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1.
J Nutr ; 154(5): 1549-1560, 2024 May.
Artigo em Inglês | MEDLINE | ID: mdl-38467279

RESUMO

BACKGROUND: Digestibility is a primary factor in determining the quality of dietary protein. Microbial protease supplementation may be a strategy for improving protein digestion and subsequent postprandial plasma amino acid availability. OBJECTIVES: To assess the effect of co-ingesting a microbial protease mixture with pea protein on postprandial plasma amino acid concentrations. DESIGN: A mixture of 3 microbial protease preparations (P3) was tested for proteolytic efficacy in an in vitro static simulation of gastrointestinal digestion. Subsequently, in a randomized, double-blind, placebo-controlled crossover trial, 24 healthy adults (27 ± 4 y; 12 females, 12 males) ingested 25 g pea protein isolate (20 g protein, 2.2 g fat) with either P3 or maltodextrin placebo (PLA). Blood samples were collected at baseline and throughout a 0‒5 h postprandial period and both the early (0-2 h) iAUC and total (0-5 h) iAUC were examined. RESULTS: Plasma glucose concentrations decreased in both conditions (P < 0.001), with higher concentrations after P3 ingestion compared with PLA (P < 0.001). Plasma insulin concentrations increased for both conditions (P < 0.001) with no difference between conditions (P = 0.331). Plasma total amino acid (TAA) concentrations increased over time (P < 0.001) with higher concentrations observed for P3 compared with PLA (P = 0.010) during the 0‒5 h period. There was a trend for elevated essential amino acid (EAA) concentrations for P3 compared with PLA (P = 0.099) during the 0‒5 h postprandial period but not for leucine (P = 0.282) or branched-chain amino acids (BCAA, P = 0.410). The early net exposure (0‒2 h iAUC) to amino acids (leucine, BCAA, EAA, and TAA) was higher for P3 compared with PLA (all, P < 0.05). CONCLUSIONS: Microbial protease co-ingestion increases plasma TAA concentrations (0-5 h) and leucine, BCAA, EAA, and TAA availability in the early postprandial period (0‒2 h) compared with ingesting pea protein with placebo in healthy adults.


Assuntos
Aminoácidos , Estudos Cross-Over , Suplementos Nutricionais , Proteínas de Ervilha , Período Pós-Prandial , Humanos , Adulto , Masculino , Feminino , Método Duplo-Cego , Aminoácidos/sangue , Aminoácidos/metabolismo , Adulto Jovem , Insulina/sangue , Glicemia/metabolismo , Peptídeo Hidrolases/sangue , Peptídeo Hidrolases/metabolismo , Digestão/efeitos dos fármacos , Pisum sativum
2.
J Appl Physiol (1985) ; 136(6): 1388-1399, 2024 Jun 01.
Artigo em Inglês | MEDLINE | ID: mdl-38385186

RESUMO

Feeding and resistance exercise stimulate myofibrillar protein synthesis (MPS) rates in healthy adults. This anabolic characterization of "healthy adults" has been namely focused on males. Therefore, the purpose of this study was to examine the temporal responses of MPS and anabolic signaling to resistance exercise alone or combined with the ingestion of protein in postmenopausal females and compare postabsorptive rates with young females. Sixteen females [60 ± 7 yr; body mass index (BMI) = 26 ± 12 kg·m-2] completed an acute bout of unilateral resistance exercise before consuming either: a fortified whey protein supplement (WHEY) or water. Participants received primed continuous infusions of L-[ring-13C6]phenylalanine with bilateral muscle biopsies before and after treatment ingestion at 2 h and 4 h in nonexercised and exercised legs. Resistance exercise transiently increased MPS above baseline at 0-2 h in the water condition (P = 0.007). Feeding after resistance exercise resulted in a late phase (2-4 h) increase in MPS in the WHEY condition (P = 0.005). In both conditions, resistance exercise did not enhance the cumulative (0-4 h) MPS response. In the nonexercised leg, MPS did not differ at 0-2 h, 2-4 h, or 0-4 h of the measurement periods (all, P > 0.05). Likewise, there were no changes in the phosphorylation of p70S6K, AMPKα, or total and phosphorylated yes-associated protein on Ser127. Finally, postabsorptive MPS was lower in premenopausal versus postmenopausal females (P = 0.023). Our results demonstrate that resistance exercise-induced changes in MPS are temporally regulated, but do not result in greater cumulative (0-4 h) MPS in postmenopausal women.NEW & NOTEWORTHY An adequate quality and quantity of skeletal muscle is relevant to support physical performance and metabolic health. Muscle protein synthesis (MPS) is an established remodeling marker, which can be hypertrophic or nonhypertrophic. Importantly, protein ingestion and resistance exercise are two strategies that support healthy muscle by stimulating MPS. Our study shows postmenopause modulates baseline MPS that may diminish the MPS response to the fundamental anabolic stimuli of protein ingestion and resistance exercise in older females.


Assuntos
Proteínas Musculares , Miofibrilas , Pós-Menopausa , Período Pós-Prandial , Treinamento Resistido , Proteínas do Soro do Leite , Humanos , Feminino , Pós-Menopausa/fisiologia , Pós-Menopausa/metabolismo , Treinamento Resistido/métodos , Pessoa de Meia-Idade , Período Pós-Prandial/fisiologia , Miofibrilas/metabolismo , Proteínas Musculares/biossíntese , Proteínas Musculares/metabolismo , Proteínas do Soro do Leite/metabolismo , Músculo Esquelético/metabolismo , Descanso/fisiologia , Idoso , Fenilalanina/metabolismo , Biossíntese de Proteínas/fisiologia , Suplementos Nutricionais , Adulto , Exercício Físico/fisiologia , Fosforilação
3.
Toxicol Sci ; 196(2): 229-237, 2023 11 28.
Artigo em Inglês | MEDLINE | ID: mdl-37632782

RESUMO

Neonicotinoid insecticides are synthetic nicotine derivatives that have high affinity for invertebrate nicotine receptors and low affinity for mammalian nicotine receptors. However, imidacloprid (IMI), the most commonly used neonicotinoid, can be bioactivated by the liver in mammals to desnitro-imidacloprid, an intermediate metabolite that effectively binds and activates mammalian receptors. However, it is not known if other tissues such as the ovaries can metabolize IMI. Thus, the present study tested the hypothesis that ovarian antral follicles metabolize and bioactivate IMI. Antral follicles were dissected from the ovaries of CD-1 mice and cultured in media containing dimethyl sulfoxide or IMI (0.2-200 µg/ml) for 48 and 96 h. Media were subjected to liquid chromatography-mass spectrometry for detection of phase I IMI metabolites. Follicles from the cultures were used for gene expression analysis of metabolic enzymes associated with IMI metabolism. All IMI metabolites were detected at 48 and 96 h. Oxidized IMI intermediates were detected in media from cultured follicles, but not environmental controls. Reduced IMI intermediates were detected in media from cultured follicles and the environmental controls. At 48 h, IMI did not affect expression of any metabolic enzymes compared with control. At 96 h, IMI induced Cyp2e1 and Cyp4f18 compared with control. These data indicate that mouse ovarian follicles metabolize IMI and that IMI induces ovarian Cyp expression over time.


Assuntos
Inseticidas , Nicotina , Feminino , Camundongos , Animais , Nicotina/farmacologia , Neonicotinoides/toxicidade , Inseticidas/toxicidade , Inseticidas/metabolismo , Nitrocompostos/toxicidade , Folículo Ovariano , Mamíferos/metabolismo
4.
J Nutr ; 153(5): 1359-1372, 2023 05.
Artigo em Inglês | MEDLINE | ID: mdl-36870539

RESUMO

BACKGROUND: Protein is most commonly consumed as whole foods as opposed to single nutrients. However, the food matrix regulation of the postprandial muscle protein synthetic response has received little attention. OBJECTIVES: The purpose of this study was to assess the effects of eating salmon (SAL) and of ingesting the same nutrients as an isolated mixture of crystalline amino acids and fish oil (ISO) on the stimulation of postexercise myofibrillar protein synthesis (MPS) and whole-body leucine oxidation rates in healthy young adults. METHODS: Ten recreationally active adults (24 ± 4 y; 5 men, 5 women) performed an acute bout of resistance exercise, followed by the ingestion of SAL or ISO in a crossover fashion. Blood, breath, and muscle biopsies were collected at rest and after exercise during primed continuous infusions of L-[ring-2H5]phenylalanine and L-[1-13C]leucine. All data are presented as means ± SD and/or mean differences (95% CIs). RESULTS: Postprandial essential amino acid (EAA) concentrations peaked earlier (P = 0.024) in the ISO group than those in the SAL group. Postprandial leucine oxidation rates increased over time (P < 0.001) and peaked earlier in the ISO group (1.239 ± 0.321 nmol/kg/min; 63 ± 25 min) than those in the SAL group (1.230 ± 0.561 nmol/kg/min; 105 ± 20 min; P = 0.003). MPS rates for SAL (0.056 ± 0.022 %/h; P = 0.001) and ISO (0.046 ± 0.025 %/h; P = 0.025) were greater than the basal rates (0.020 ± 0.011 %/h) during the 0- to 5-h recovery period, with no differences between conditions (P = 0.308). CONCLUSION: We showed that the postexercise ingestion of SAL or ISO stimulate postexercise MPS rates with no differences between the conditions. Thus, our results indicate that ingesting protein from SAL as a whole-food matrix is similarly anabolic to ISO in healthy young adults. This trial was registered at www. CLINICALTRIALS: gov as NCT03870165.


Assuntos
Proteínas Alimentares , Salmão , Animais , Feminino , Proteínas Alimentares/metabolismo , Ingestão de Alimentos , Leucina/farmacologia , Músculo Esquelético , Nutrientes , Período Pós-Prandial , Salmão/metabolismo
5.
Int J Sport Nutr Exerc Metab ; 32(6): 446-452, 2022 Nov 01.
Artigo em Inglês | MEDLINE | ID: mdl-36007881

RESUMO

Creatine (Cr) supplementation is a well-established strategy to enhance gains in strength, lean body mass, and power from a period of resistance training. However, the effectiveness of creatyl-L-leucine (CLL), a purported Cr amide, is unknown. Therefore, the purpose of this study was to assess the effects of CLL on muscle Cr content. Twenty-nine healthy men (n = 17) and women (n = 12) consumed 5 g/day of either Cr monohydrate (n = 8; 28.5 ± 7.3 years, 172.1 ± 11.0 cm, 76.6 ± 10.7 kg), CLL (n = 11; 29.2 ± 9.3 years, 170.3 ± 10.5 cm, 71.9 ± 14.5 kg), or placebo (n = 10; 30.3 ± 6.9 years, 167.8 ± 9.9 cm, 69.9 ± 11.1 kg) for 14 days in a randomized, double-blind design. Participants completed three bouts of supervised resistance exercise per week. Muscle biopsies were collected before and after the intervention for quantification of muscle Cr. Cr monohydrate supplementation which significantly increased muscle Cr content with 14 days of supplementation. No changes in muscle Cr were observed for the placebo or CLL groups. Cr monohydrate supplementation is an effective strategy to augment muscle Cr content while CLL is not.


Assuntos
Creatina , Leucemia Linfocítica Crônica de Células B , Masculino , Adulto Jovem , Feminino , Humanos , Leucina/metabolismo , Leucemia Linfocítica Crônica de Células B/metabolismo , Músculo Esquelético/fisiologia , Suplementos Nutricionais , Composição Corporal/fisiologia , Método Duplo-Cego , Amidas/metabolismo , Amidas/farmacologia , Força Muscular
6.
J Vet Diagn Invest ; 34(4): 622-630, 2022 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-35658640

RESUMO

Spontaneous hypercortisolism (HC) is a common endocrine disease of senior dogs, often overlapping in selected clinical signs and hematologic and blood biochemical abnormalities with nonadrenal diseases (NADs). HC and NAD could differentially affect cortisol metabolism, which is a complex 10-enzymatic pathway process. HC might also affect blood and urine lactate levels through its effects on mitochondrial function. We aimed to differentiate between HC and NAD via a urinary cortisol metabolites and lactate panel. We prospectively recruited 7 healthy dogs and 18 dogs with HC, 15 with congestive heart failure (CHF), and 9 with NAD. We analyzed urine by gas chromatography-mass spectrometry and liquid chromatography-mass spectrometry. We normalized urinary lactate and cortisol metabolites to urine creatinine concentration, and then compared groups using a linear-mixed model and principal component (PC) analysis. A machine-learning classification algorithm generated a decision tree (DT) model for predicting HC. The least-squares means of normalized urinary 6ß-hydroxycortisol and PC1 of the HC and CHF groups were higher than those of the healthy and NAD groups (p = 0.05). Creatinine-normalized urinary 6ß-hydroxycortisol had better sensitivity (Se, 0.78; 95% CI: 0.55-0.91), specificity (Sp, 0.89; 95% CI: 0.57-0.99), and a likelihood ratio (LR; 7), than the Se (0.72; 95% CI: 0.49-0.88), Sp (0.89; 95% CI: 0.57-0.99), and LR (6.5) of PC1 for distinguishing HC from NAD. Lactate and dihydrocortisone had the highest decreasing node-weighted impurity value and were considered the most important features in the DT model; dihydrocortisol had no role in determining whether a dog had HC.


Assuntos
Síndrome de Cushing , Doenças do Cão , Insuficiência Cardíaca , Animais , Creatinina/urina , Síndrome de Cushing/veterinária , Cães , Insuficiência Cardíaca/veterinária , Hidrocortisona/urina , Ácido Láctico , NAD
7.
J Vet Pharmacol Ther ; 45(1): 107-116, 2022 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-34494277

RESUMO

This study aimed to evaluate pharmacokinetic profiles of morphine in goats following a single dose administered intravenously, intramuscularly, or subcutaneously at 0.1 mg/kg, 0.25 mg/kg, and 0.4 mg/kg. Study population included eight healthy adult goats in a randomized cross-over study. Serial plasma samples were collected and morphine was quantified using high-performance liquid chromatography/mass spectrometry. Data fit a two-compartment model following intravenous administration and a non-compartmental model following both intramuscular and subcutaneous administration. Plasma elimination half-life was 2.88 ± 1.13 h (0.1 mg/kg), 2.30 ± 0.49 h (0.25 mg/kg), and 2.67 ± 0.82 h (0.4 mg/kg) following IV morphine. Intramuscular Cmax values were 13.4 ± 2.77 ng/ml (0.1 mg/kg), 34 ± 11.50 ng/ml (0.25 mg/kg), and 68.9 ± 24.5 ng/ml (0.4 mg/kg). Intramuscular Tmax f(h) or IM dosing (in hrs) was 0.19 ± 0.14 (0.1 mg/kg), 0.24 ± 0.24 (0.25 mg/kg), and 0.21 ± 0.24 (0.4 mg/kg). Subcutaneous Cmax values were 9.88 ± 3.31 ng/ml (0.1 mg/kg), 28.5 ± 11.6 ng/ml (0.25 mg/kg), and 39.4 ± 14.3 ng/ml (0.4 mg/kg). Subcutaneous Tmax (h) values for SC dosing were 0.36 ± 0.21 (0.1 mg/kg), 0.31 ± 0.17 (0.25 mg/kg), and 0.4 ± 0.13 (0.4 mg/kg). Intramuscular bioavailability values were 153.77 ± 12.60% (0.4 mg/kg), 104.8 ± 25.12% (0.25 mg/kg), and 100.7 ± 29.57% (0.1 mg/kg). Subcutaneous bioavailability values were 130.58 ± 19.07% (0.4 mg/kg), 116.6 ± 27.03% (0.25 mg/kg), and 111.6 ± 23.24% (0.1 mg/kg). No adverse effects were observed. Assuming plasma concentration required to induce analgesia is 16 ± 9 ng/ml in goats, as demonstrated in humans, it is suggested to administer morphine intramuscularly at 0.4 mg/kg every 3-4 h or SC every 2-3 h. This is a speculative conclusion therefore further studies evaluating pharmacodynamics and plasma analgesic threshold in goats is recommended.


Assuntos
Analgesia , Morfina , Animais , Administração Intravenosa/veterinária , Analgesia/veterinária , Área Sob a Curva , Disponibilidade Biológica , Estudos Cross-Over , Cabras , Meia-Vida , Injeções Intramusculares/veterinária
8.
PLoS One ; 16(10): e0258150, 2021.
Artigo em Inglês | MEDLINE | ID: mdl-34618833

RESUMO

Bigheaded Carp have spread throughout the Mississippi River basin since the 1970s. Little has stopped the spread as carp have the ability to pass through locks and dams, and they are currently approaching the Great Lakes. However, the location of the leading edge in the Illinois River has stalled for over a decade, even though there is no barrier preventing further advancement towards the Great Lakes. Defining why carp are not moving towards the Great Lakes is important for predicting why they might advance in the future. The aim of this study was to test the hypothesis that anthropogenic contaminants in the Illinois River may be playing a role in preventing further upstream movement of Bigheaded Carp. Ninety three livers were collected from carp at several locations between May and October of 2018. Liver samples were analyzed using gas chromatography-mass spectrometry in a targeted metabolite profiling approach. Livers from carp at the leading edge had differences in energy use and metabolism, and suppression of protective mechanisms relative to downstream fish; differences were consistent across time. This body of work provides evidence that water quality is linked to carp movement in the Illinois River. As water quality in this region continues to improve, consideration of this impact on carp spread is essential to protect the Great Lakes.


Assuntos
Migração Animal/fisiologia , Carpas/metabolismo , Ecossistema , Metabolômica , Animais , Carpas/fisiologia , Monitoramento Ambiental/métodos , Humanos , Illinois , Espécies Introduzidas , Lagos , Mississippi , Rios , Alimentos Marinhos
9.
Front Mol Biosci ; 8: 660764, 2021.
Artigo em Inglês | MEDLINE | ID: mdl-34336923

RESUMO

Weaning wields environmental, social, and nutritional stresses that are detectable in the blood metabolite levels of the offspring. Prenatal stress in the form of maternal immune activation (MIA) in response to infection, which is associated with health and behavior disorders, also elicits prolonged changes in blood and brain cytokine and metabolite levels of the offspring. The goal of this study was to investigate the effects of weaning and MIA on the offspring's liver function to advance the understanding of the impact of stressors on peripheral and central nervous systems, physiology, and health. Gas chromatography-mass spectrometry analysis was used to compare the level of hepatic metabolites from 22-day-old pigs (n = 48) evenly distributed among weaning (nursed or weaned), viral MIA exposure (yes or no), and sexes. Weaning effects were detected on 38 metabolites at p-value < 0.05 (28 metabolites at FDR p-value < 0.05), and sex-dependent MIA effects were detected on 11 metabolites. Multiple intermediate and final products of the enriched (FDR p-value < 0.05) glycolysis and gluconeogenesis and pentose phosphate pathways were over-abundant in nursed relative to weaned pigs. The enriched pathways confirm the impact of weaning on hepatic metabolic shift, oxidative stress, and inflammation. Higher levels of the glucogenic amino acid histidine are observed in pigs exposed to MIA relative to controls, suggesting that the role of this metabolite in modulating inflammation may supersede the role of this amino acid as an energy source. The lower levels of cholesterol detected in MIA pigs are consistent with hypocholesterolemia profiles detected in individuals with MIA-related behavior disorders. Our findings underline the impact of weaning and MIA stressors on hepatic metabolites that can influence peripheral and central nervous system metabolic products associated with health and behavior disorders.

10.
J Physiol ; 599(18): 4287-4307, 2021 09.
Artigo em Inglês | MEDLINE | ID: mdl-34320223

RESUMO

KEY POINTS: The ingestion of protein potentiates the stimulation of myofibrillar protein synthesis rates after an acute bout of resistance exercise. Protein supplementation (eating above the protein Recommended Dietary Allowance) during resistance training has been shown to maximize lean mass and strength gains in healthy young and older adults. Here, contractile, oxidative, and structural protein synthesis were assessed in skeletal muscle in response to a moderate or higher protein diet during the early adaptive phase of resistance training in middle-aged adults. The stimulation of myofibrillar, mitochondrial or collagen protein synthesis rates during 0-3 weeks of resistance training is not further enhanced by a higher protein diet. These results show that moderate protein diets are sufficient to support the skeletal muscle adaptive response during the early phase of a resistance training programme. ABSTRACT: Protein ingestion augments muscle protein synthesis (MPS) rates acutely after resistance exercise and can offset age-related loss in muscle mass. Skeletal muscle contains a variety of protein pools, such as myofibrillar (contractile), mitochondrial (substrate oxidation), and collagen (structural support) proteins, and the sensitivity to nutrition and exercise seems to be dependent on the major protein fraction studied. However, it is unknown how free-living conditions with high dietary protein density and habitual resistance exercise mediates muscle protein subfraction synthesis. Therefore, we investigated the effect of moderate (MOD: 1.06 ± 0.22 g kg-1  day-1 ) or high (HIGH: 1.55 ± 0.25 g kg-1  day-1 ) protein intake on daily MPS rates within the myofibrillar (MyoPS), mitochondrial (MitoPS) and collagen (CPS) protein fractions in middle-aged men and women (n = 20, 47 ± 1 years, BMI 28 ± 1 kg m-2 ) during the early phase (0-3 weeks) of a dietary counselling-controlled resistance training programme. Participants were loaded with deuterated water, followed by daily maintenance doses throughout the intervention. Muscle biopsies were collected at baseline and after weeks 1, 2 and 3. MyoPS in the HIGH condition remained constant (P = 1.000), but MOD decreased over time (P = 0.023). MitoPS decreased after 0-3 weeks when compared to 0-1 week (P = 0.010) with no effects of protein intake (P = 0.827). A similar decline with no difference between groups (P = 0.323) was also observed for CPS (P = 0.007). Our results demonstrated that additional protein intake above moderate amounts does not potentiate the stimulation of longer-term MPS responses during the early stage of resistance training adaptations in middle-aged adults.


Assuntos
Treinamento Resistido , Idoso , Proteínas Alimentares , Exercício Físico , Feminino , Humanos , Masculino , Pessoa de Meia-Idade , Proteínas Musculares , Músculo Esquelético
11.
J Appl Physiol (1985) ; 131(3): 1111-1122, 2021 09 01.
Artigo em Inglês | MEDLINE | ID: mdl-34323596

RESUMO

Leucine is regarded as an anabolic trigger for the mTORC1 pathway and the stimulation muscle protein synthesis rates. More recently, there has been an interest in underpinning the relevance of branched-chain amino acid (BCAA)-containing dipeptides and their intact absorption into circulation to regulate muscle anabolic responses. We investigated the effects of dileucine and leucine ingestion on postprandial muscle protein turnover. Ten healthy young men (age: 23 ± 3 yr) consumed either 2 g of leucine (LEU) or 2 g of dileucine (DILEU) in a randomized crossover design. The participants underwent repeated blood and muscle biopsy sampling during primed continuous infusions of l-[ring-13C6]phenylalanine and l-[15N]phenylalanine to determine myofibrillar protein synthesis (MPS) and mixed muscle protein breakdown rates (MPB), respectively. LEU and DILEU similarly increased plasma leucine net area under the curve (AUC; P = 0.396). DILEU increased plasma dileucine AUC to a greater extent than LEU (P = 0.013). Phosphorylation of Akt (P = 0.002), rpS6 (P < 0.001), and p70S6K (P < 0.001) increased over time under both LEU and DILEU conditions. Phosphorylation of 4E-BP1 (P = 0.229) and eEF2 (P = 0.999) did not change over time irrespective of condition. Cumulative (0-180 min) MPS increased in DILEU (0.075 ± 0.032%·h-1), but not in LEU (0.047 ± 0.029%·h-1; P = 0.023). MPB did not differ between LEU (0.043 ± 0.030%·h-1) and DILEU conditions (0.051 ± 0.027%·h-1; P = 0.659). Our results showed that dileucine ingestion elevated plasma dileucine concentrations and muscle protein turnover by stimulating MPS in young men.NEW & NOTEWORTHY The role of dipeptides as anabolic agents remains unresolved in humans. We show that the ingestion of 2 g dileucine increased plasma dileucine concentrations and resulted in an enhancement of muscle protein turnover by stimulating an increase in muscle protein synthesis rates in healthy young males. The ingestion of 2 g leucine, however, did not stimulate an increase in muscle protein turnover. Our work provides the first insights into the effects of dipeptides on human protein metabolism.


Assuntos
Proteínas Musculares , Músculo Esquelético , Adulto , Ingestão de Alimentos , Humanos , Leucina , Masculino , Período Pós-Prandial , Adulto Jovem
12.
Sci Rep ; 10(1): 3420, 2020 02 25.
Artigo em Inglês | MEDLINE | ID: mdl-32098988

RESUMO

Chlamydia trachomatis (CT) and Mycoplasma genitalium (MG) are two highly prevalent bacterial sexually transmitted infections (STIs) with a significant rate of co-infection in some populations. Vaginal metabolites are influenced by resident vaginal microbiota, affect susceptibility to sexually transmitted infections (STIs), and may impact local inflammation and patient symptoms. Examining the vaginal metabolome in the context of CT mono (CT+) and CT/MG co-infection (CT+/MG+) may identify biomarkers for infection or provide new insights into disease etiology and pathogenesis. Yet, the vaginal metabolome in the setting of CT infection is understudied and the composition of the vaginal metabolome in CT/MG co-infected women is unknown. Therefore, in this analysis, we used an untargeted metabolomic approach combined with 16S rRNA gene amplicon sequencing to characterize the vaginal microbiota and metabolomes of CT+, CT+/MG+, and uninfected women. We found that CT+ and CT+/MG+ women had distinct vaginal metabolomic profiles as compared to uninfected women both before and after adjustment for the vaginal microbiota. This study provides important foundational data documenting differences in the vaginal metabolome between CT+, CT+/MG+ and uninfected women. These data may guide future mechanistic studies that seek to provide insight into the pathogenesis of CT and CT/MG infections.


Assuntos
Chlamydia trachomatis/metabolismo , Linfogranuloma Venéreo/metabolismo , Metaboloma , Infecções por Mycoplasma/metabolismo , Mycoplasma genitalium/metabolismo , Vagina/metabolismo , Vaginose Bacteriana/metabolismo , Adulto , Feminino , Humanos , Linfogranuloma Venéreo/patologia , Infecções por Mycoplasma/patologia , Vagina/microbiologia , Vaginose Bacteriana/microbiologia , Vaginose Bacteriana/patologia
13.
Metabolism ; 102: 153996, 2020 01.
Artigo em Inglês | MEDLINE | ID: mdl-31678069

RESUMO

BACKGROUND: We have recently shown that a novel signalling kinase, inositol hexakisphosphate kinase 1 (IP6K1), is implicated in whole-body insulin resistance via its inhibitory action on Akt. Insulin and insulin like growth factor 1 (IGF-1) share many intracellular processes with both known to play a key role in glucose and protein metabolism in skeletal muscle. AIMS: We aimed to compare IGF/IP6K1/Akt signalling and the plasma proteomic signature in individuals with a range of BMIs after ingestion of lean meat. METHODS: Ten lean [Body mass index (BMI) (in kg/m2): 22.7 ±â€¯0.4; Homeostatic model assessment of insulin resistance (HOMAIR): 1.36 ±â€¯0.17], 10 overweight (BMI: 27.1 ±â€¯0.5; HOMAIR: 1.25 ±â€¯0.11), and 10 obese (BMI: 35.9 ±â€¯1.3; HOMAIR: 5.82 ±â€¯0.81) adults received primed continuous L-[ring-13C6]phenylalanine infusions. Blood and muscle biopsy samples were collected at 0 min (post-absorptive), 120 min and 300 min relative to the ingestion of 170 g pork loin (36 g protein and 5 g fat) to examine skeletal muscle protein signalling, plasma proteomic signatures, and whole-body phenylalanine disappearance rates (Rd). RESULTS: Phenylalanine Rd was not different in obese compared to lean individuals at all time points and was not responsive to a pork ingestion (basal, P = 0.056; 120 & 300 min, P > 0.05). IP6K1 was elevated in obese individuals at 120 min post-prandial vs basal (P < 0.05). There were no acute differences plasma proteomic profiles between groups in the post-prandial state (P > 0.05). CONCLUSIONS: These data demonstrate, for the first time that muscle IP6K1 protein content is elevated after lean meat ingestion in obese adults, suggesting that IP6K1 may be contributing to the dysregulation of nutrient uptake in skeletal muscle. In addition, proteomic analysis showed no differences in proteomic signatures between obese, overweight or lean individuals.


Assuntos
Proteínas Sanguíneas/metabolismo , Ingestão de Alimentos/fisiologia , Carne , Músculo Esquelético/metabolismo , Obesidade/metabolismo , Fosfotransferases (Aceptor do Grupo Fosfato)/metabolismo , Proteoma/metabolismo , Adulto , Fatores Etários , Proteínas Sanguíneas/análise , Índice de Massa Corporal , Gorduras na Dieta/farmacologia , Metabolismo Energético/fisiologia , Feminino , Glucose/metabolismo , Humanos , Resistência à Insulina/fisiologia , Masculino , Pessoa de Meia-Idade , Proteínas Musculares/análise , Proteínas Musculares/metabolismo , Músculo Esquelético/efeitos dos fármacos , Músculo Esquelético/patologia , Obesidade/sangue , Obesidade/patologia , Fosfotransferases (Aceptor do Grupo Fosfato)/análise , Período Pós-Prandial/fisiologia , Proteoma/análise , Magreza/sangue , Magreza/metabolismo , Magreza/patologia , Adulto Jovem
14.
Med Sci Sports Exerc ; 52(5): 1022-1030, 2020 05.
Artigo em Inglês | MEDLINE | ID: mdl-31703023

RESUMO

During a traditional set configuration of resistance exercise (TRD), characterized by a continuous completion of repetitions, a decrease in power output tends to occur throughout a set of repetitions. Inclusion of intraset rest, otherwise known as a cluster set configuration (CLU), counteracts this power decline. However, the effect of a CLU configuration on postexercise myofibrillar protein synthesis rates (MPS) and anabolic signaling has not been investigated. PURPOSE: We aimed to determine if any mechanistic differences exist between TRD and CLU signaling events associated with muscle anabolism. METHODS: In randomized crossover trials, eight resistance-trained participants (23 ± 1 yr, 81 ± 4.7 kg, body fat: 18% ± 1.9%; 1 repetition maximum [1RM], 150 ± 9.1 kg) performed an acute bout of CLU (4 sets × (2 × 5) repetitions, 30-s intraset rest, 90-s interset rest) and TRD (4 sets × 10 repetitions, 120-s interset rest) barbell back squats at approximately 70% 1RM with total volume load equated during primed continuous L-[ring-C6]phenylalanine infusions. Blood and muscle biopsy samples were collected at rest and after exercise at 0, 2, and 5 h. RESULTS: There was no difference in postexercise MPS between the CLU and TRD condition (P > 0.05) and no changes in phosphorylation of mTORC1 downstream targets (p70S6K and 4EBP1). Total and phosphorylated yes-associated protein on Ser127 transiently increased (P < 0.01) immediately after exercise (t = 0) in CLU (~2.1-fold) and TRD condition (~2.2-fold). CONCLUSIONS: Our results show that CLU is a viable anabolic option by preserving power output with similar MPS stimulation when compared with the TRD condition in trained young adults.


Assuntos
Proteínas Musculares/biossíntese , Miofibrilas/metabolismo , Treinamento Resistido/métodos , Descanso , Proteínas Adaptadoras de Transdução de Sinal/biossíntese , Aminoácidos/sangue , Glicemia/metabolismo , Estudos Cross-Over , Feminino , Humanos , Insulina/sangue , Ácido Láctico/sangue , Sistema de Sinalização das MAP Quinases , Masculino , Alvo Mecanístico do Complexo 1 de Rapamicina/biossíntese , Percepção/fisiologia , Fosforilação , Esforço Físico/fisiologia , Fatores de Transcrição/biossíntese , Proteínas de Sinalização YAP , Adulto Jovem
15.
J Appl Physiol (1985) ; 127(6): 1651-1659, 2019 12 01.
Artigo em Inglês | MEDLINE | ID: mdl-31622159

RESUMO

Carbohydrate (CHO) ingestion is an established strategy to improve endurance performance. Race fuels should not only sustain performance but also be readily digested and absorbed. Potatoes are a whole-food-based option that fulfills these criteria, yet their impact on performance remains unexamined. We investigated the effects of potato purée ingestion during prolonged cycling on subsequent performance vs. commercial CHO gel or a water-only condition. Twelve cyclists (70.7 ± 7.7 kg, 173 ± 8 cm, 31 ± 9 yr, 22 ± 5.1% body fat; means ± SD) with average peak oxygen consumption (V̇o2peak) of 60.7 ± 9.0 mL·kg-1·min-1 performed a 2-h cycling challenge (60-85% V̇o2peak) followed by a time trial (TT; 6 kJ/kg body mass) while consuming potato, gel, or water in a randomized-crossover design. The race fuels were administered with [U-13C6]glucose for an indirect estimate of gastric emptying rate. Blood samples were collected throughout the trials. Blood glucose concentrations were higher (P < 0.001) in potato and gel conditions compared with water condition. Blood lactate concentrations were higher (P = 0.001) after the TT completion in both CHO conditions compared with water condition. TT performance was improved (P = 0.032) in both potato (33.0 ± 4.5 min) and gel (33.0 ± 4.2 min) conditions compared with water condition (39.5 ± 7.9 min). Moreover, no difference was observed in TT performance between CHO conditions (P = 1.00). In conclusion, potato and gel ingestion equally sustained blood glucose concentrations and TT performance. Our results support the effective use of potatoes to support race performance for trained cyclists.NEW & NOTEWORTHY The ingestion of concentrated carbohydrate gels during prolonged exercise has been shown to promote carbohydrate availability and improve exercise performance. Our study aim was to expand and diversify race fueling menus for athletes by providing an evidence-based whole-food alternative to the routine ingestion of gels during training and competition. Our work shows that russet potato ingestion during prolonged cycling is as effective as carbohydrate gels to support exercise performance in trained athletes.


Assuntos
Desempenho Atlético/fisiologia , Ciclismo/fisiologia , Carboidratos da Dieta/administração & dosagem , Solanum tuberosum , Adulto , Glicemia , Digestão , Feminino , Humanos , Masculino , Esforço Físico , Adulto Jovem
16.
Food Microbiol ; 82: 46-52, 2019 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-31027806

RESUMO

Although Staphylococcus aureus is a major cause of food poisoning, little is known about its response to growth on food. Utilizing a transcriptional profiling and metabolomics approach, we compared S. aureus grown on autoclaved chicken breast (ACB) to Luria broth agar. ACB cultures demonstrated increased expression of genes associated with protein synthesis, cofactors, secondary metabolites, nitrogen and nucleotide metabolism, amino acid transport, and reduced expression of general stress, lipid metabolism, and virulence genes. The ACB culture also displayed characteristics of catabolite de-repression and anaerobic growth, and increased expression of arginine biosynthesis genes (argFGH) and an arginine/ornithine antiporter gene (arcD). S. aureus synthesizes arginine from proline and the ACB culture exhibited increased expression of proline transport genes (opuBA, opuBB and putP) and increased proline accumulation. Amino acid and sugar content in the ACB grown culture increased, and this was attributed to the consumption of ACB, transport of amino acids, and gluconeogenesis. Genes involved with biotin biosynthesis and uptake were upregulated and biotin is required for amino acid catabolism. Genes encoding urease and urease activity were upregulated in ACB cultures, while urea levels were reduced. This research provides fundamental information on the response of S. aureus growing on chicken meat that could find application in future attempts to reduce the growth of S. aureus in food.


Assuntos
Proteínas de Bactérias/genética , Perfilação da Expressão Gênica , Temperatura Alta , Metabolômica , Produtos Avícolas/microbiologia , Staphylococcus aureus/genética , Aminoácidos/química , Anaerobiose , Animais , Arginina/química , Biotina/biossíntese , Repressão Catabólica , Galinhas , Gluconeogênese/genética , Staphylococcus aureus/crescimento & desenvolvimento , Urease/metabolismo , Virulência
17.
Kidney Int Rep ; 3(6): 1403-1415, 2018 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-30450467

RESUMO

INTRODUCTION: Skeletal muscle loss is common in patients with renal failure who receive maintenance hemodialysis (MHD) therapy. Regular ingestion of protein-rich meals are recommended to help offset muscle protein loss in MHD patients, but little is known about the anabolic potential of this strategy. METHODS: Eight MHD patients (age: 56 ± 5 years; body mass index [BMI]: 32 ± 2 kg/m2) and 8 nonuremic control subjects (age: 50 ± 2 years: BMI: 31 ± 1 kg/m2) received primed continuous L-[ring-2H5]phenylalanine and L-[1-13C]leucine infusions with blood and muscle biopsy sampling on a nondialysis day. Participants consumed a mixed meal (546 kcal; 20-g protein, 59-g carbohydrates, 26-g fat) with protein provided as L-[5,5,5-2H3]leucine-labeled eggs. RESULTS: Circulating dietary amino acid availability was reduced in MHD patients (41 ± 5%) versus control subjects (61 ± 4%; P = 0.03). Basal muscle caspase-3 protein content was elevated (P = 0.03) and large neutral amino acid transporter 1 (LAT1) protein content was reduced (P = 0.02) in MHD patients versus control subjects. Basal muscle protein synthesis (MPS) was ∼2-fold higher in MHD patients (0.030 ± 0.005%/h) versus control subjects (0.014 ± 0.003%/h) (P = 0.01). Meal ingestion failed to increase MPS in MHD patients (absolute change from basal: 0.0003 ± 0.007%/h), but stimulated MPS in control subjects (0.009 ± 0.002%/h; P = 0.004). CONCLUSIONS: MHD patients demonstrated muscle anabolic resistance to meal ingestion. This blunted postprandial MPS response in MHD patients might be related to high basal MPS, which results in a stimulatory ceiling effect and/or reduced plasma dietary amino acid availability after mixed-meal ingestion.

18.
J Physiol ; 596(21): 5119-5133, 2018 11.
Artigo em Inglês | MEDLINE | ID: mdl-30113718

RESUMO

KEY POINTS: Lifestyle modifications that include the regular performance of exercise are probably important for counteracting the negative consequences of obesity on postprandial myofibrillar protein synthetic responses to protein dense food ingestion. We show that the interactive effect of resistance exercise and feeding on the stimulation of myofibrillar protein synthesis rates is diminished with obesity compared to normal weight adults. The blunted myofibrillar protein synthetic response with resistance exercise in people with obesity may be underpinned by alterations in muscle anabolic signalling phosphorylation (p70S6K and 4E-BP1). The results obtained in the present study suggest that further exercise prescription manipulation may be necessary to optimize post-exercise myofibrillar protein synthesis rates in adults with obesity. ABSTRACT: We aimed to determine whether obesity alters muscle anabolic and inflammatory signalling phosphorylation and also muscle protein synthesis within the myofibrillar (MYO) and sarcoplasmic (SARC) protein fractions after resistance exercise. Nine normal weight (NW) (21 ± 1 years, body mass index 22 ± 1 kg m-2 ) and nine obese (OB) (22 ± 1 years, body mass index 36 ± 2 kg m-2 ) adults received l-[ring-13 C6 ]phenylalanine infusions with blood and muscle sampling at basal and fed-state of the exercise (EX) and non-exercise (CON) legs. Participants performed unilateral leg extensions and consumed pork (36 g of protein) immediately after exercise. Basal muscle Toll-like receptor 4 (TLR4) protein was similar between OB and NW groups (P > 0.05) but increased at 300 min after pork ingestion only in the OB group (P = 0.03). Resistance exercise reduced TLR4 protein in the OB group at 300 min (EX vs. CON leg in OB: P = 0.04). Pork ingestion increased p70S6K phosphorylation at 300 min in CON and EX of the OB and NW groups (P > 0.05), although the response was lower in the EX leg of OB vs. NW at 300 min (P = 0.05). Basal MYO was similar between the NW and OB groups (P > 0.05) and was stimulated by pork ingestion in the EX and CON legs in both groups (Δ from basal NW: CON 0.04 ± 0.01% h-1 ; EX 0.10 ± 0.02% h-1 ; OB: CON 0.06 ± 0.01% h-1 ; EX 0.06 ± 0.01% h-1 ; P < 0.05). MYO was more strongly stimulated in the EX vs. CON legs in NW (P = 0.02) but not OB (P = 0.26). SARC was feeding sensitive but not further potentiated by resistance exercise in both groups. Our results suggest that obesity may attenuate the effectiveness of resistance exercise to augment fed-state MYO.


Assuntos
Ingestão de Alimentos , Miofibrilas/metabolismo , Obesidade/metabolismo , Treinamento Resistido , Transdução de Sinais , Proteínas Adaptadoras de Transdução de Sinal/genética , Proteínas Adaptadoras de Transdução de Sinal/metabolismo , Proteínas de Ciclo Celular , Feminino , Humanos , Masculino , Obesidade/fisiopatologia , Fosfoproteínas/genética , Fosfoproteínas/metabolismo , Proteínas Quinases S6 Ribossômicas 70-kDa/genética , Proteínas Quinases S6 Ribossômicas 70-kDa/metabolismo , Receptor 4 Toll-Like/genética , Receptor 4 Toll-Like/metabolismo , Adulto Jovem
19.
Ultrason Sonochem ; 40(Pt A): 791-797, 2018 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-28946487

RESUMO

Red rice (Oryza sativa L.) that has a red (reddish brown) bran layer in de-hulled rice is known to contain rich biofunctional components. Germination is an effective technique to improve the nutritional quality, digestibility, and flavor of de-hulled rice. Ultrasonication, a form of physical stimulation, has been documented as a novel approach to improve the nutritional quality of plant-based food. This study was undertaken to test the use of ultrasound to enhance the nutritional value of red rice. Ultrasonication (5min, 16W/L) was applied to rice during soaking or after 66h germination. Changes of metabolites (amino acids, sugars, and organic acids) in red rice treated by ultrasonication were determined using a GC/MS plant primary metabolomics analysis platform. Differential expressed metabolites were identified through multivariate statistical analysis. Results showed that γ-aminobutyric acid (GABA) and riboflavin (vitamin B2) in red rice significantly increased after germination for 72h, and then experienced a further increase after treatment by ultrasound at different stages during germination. The metabolomics analysis showed that some plant metabolites, i.e. GABA, O-phosphoethanolamine, and glucose-6-phosphate were significantly increased after the ultrasonic treatment (VIP>1.5) in comparison with the untreated germinated rice. The findings of this study showed that controlled germination with ultrasonic stress is an effective method to enhance GABA and other health-promoted components in de-hulled rice.


Assuntos
Germinação , Saúde , Oryza/metabolismo , Sonicação , Ácido gama-Aminobutírico/metabolismo , Qualidade dos Alimentos , Riboflavina/metabolismo , Sementes/metabolismo
20.
Am J Clin Nutr ; 106(6): 1401-1412, 2017 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-28978542

RESUMO

Background: Protein in the diet is commonly ingested from whole foods that contain various macro- and micronutrients. However, the effect of consuming protein within its natural whole-food matrix on postprandial protein metabolism remains understudied in humans.Objective: We aimed to compare the whole-body and muscle protein metabolic responses after the consumption of whole eggs with egg whites during exercise recovery in young men.Design: In crossover trials, 10 resistance-trained men [aged 21 ± 1 y; 88 ± 3 kg; body fat: 16% ± 1% (means ± SEMs)] received primed continuous l-[ring-2H5]phenylalanine and l-[1-13C]leucine infusions and performed a single bout of resistance exercise. After exercise, participants consumed intrinsically l-[5,5,5-2H3]leucine-labeled whole eggs (18 g protein, 17 g fat) or egg whites (18 g protein, 0 g fat). Repeated blood and muscle biopsy samples were collected to assess whole-body leucine kinetics, intramuscular signaling, and myofibrillar protein synthesis.Results: Plasma appearance rates of protein-derived leucine were more rapid after the consumption of egg whites than after whole eggs (P = 0.01). Total plasma availability of leucine over the 300-min postprandial period was similar (P= 0.75) between the ingestion of whole eggs (68% ± 1%) and egg whites (66% ± 2%), with no difference in whole-body net leucine balance (P = 0.27). Both whole-egg and egg white conditions increased the phosphorylation of mammalian target of rapamycin complex 1, ribosomal protein S6 kinase 1, and eukaryotic translation initiation factor 4E-binding protein 1 during postexercise recovery (all P < 0.05). However, whole-egg ingestion increased the postexercise myofibrillar protein synthetic response to a greater extent than did the ingestion of egg whites (P= 0.04).Conclusions: We show that the ingestion of whole eggs immediately after resistance exercise resulted in greater stimulation of myofibrillar protein synthesis than did the ingestion of egg whites, despite being matched for protein content in young men. Our data indicate that the ingestion of nutrient- and protein-dense foods differentially stimulates muscle anabolism compared with protein-dense foods. This trial was registered at clinicaltrials.gov as NCT03117127.


Assuntos
Proteínas Alimentares/farmacologia , Ovos , Exercício Físico/fisiologia , Proteínas Musculares/biossíntese , Músculo Esquelético/efeitos dos fármacos , Biossíntese de Proteínas/efeitos dos fármacos , Tecido Adiposo , Adulto , Estudos Cross-Over , Dieta , Proteínas Alimentares/administração & dosagem , Ingestão de Alimentos , Clara de Ovo , Humanos , Leucina/sangue , Leucina/farmacocinética , Masculino , Músculo Esquelético/metabolismo , Nitrogênio/administração & dosagem , Nitrogênio/farmacologia , Fenilalanina/metabolismo , Período Pós-Prandial , Adulto Jovem
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