of eIF2 and mRNA expression of AAR target genes activating transcription factor 4, asparagine synthetase, eIF4E-binding protein 1, and CAAT enhancer-binding protein homologous protein were significantly blunted or blocked in the liver of Gcn2(-/-) mice. Loss of AAR during asparaginase coincided with increases in mammalian target of rapamycin signaling, hepatic triglyceride accumulation, and DNA damage in association with genetic markers of oxidative stress (glutathione peroxidase) and inflammation (tumor necrosis factor alpha-α). Although asparaginase depleted circulating asparagine in both Gcn2(+/+) and Gcn2(-/-) mice, all other amino acids, including plasma glutamine, were elevated in the plasma of Gcn2(-/-) mice. This study shows that loss of GCN2 promotes oxidative stress and inflammatory-mediated DNA damage during asparaginase therapy, suggesting that patients with reduced or dysfunctional AAR may be at risk of developing hepatic complications during asparaginase treatment.


Assuntos
Antineoplásicos/antagonistas & inibidores , Antineoplásicos/toxicidade , Asparaginase/antagonistas & inibidores , Asparaginase/toxicidade , Doença Hepática Induzida por Substâncias e Drogas/prevenção & controle , Proteínas Serina-Treonina Quinases/farmacologia , Aminoácidos/sangue , Animais , Antineoplásicos/uso terapêutico , Asparaginase/uso terapêutico , Western Blotting , Peso Corporal/genética , Peso Corporal/fisiologia , Dano ao DNA , Ingestão de Alimentos/genética , Ingestão de Alimentos/fisiologia , Estresse do Retículo Endoplasmático/efeitos dos fármacos , Feminino , Inflamação/fisiopatologia , Fígado/metabolismo , Masculino , Alvo Mecanístico do Complexo 1 de Rapamicina , Camundongos , Camundongos Endogâmicos C57BL , Camundongos Knockout , Complexos Multiproteicos/genética , Complexos Multiproteicos/fisiologia , Tamanho do Órgão/genética , Tamanho do Órgão/fisiologia , Reação em Cadeia da Polimerase em Tempo Real , Serina-Treonina Quinases TOR/genética , Serina-Treonina Quinases TOR/fisiologia , Triglicerídeos/metabolismo , Resposta a Proteínas não Dobradas/efeitos dos fármacos , Resposta a Proteínas não Dobradas/genética
6.
J Strength Cond Res ; 26(6): 1724-9, 2012 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-21912291

RESUMO

Muscle fibers are generally fractionated into type I, IIA, and IIX fibers. Type I fibers specialize in long duration contractile activities and are found in abundance in elite endurance athletes. Conversely type IIA and IIX fibers facilitate short-duration anaerobic activities and are proportionally higher in elite strength and power athletes. A central area of interest concerns the capacity of training to increase or decrease fiber types to enhance high-performance activities. Although interconversions between type IIA and IIX are well recognized in the literature, there are conflicting studies regarding the capacity of type I and II fibers to interconvert. Therefore, the purpose of this article is to analyze the effects of various forms of exercise on type I and type II interconversions. Possible variables that may increase type II fibers and decrease type I fibers are discussed, and these include high velocity isokinetic contractions; ballistic movements such as bench press throws and sprints. Conversely, a shift from type II to type I fibers may occur under longer duration, higher volume endurance type events. Special care is taken to provide practical applications for both the scientist and the athlete.


Assuntos
Exercício Físico/fisiologia , Contração Muscular/fisiologia , Fibras Musculares Esqueléticas/fisiologia , Resistência Física/fisiologia , Treinamento Resistido/métodos , Atletas , Humanos
7.
Am J Physiol Endocrinol Metab ; 301(6): E1236-42, 2011 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-21917636

RESUMO

Muscle protein synthesis (MPS) increases after consumption of a protein-containing meal but returns to baseline values within 3 h despite continued elevations of plasma amino acids and mammalian target of rapamycin (mTORC1) signaling. This study evaluated the potential for supplemental leucine (Leu), carbohydrates (CHO), or both to prolong elevated MPS after a meal. Male Sprague-Dawley rats (∼270 g) trained to consume three meals daily were food deprived for 12 h, and then blood and gastrocnemius muscle were collected 0, 90, or 180 min after a standard 4-g test meal (20% whey protein). At 135 min postmeal, rats were orally administered 2.63 g of CHO, 270 mg of Leu, both, or water (sham control). Following test meal consumption, MPS peaked at 90 min and then returned to basal (time 0) rates at 180 min, although ribosomal protein S6 kinase and eIF4E-binding protein-1 phosphorylation remained elevated. In contrast, rats administered Leu and/or CHO supplements at 135 min postmeal maintained peak MPS through 180 min. MPS was inversely associated with the phosphorylation states of translation elongation factor 2, the "cellular energy sensor" adenosine monophosphate-activated protein kinase-α (AMPKα) and its substrate acetyl-CoA carboxylase, and increases in the ratio of AMP/ATP. We conclude that the incongruity between MPS and mTORC1 at 180 min reflects a block in translation elongation due to reduced cellular energy. Administering Leu or CHO supplements ∼2 h after a meal maintains cellular energy status and extends the postprandial duration of MPS.


Assuntos
Adenilato Quinase/metabolismo , Carboidratos da Dieta/farmacologia , Leucina/farmacologia , Fator 2 de Elongação de Peptídeos/metabolismo , Período Pós-Prandial/efeitos dos fármacos , Biossíntese de Proteínas/efeitos dos fármacos , Aminoácidos/sangue , Aminoácidos/metabolismo , Animais , Suplementos Nutricionais , Leucina/administração & dosagem , Leucina/sangue , Masculino , Proteínas Musculares/efeitos dos fármacos , Proteínas Musculares/metabolismo , Fosforilação , Período Pós-Prandial/fisiologia , Proteínas Quinases/metabolismo , Ratos , Ratos Sprague-Dawley , Fatores de Tempo
8.
Sports (Basel) ; 4(2)2016 May 06.
Artigo em Inglês | MEDLINE | ID: mdl-29910274

RESUMO

Periods of intense training can elicit an acute decline in performance and body composition associated with weakened hormone profiles. This study investigated the effects of a multi-ingredient performance supplement (MIPS) on body composition and hormone levels in college athletes following a six-week training protocol. Twenty male college athletes were equally assigned to MIPS and placebo (PLA) groups for supplementation (three pills, twice daily) in conjunction with resistance training and specialized sports training (e.g., nine total sessions/week) for six weeks. Dual Energy X-ray Absorptiometry determined body composition at weeks 0 and 6. Serum samples collected at weeks 0 and 6 determined free testosterone (FT), total testosterone (TT), IGF-1 and total estrogen (TE) levels. PLA experienced a significant decline in lean body mass (LBM) (-1.5 kg; p < 0.05) whereas the MIPS sustained LBM. The MIPS increased TT 21.9% (541.5 ± 48.7 to 639.1 ± 31.7) and increased FT 15.2% (13.28 ± 1.1 to 15.45 ± 1.3 ng/dL) (p < 0.05). Conversely, PLA decreased TT 7.9% (554.5 ± 43.3 to 497.2 ± 39.1 ng/dL), decreased FT 17.4% (13.41 ± 1.8 to 11.23 ± 2.55 ng/dL), and decreased FT:E 12.06% (p < 0.05). These findings suggest the MIPS can prevent decrements in LBM and anabolic hormone profiles during intense training periods.

9.
J Appl Physiol (1985) ; 118(1): 61-70, 2015 Jan 01.
Artigo em Inglês | MEDLINE | ID: mdl-25257878

RESUMO

Precise regulation of hepatic triglyceride (TG) metabolism and secretion is critical for health, and exercise could play a significant role. We compared one session of high-intensity interval exercise (HIIE) vs. continuous exercise (CE) on hepatic TG metabolism. Female and male mice were assigned to CE, HIIE, or sedentary control (CON). HIIE was a 30-min session of 30-s running intervals (30 m/min) interspersed with 60-s walking periods (5 m/min). CE was a distance- and duration-matched run at 13.8 m/min. Hepatic content of TG and TG secretion rates, as well as expression of relevant genes/proteins, were measured at 3 h (day 1) and 28 h (day 2) postexercise. On day 1, hepatic [TG] in CE and HIIE were both elevated vs. CON in both sexes with an approximately twofold greater elevation in HIIE vs. CE in females. In both sexes, hepatic perilipin 2 (PLIN2) protein on day 1 was increased significantly by both exercise types with a significantly greater increase with HIIE than CE, whereas the increase in mRNA reached significance only after HIIE. On day 2 in both sexes the increases in hepatic TG and PLIN2 with exercise declined toward CON levels. Only HIIE on day 2 resulted in reduced hepatic TG secretion by ∼20% in females with no effect in males. Neither exercise modality altered AMPK signaling or microsomal triglyceride transfer protein expression. Females exhibited higher hepatic TG secretion than males in association with different expression levels of related metabolic enzymes. These intensity-dependent and sex-specific alterations following exercise may have implications for sex-based exercise prescription.


Assuntos
Fígado/metabolismo , Condicionamento Físico Animal/fisiologia , Triglicerídeos/metabolismo , Adenilato Quinase/metabolismo , Animais , Feminino , Metabolismo dos Lipídeos , Masculino , Proteínas de Membrana/metabolismo , Camundongos , Consumo de Oxigênio/fisiologia , Perilipina-2 , Fosforilação , Condicionamento Físico Animal/métodos , Esforço Físico , Fatores Sexuais
10.
Nutrition ; 29(1): 29-36, 2013 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-23085015

RESUMO

Muscle loss is common during aging and chronic diseases, such as cancer and acquired immunodeficiency syndrome. Moreover, muscle loss has been correlated with decreased physical function, quality of life, and mortality in these populations. Therefore, interventions to counteract muscle loss in the elderly and clinical populations are needed. Recently, the efficacy of the leucine metabolite, ß-hydroxy-ß-methylbutyrate (HMB), to maintain muscle mass has been investigated in these populations. Many studies have found increases in lean mass and strength in the elderly and clinical populations when using HMB; however, not all studies have found beneficial effects of HMB supplementation. The present review summarizes published human studies investigating the efficacy of HMB supplementation in the elderly and clinical populations. In addition, the mechanisms by which HMB may exert its effects are summarized and future research directions are suggested.


Assuntos
Suplementos Nutricionais , Valeratos/administração & dosagem , Idoso , Envelhecimento/patologia , Envelhecimento/fisiologia , Animais , Atletas , Modelos Animais de Doenças , Humanos , Modelos Biológicos , Força Muscular , Músculo Esquelético/patologia , Músculo Esquelético/fisiopatologia , Atrofia Muscular/dietoterapia , Atrofia Muscular/patologia , Atrofia Muscular/fisiopatologia , Segurança , Transdução de Sinais , Resultado do Tratamento , Valeratos/metabolismo
11.
J Int Soc Sports Nutr ; 10(1): 6, 2013 Feb 02.
Artigo em Inglês | MEDLINE | ID: mdl-23374455

RESUMO

Position Statement: The International Society of Sports Nutrition (ISSN) bases the following position stand on a critical analysis of the literature on the use of beta-hydroxy-beta-methylbutyrate (HMB) as a nutritional supplement. The ISSN has concluded the following. 1. HMB can be used to enhance recovery by attenuating exercise induced skeletal muscle damage in trained and untrained populations. 2. If consuming HMB, an athlete will benefit from consuming the supplement in close proximity to their workout. 3. HMB appears to be most effective when consumed for 2 weeks prior to an exercise bout. 4. Thirty-eight mg·kg·BM-1 daily of HMB has been demonstrated to enhance skeletal muscle hypertrophy, strength, and power in untrained and trained populations when the appropriate exercise prescription is utilized. 5. Currently, two forms of HMB have been used: Calcium HMB (HMB-Ca) and a free acid form of HMB (HMB-FA). HMB-FA may increase plasma absorption and retention of HMB to a greater extent than HMB-CA. However, research with HMB-FA is in its infancy, and there is not enough research to support whether one form is superior. 6. HMB has been demonstrated to increase LBM and functionality in elderly, sedentary populations. 7. HMB ingestion in conjunction with a structured exercise program may result in greater declines in fat mass (FM). 8. HMB's mechanisms of action include an inhibition and increase of proteolysis and protein synthesis, respectively. 9. Chronic consumption of HMB is safe in both young and old populations.

12.
Nutrients ; 4(11): 1723-39, 2012 Nov 13.
Artigo em Inglês | MEDLINE | ID: mdl-23201843

RESUMO

Previous research demonstrates that the anabolic response of muscle protein synthesis (MPS) to a meal is regulated at the level of translation initiation with signals derived from leucine (Leu) and insulin to activate mTORC1 signaling. Recent evidence suggests that the duration of the meal response is limited by energy status of the cell and inhibition of translation elongation factor 2 (eEF2). This study evaluates the potential to extend the anabolic meal response with post-meal supplements of Leu or carbohydrates. Adult (~256 g) male Sprague-Dawley rats were food deprived for 12 h, then either euthanized before a standard meal (time 0) or at 90 or 180 min post-meal. At 135 min post-meal, rats received one of five oral supplements: 270 mg leucine (Leu270), 80:40:40 mg leucine, isoleucine, and valine (Leu80), 2.63 g carbohydrates (CHO2.6), 1 g carbohydrates (CHO1.0), or water (Sham control). Following the standard meal, MPS increased at 90 min then declined to pre-meal baseline at 180 min. Rats administered Leu270, Leu80, CHO2.6, or CHO1.0 maintained elevated rates of MPS at 180 min, while Sham controls declined from peak values. Leu80 and CHO1.0 treatments maintained MPS, but with values intermediate between Sham controls and Leu270 and CHO2.6 supplements. Consistent with MPS findings, the supplements maintained elongation activity and cellular energy status by preventing increases in AMP/ATP and phosphorylation of adenosine monophosphate-activated protein kinase (AMPK), acetyl-CoA carboxylase ACC and eEF2. The impact of the supplements on MPS and cellular energy status was in proportion to the energy content within the individual treatments (i.e., Leu270 > Leu80; CHO2.6 > CHO1.0), but the Leu supplements produced a disproportionate anabolic stimulation of MPS, eEF2 and energy status with significantly lower energy content. In summary, the incongruity between MPS and translation initiation at 180 min reflects a block in translation elongation due to reduced cellular energy, and the extent to which Leu or carbohydrate supplements are able to enhance energy status and prolong the period of muscle anabolism are dose and time-dependent.


Assuntos
Adenilato Quinase/metabolismo , Carboidratos da Dieta/administração & dosagem , Leucina/administração & dosagem , Proteínas Musculares/biossíntese , Fator 2 de Elongação de Peptídeos/metabolismo , Período Pós-Prandial/fisiologia , Aminoácidos Essenciais/sangue , Animais , Suplementos Nutricionais , Relação Dose-Resposta a Droga , Metabolismo Energético/efeitos dos fármacos , Homeostase/efeitos dos fármacos , Cinética , Masculino , Músculo Esquelético/efeitos dos fármacos , Músculo Esquelético/metabolismo , Elongação Traducional da Cadeia Peptídica , Iniciação Traducional da Cadeia Peptídica , Fosforilação , Ratos , Ratos Sprague-Dawley
13.
Nutr Metab (Lond) ; 9(1): 67, 2012 Jul 20.
Artigo em Inglês | MEDLINE | ID: mdl-22818257

RESUMO

BACKGROUND: Leucine (Leu) regulates muscle protein synthesis (MPS) producing dose-dependent plasma Leu and MPS responses from free amino acid solutions. This study examined the role of Leu content from dietary proteins in regulation of MPS after complete meals. METHODS: Experiment 1 examined 4 protein sources (wheat, soy, egg, and whey) with different Leu concentrations (6.8, 8.0, 8.8, and 10.9% (w/w), respectively) on the potential to increase plasma Leu, activate translation factors, and stimulate MPS. Male rats (~250 g) were trained for 14 day to eat 3 meals/day consisting of 16/54/30% of energy from protein, carbohydrates and fats. Rats were killed on d14 either before or 90 min after consuming a 4 g breakfast meal. Experiment 2 compared feeding wheat, whey, and wheat + Leu to determine if supplementing the Leu content of the wheat meal would yield similar anabolic responses as whey. RESULTS: In Experiment 1, only whey and egg groups increased post-prandial plasma Leu and stimulated MPS above food-deprived controls. Likewise, greater phosphorylation of p70 S6 kinase 1 (S6K1) and 4E binding protein-1 (4E-BP1) occurred in whey and egg groups versus wheat and soy groups. Experiment 2 demonstrated that supplementing wheat with Leu to equalize the Leu content of the meal also equalized the rates of MPS. CONCLUSION: These findings demonstrate that Leu content is a critical factor for evaluating the quantity and quality of proteins necessary at a meal for stimulation of MPS.

14.
Res Q Exerc Sport ; 80(3): 469-79, 2009 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-19791633

RESUMO

We tested expert baseball pitchers for evidence of especial skills at the regulation pitching distance. Seven college pitchers threw indoors to a target placed at 60.5 feet (18.44 m) and four closer and four further distances away. Accuracy at the regulation distance was significantly better than predicted by regression on the nonregulation distances (p < .02), indicating an especial skill effect emerged despite the absence of normal contextual cues. Self-efficacy data failed to support confidence as a mediating factor in especial skill effect. We concluded that cognitive theories fail to fully account for the patterns of observed data, and therefore theoretical explanations of the especial skills must address noncognitive aspects of motor learning and control.


Assuntos
Beisebol/fisiologia , Aprendizagem , Destreza Motora/fisiologia , Autoeficácia , Comportamento Competitivo , Humanos , Masculino , Desempenho Psicomotor , Análise de Regressão , Inquéritos e Questionários , Adulto Jovem
15.
Nutr Metab (Lond) ; 5: 1, 2008 Jan 03.
Artigo em Inglês | MEDLINE | ID: mdl-18173841

RESUMO

The leucine metabolite beta-hydroxy-beta-methylbutyrate (HMB) has been extensively used as an ergogenic aid; particularly among bodybuilders and strength/power athletes, who use it to promote exercise performance and skeletal muscle hypertrophy. While numerous studies have supported the efficacy of HMB in exercise and clinical conditions, there have been a number of conflicting results. Therefore, the first purpose of this paper will be to provide an in depth and objective analysis of HMB research. Special care is taken to present critical details of each study in an attempt to both examine the effectiveness of HMB as well as explain possible reasons for conflicting results seen in the literature. Within this analysis, moderator variables such as age, training experience, various states of muscle catabolism, and optimal dosages of HMB are discussed. The validity of dependent measurements, clustering of data, and a conflict of interest bias will also be analyzed. A second purpose of this paper is to provide a comprehensive discussion on possible mechanisms, which HMB may operate through. Currently, the most readily discussed mechanism has been attributed to HMB as a precursor to the rate limiting enzyme to cholesterol synthesis HMG-coenzyme A reductase. However, an increase in research has been directed towards possible proteolytic pathways HMB may operate through. Evidence from cachectic cancer studies suggests that HMB may inhibit the ubiquitin-proteasome proteolytic pathway responsible for the specific degradation of intracellular proteins. HMB may also directly stimulate protein synthesis, through an mTOR dependent mechanism. Finally, special care has been taken to provide future research implications.

16.
J Sport Exerc Psychol ; 29(5): 664-72, 2007 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-18089898

RESUMO

Many of the measurements used in sport psychology research are arbitrary metrics, and researchers often cannot make the jump from scores on paper-and-pencil tests to what those scores actually mean in terms of real-world behaviors. Effect sizes for behavioral data are often interpretable, but the meaning of a small, medium, or large effect for an arbitrary metric is elusive. We reviewed all the issues in the 2005 volumes of the Journal of Sport & Exercise Psychology, The Sport Psychologist, and the Journal of Applied Sport Psychology to determine whether the arbitrary metrics used in sport psychology research were interpreted, or calibrated, against real-world variables. Of the 54 studies that used quantitative methods, 25 reported only paper-and-pencil arbitrary metrics with no connections to behavior or other real-world variables. Also, 44 of the 54 studies reported effect sizes, but only 7 studies, using both arbitrary and behavioral metrics, had calculated effect indicators and interpreted them in terms of real-world meaning.


Assuntos
Interpretação Estatística de Dados , Psicometria , Esportes/psicologia , Bibliometria , Humanos , Pesquisa
17.
J Int Soc Sports Nutr ; 3: 7-27, 2006 Jun 05.
Artigo em Inglês | MEDLINE | ID: mdl-18500966

RESUMO

In recent years an explosion of research papers concerning protein consumption has been published. The need to consolidate this information has become critical from both practical and future research standpoints. For this reason, the following paper presents an in depth analysis of contemporary issues in protein requirements and consumption for resistance trained athletes. Specifically, the paper covers: 1.) protein requirements for resistance trained athletes; 2.) the effect of the digestion rate of protein on muscular protein balance; 3.) the optimal timing of protein intake relative to exercise; 4.) the optimal pattern of protein ingestion, relative to how an individual should consume their protein throughout a 24 hour period, and what sources are utilized during this time frame; 5.) protein composition and its interaction with measures of protein balance and strength performance; 6.) the combination of protein and carbohydrates on plasma insulin levels and protein balance; 7.) the efficacy of protein supplements and whole food protein sources. Our goal is to provide the reader with practical information in optimizing protein intake as well as for provision of sound advice to their clients. Finally, special care was taken to provide future research implications.

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