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1.
J Nutr ; 149(9): 1511-1522, 2019 Sep 01.
Artigo em Inglês | MEDLINE | ID: mdl-31152658

RESUMO

BACKGROUND: Resistance exercise and dietary protein stimulate muscle protein synthesis (MPS). The rate at which proteins are digested and absorbed into circulation alters peak plasma amino acid concentrations and may modulate postexercise MPS. A novel mineral modified milk protein concentrate (mMPC), with identical amino acid composition to standard milk protein concentrate (MPC), was formulated to induce rapid aminoacidemia. OBJECTIVES: The aim of this study was to determine whether rapid aminoacidemia and greater peak essential amino acid (EAA) concentrations induced by mMPC would stimulate greater postresistance exercise MPS, anabolic signaling, and ribosome biogenesis compared to standard dairy proteins, which induce a small but sustained plasma essential aminoacidemia. METHODS: Thirty healthy young men (22.5 ± 3.0 y; BMI 23.8 ± 2.7 kg/m2) received primed constant infusions of l-[ring-13C6]-phenylalanine and completed 3 sets of leg presses and leg extensions at 80% of 1 repetition. Afterwards, participants were randomly assigned in a double-blind fashion to consume 25 g mMPC, MPC, or calcium caseinate (CAS). Vastus lateralis biopsies were collected at rest, and 2 and 4 h post exercise. RESULTS: Plasma EAA concentrations, including leucine, were 19.2-26.6% greater in the mMPC group 45-90 min post ingestion than in MPC and CAS groups (P < 0.001). Myofibrillar fractional synthetic rate from baseline to 4 h was increased by 82.6 ± 64.8%, 137.8 ± 72.1%, and 140.6 ± 52.4% in the MPC, mMPC, and CAS groups, respectively, with no difference between groups (P = 0.548). Phosphorylation of anabolic signaling targets (P70S6KThr389, P70S6KThr421/Ser424, RPS6Ser235/236, RPS6Ser240/244, P90RSKSer380, 4EBP1) were elevated by <3-fold at both 2 and 4 h post exercise in all groups (P < 0.05). CONCLUSIONS: The amplitude of plasma leucine and EAA concentrations does not modulate the anabolic response to resistance exercise after ingestion of 25 g dairy protein in young men. This trial was registered at http://www.anzctr.org.au/ as ACTRN12617000393358.

2.
Mol Nutr Food Res ; 62(7): e1701028, 2018 04.
Artigo em Inglês | MEDLINE | ID: mdl-29377592

RESUMO

Limb immobilization results in a rapid loss of muscle size and strength. The resultant alterations in signaling pathways governing myogenesis, catabolism, and mitochondrial biogenesis are likely to include posttranscriptional regulation mediated by altered microRNAs (miRNAs). Given that protein ingestion exerts an anabolic action and may act as a countermeasure to mitigate muscle loss with immobilization, it is important to examine miRNA in this context. The objective of the study is therefore to characterize the vastus lateralis miRNA response to 14 days of disuse in males (45-60 years) randomized to receive supplementation with 20 g d-1 of dairy protein (n = 12) or isocaloric carbohydrate placebo (n = 13). Biopsies are collected before and after a 2-week immobilization period. Of the 24 miRNAs previously identified in myogenic regulation, seven (miR-133a, -206, -15a, -451a, -126, -208b, and let-7e) are increased with immobilization irrespective of group; five (miR-16, -494, let-7a, -7c, and 7d) increased only in the carbohydrate group; and eight (miR-1, -486, -23a, -23b, -26a, -148b, let-7b, and -7g) are divergently expressed between groups (suppressed with protein). The ability of protein supplementation to differentially regulate miRNAs involved in key muscle regulatory pathways following short-term limb immobilization reflects potential protective function in mitigating muscle loss during limb immobilization.


Assuntos
Suplementos Nutricionais , Regulação da Expressão Gênica , MicroRNAs/metabolismo , Proteínas do Leite/uso terapêutico , Músculo Esquelético/metabolismo , Atrofia Muscular/prevenção & controle , Restrição Física/efeitos adversos , Bebidas , Biópsia por Agulha , Desjejum , Estudos de Coortes , Perfilação da Expressão Gênica , Humanos , Joelho , Extremidade Inferior , Masculino , Pessoa de Meia-Idade , Músculo Esquelético/patologia , Atrofia Muscular/etiologia , Atrofia Muscular/metabolismo , Atrofia Muscular/patologia , Músculo Quadríceps
3.
J Appl Physiol (1985) ; 124(3): 717-728, 2018 03 01.
Artigo em Inglês | MEDLINE | ID: mdl-29122965

RESUMO

Muscle disuse results in the loss of muscular strength and size, due to an imbalance between protein synthesis (MPS) and breakdown (MPB). Protein ingestion stimulates MPS, although it is not established if protein is able to attenuate muscle loss with immobilization (IM) or influence the recovery consisting of ambulatory movement followed by resistance training (RT). Thirty men (49.9 ± 0.6 yr) underwent 14 days of unilateral leg IM, 14 days of ambulatory recovery (AR), and a further six RT sessions over 14 days. Participants were randomized to consume an additional 20 g of dairy protein or placebo with a meal during the intervention. Isometric knee extension strength was reduced following IM (-24.7 ± 2.7%), partially recovered with AR (-8.6 ± 2.6%), and fully recovered after RT (-0.6 ± 3.4%), with no effect of supplementation. Thigh muscle cross-sectional area decreased with IM (-4.1 ± 0.5%), partially recovered with AR (-2.1 ± 0.5%), and increased above baseline with RT (+2.2 ± 0.5%), with no treatment effect. Myofibrillar MPS, measured using deuterated water, was unaltered by IM, with no effect of protein. During AR, MPS was increased only with protein supplementation. Protein supplementation did not attenuate the loss of muscle size and function with disuse or potentiate recovery but enhanced myofibrillar MPS during AR. NEW & NOTEWORTHY Twenty grams of daily protein supplementation does not attenuate the loss of muscle size and function induced by 2 wk of muscle disuse or potentiate recovery in middle-age men. Average mitochondrial but not myofibrillar muscle protein synthesis was attenuated during immobilization with no effect of supplementation. Protein supplementation increased myofibrillar protein synthesis during a 2-wk period of ambulatory recovery following disuse but without group differences in phenotype recovery.


Assuntos
Imobilização/efeitos adversos , Proteínas do Leite/uso terapêutico , Músculo Esquelético/efeitos dos fármacos , Atrofia Muscular/prevenção & controle , Citrato (si)-Sintase/metabolismo , Suplementos Nutricionais , Exercício , Humanos , Masculino , Pessoa de Meia-Idade , Proteínas do Leite/farmacologia , Proteínas Musculares/biossíntese , Proteínas Musculares/metabolismo , Força Muscular/efeitos dos fármacos , Músculo Esquelético/diagnóstico por imagem , Músculo Esquelético/metabolismo , Atrofia Muscular/etiologia , Proteínas Ligases SKP Culina F-Box/metabolismo
4.
J Int Soc Sports Nutr ; 14: 17, 2017.
Artigo em Inglês | MEDLINE | ID: mdl-28603468

RESUMO

BACKGROUND: Resistance training is a potent stimulus to induce muscle hypertrophy. Supplemental protein intake is known to enhance gains in muscle mass through activation of the mammalian target of rapamycin complex 1 (mTORC1) pathway, which initiates protein translation. While the optimal dose of high quality protein to promote post exercise anabolism in young or older men has been investigated, little is known about the minimum doses of protein required to potentiate the resistance exercise activation of anabolic signalling in middle aged men. METHODS: Twenty healthy men (46.3 ± 5.7 years, BMI: 23.9 ± 6.6 kg/m2) completed a single bout of unilateral resistance exercise consisting of 4 sets of leg extension and press at 80% of 1 repetition maximum. Participants were randomised to consume either formulated milk product containing 9 g milk protein (FMP) or an isoenergetic carbohydrate placebo (CHO) immediately post exercise, in a double blind fashion. A single muscle biopsy was collected at pre-exercise baseline and then bilateral biopsies were collected 90 and 240 min after beverage consumption. RESULTS: P70S6KThr389 phosphorylation was increased with exercise irrespective of group, P70S6KThr421/Ser424 was increased with exercise only in the FMP group at 240 min. Likewise, rpS6 Ser235/236 phosphorylation was increased with exercise irrespective of group, rpS6 Ser240/244 increased to a greater extent following exercise in the FMP group. mRNA expression of the amino acid transporter, LAT1/ SLC7A5 increased with both exercise and beverage consumption irrespective of group. PAT1/ SLC36A1, CAT1/ SLC7A1 and SNAT2/ SLC38A2 mRNA increased only after exercise regardless of group. CONCLUSIONS: Nine grams of milk protein is sufficient to augment some measures of downstream mTORC1 signalling after resistance exercise but does not potentiate exercise induced increases in amino acid transporter expression. Formulated products containing nine grams of milk protein would be expected stimulate muscle anabolism after resistance exercise. TRIAL REGISTRATION: New Zealand Clinical Trials Registry ACTRN12615001375549. Registered: 17 December, 2015.


Assuntos
Exercício/fisiologia , Proteínas do Leite/administração & dosagem , Treinamento de Resistência , Proteínas Quinases S6 Ribossômicas 70-kDa/metabolismo , Adulto , Sistema A de Transporte de Aminoácidos/metabolismo , Sistemas de Transporte de Aminoácidos/metabolismo , Transportador 1 de Aminoácidos Catiônicos/metabolismo , Método Duplo-Cego , Humanos , Transportador 1 de Aminoácidos Neutros Grandes/metabolismo , Masculino , Alvo Mecanístico do Complexo 1 de Rapamicina/metabolismo , Pessoa de Meia-Idade , Fosforilação , Simportadores/metabolismo
5.
Nutr Metab (Lond) ; 14: 9, 2017.
Artigo em Inglês | MEDLINE | ID: mdl-28127382

RESUMO

BACKGROUND: The milk fat globule membrane (MFGM) is primarily composed of polar phospho- and sphingolipids, which have established biological effects on neuroplasticity. The present study aimed to investigate the effect of dietary MFGM supplementation on the neuromuscular system during post-natal development. METHODS: Growing rats received dietary supplementation with bovine-derived MFGM mixtures consisting of complex milk lipids (CML), beta serum concentrate (BSC) or a complex milk lipid concentrate (CMLc) (which lacks MFGM proteins) from post-natal day 10 to day 70. RESULTS: Supplementation with MFGM mixtures enriched in polar lipids (BSC and CMLc, but not CML) increased the plasma phosphatidylcholine (PC) concentration, with no effect on plasma phosphatidylinositol (PI), phosphatidylethanolamine (PE), phosphatidylserine (PS) or sphingomyelin (SM). In contrast, muscle PC was reduced in rats receiving supplementation with both BSC and CMLc, whereas muscle PI, PE, PS and SM remained unchanged. Rats receiving BSC and CMLc (but not CML) displayed a slow-to-fast muscle fibre type profile shift (MyHCI → MyHCIIa) that was associated with elevated expression of genes involved in myogenic differentiation (myogenic regulatory factors) and relatively fast fibre type specialisation (Myh2 and Nfatc4). Expression of neuromuscular development genes, including nerve cell markers, components of the synaptogenic agrin-LRP4 pathway and acetylcholine receptor subunits, was also increased in muscle of rats supplemented with BSC and CMLc (but not CML). CONCLUSIONS: These findings demonstrate that dietary supplementation with bovine-derived MFGM mixtures enriched in polar lipids can promote neuromuscular development during post-natal growth in rats, leading to shifts in adult muscle phenotype.

6.
Nutrients ; 7(10): 8685-99, 2015 Oct 21.
Artigo em Inglês | MEDLINE | ID: mdl-26506377

RESUMO

The differential ability of various milk protein fractions to stimulate muscle protein synthesis (MPS) has been previously described, with whey protein generally considered to be superior to other fractions. However, the relative ability of a whole milk protein to stimulate MPS has not been compared to whey. Sixteen healthy middle-aged males ingested either 20 g of milk protein (n = 8) or whey protein (n = 8) while undergoing a primed constant infusion of ring (13)C6 phenylalanine. Muscle biopsies were obtained 120 min prior to consumption of the protein and 90 and 210 min afterwards. Resting myofibrillar fractional synthetic rates (FSR) were 0.019% ± 0.009% and 0.021% ± 0.018% h(-1) in the milk and whey groups respectively. For the first 90 min after protein ingestion the FSR increased (p < 0.001) to 0.057% ± 0.018% and 0.052% ± 0.024% h(-1) in the milk and whey groups respectively with no difference between groups (p = 0.810). FSR returned to baseline in both groups between 90 and 210 min after protein ingestion. Despite evidence of increased rate of digestion and leucine availability following the ingestion of whey protein, there was similar activation of MPS in middle-aged men with either 20 g of milk protein or whey protein.


Assuntos
Proteínas do Leite/farmacologia , Proteínas Musculares/metabolismo , Músculos/metabolismo , Biossíntese de Proteínas/efeitos dos fármacos , Humanos , Masculino , Pessoa de Meia-Idade , Miofibrilas/metabolismo , Proteínas do Soro do Leite/farmacologia
7.
J Nutr ; 145(2): 372-9, 2015 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-25644361

RESUMO

BACKGROUND: The FAO has recommended replacing the protein digestibility-corrected amino acid score (PDCAAS) with the digestible indispensable amino acid score (DIAAS). OBJECTIVE: The objective of this study was to compare aspects underlying the calculation of the DIAAS and PDCAAS, including 1) fecal digestibility vs. ileal digestibility, 2) using a single nitrogen digestibility value for all amino acids, and 3) the effect of truncation. Truncated PDCAAS and untruncated DIAAS values calculated as formally defined were also compared and DIAAS data presented for 14 dietary protein sources. METHODS: Semisynthetic wheat starch-based diets were formulated to contain the test protein (as consumed by humans) source (whey- and soy-protein isolates, milk-, whey-, rice- and pea- protein concentrates, cooked kidney beans, roasted peanuts, cooked peas, corn-based breakfast cereal, cooked rice, cooked rolled oats, and wheat bran) as the sole nitrogen source and with an indigestible marker (titanium dioxide). Growing male rats (∼250 g bodyweight) were given a basal casein-based diet from day 1 to day 7 and then allocated (n = 6) to the test diets for day 8 to day 14 before ileal digesta were collected after the rats were killed. Total feces were collected from day 11 to day 14. RESULTS: True fecal nitrogen digestibility was different (P < 0.05; 10% difference on average) from true ileal nitrogen digestibility for 11 of the 14 protein sources. True ileal nitrogen digestibility was different (P < 0.05) from true ileal amino acid digestibility for almost half of the indispensable and conditionally indispensable amino acids (differences ranged from 0.9% to 400%). DIAAS values ranged from 0.01 for a corn-based cereal to 1.18 for milk protein concentrate. CONCLUSION: Untruncated PDCAAS values were generally higher than a DIAAS values, especially for the poorer quality proteins; therefore, the reported differences in the scores are of potential practical importance for populations in which dietary protein intake may be marginal.


Assuntos
Aminoácidos Essenciais/administração & dosagem , Digestão/fisiologia , Aminoácidos/administração & dosagem , Aminoácidos/metabolismo , Aminoácidos Essenciais/metabolismo , Animais , Estudos Transversais , Proteínas na Dieta/administração & dosagem , Proteínas na Dieta/metabolismo , Grão Comestível/química , Fabaceae/química , Fezes/química , Análise de Alimentos , Íleo/efeitos dos fármacos , Íleo/metabolismo , Masculino , Leite/química , Nitrogênio/administração & dosagem , Nitrogênio/metabolismo , Oryza/química , Ratos , Ratos Sprague-Dawley , Triticum/química , Zea mays/química
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