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1.
Biomed Res Int ; 2019: 6289380, 2019.
Artículo en Inglés | MEDLINE | ID: mdl-31275980

RESUMEN

Early recovery from muscular injury is crucial for elite athletes. Hyperbaric oxygen therapy (HBOT) has been reported to be beneficial in terms of accelerating cell recovery and tissue repair, which are considered to be helpful for eliminating fatigue and recovering stamina. This study was performed to evaluate the efficacy of HBOT for exercise-related muscular injury. Forty-one athletes with exercise-related muscular injuries were recruited and randomized into an HBOT group and a control group. All participants received 10 sessions of either HBOT or placebo treatment. The brief pain inventory (BPI) was completed, and serum samples were analyzed. Data were collected before treatment (T1), at the end of the fifth treatment session (T2), at the end of the tenth treatment session (T3), and two weeks after T3 (T4). At T3, the HBOT group showed prominent reductions in the levels of creatine phosphokinase (CK), glutamic oxaloacetate transaminase (GOT), and myoglobin (MB), which lasted until T4. However, the control group did not present any statistical differences in levels from T1 to T4. In terms of pain intensity and interference, the HBOT group showed significant improvements at T3, while no improvements were observed in the control group. In conclusion, HBOT facilitates the early recovery of exercise-related muscular injury. This trial is registered with ISRCTN17817041.


Asunto(s)
Ejercicio Físico/fisiología , Oxigenoterapia Hiperbárica , Músculos/lesiones , Adulto , Enzimas/sangre , Humanos , Masculino , Músculos/enzimología , Dolor/patología , Dimensión del Dolor , Resultado del Tratamiento , Adulto Joven
2.
Artículo en Inglés | MEDLINE | ID: mdl-31091463

RESUMEN

AMP-activated protein kinase (AMPK) is considered as the master cellular metabolism regulator that activates various proteins, including O-GlcNAc transferase (OGT). Physiological roles of AMPK and OGT, including the relationship between their mRNA expression and food intake, are poorly understood in channel catfish. This study examined the tissue distribution of AMPK and OGT mRNA and changes in their expression in response to changes in food intake in channel catfish. Expression of all AMPK subunit and OGT mRNA was detectable in the whole brain, liver, heart, spleen, white muscle, and kidney of channel catfish. The OGT mRNA was highly localized in the brain compared to other tissues. 28-day fasting increased hepatic expression of AMPK α1, ß1, and OGT mRNA while refeeding fish for 14 days after the 14-day fast decreased their expression to the level similar to that of fish that were fed daily. No changes were noted in the expression of muscle and brain AMPK mRNA or OGT mRNA by fasting and refeeding. Hepatic AMPK α1, α2 and ß1 mRNA decreased in response to increased feeding frequency, whereas no changes in the expression of AMPK or OGT mRNA were noted in the brain or the muscle. Results of the current study indicated that the hepatic expression of AMPK and OGT mRNA appeared to be more sensitive to changes in food intake in channel catfish. However, further studies are needed to clearly demonstrate if food intake influences the expression of AMPK and OGT mRNA in various tissues, including the hypothalamus.


Asunto(s)
Bagres/genética , N-Acetilglucosaminiltransferasas/genética , Proteínas Quinasas/genética , Quinasas de la Proteína-Quinasa Activada por el AMP , Animales , Ingestión de Alimentos/genética , Regulación de la Expresión Génica/genética , Hipotálamo/enzimología , Hígado/enzimología , Músculos/enzimología , ARN Mensajero/genética , Distribución Tisular/genética
3.
Artículo en Inglés | MEDLINE | ID: mdl-31059784

RESUMEN

This study evaluated the efficacy of replacing dietary fish oil (FO) with vegetable oils (virgin coconut and corn oil) on enzyme activities (glycolytic, oxidative and lipid metabolites), mRNA expression of lipid metabolic genes and histomorphology of liver and intestine in O. niloticus. O. niloticus (6.07 ±â€¯0.07 g) was fed six experimental diets where fish oil (FO) served as the control diet, and then was supplemented by dietary oils; virgin coconut oil (VCO) {3%FO + 3%VCO; 3FVCO}, and corn oil (CO) {3%FO + 3%CO; 3FCO}, 6%VCO (VCO), 6%CO (CO) and 6%VO {3%VCO + 3%CO; VO}. Growth performances measured indicated fish fed diet 3FCO had higher weight gain (WG) and specific growth rate (SGR). Fish fed diet 3FCO recorded the highest activities in lactate dehydrogenase (LDH), pyruvate kinase (PK), citrate synthase (CS), cytochrome coxidase (COX), malic enzymes (ME) and lipoprotein lipase (LPL) respectively. Stearoyl-CoA desaturase (SCD1) was upregulated in groups fed diets 3FVCO and 3FCO. Also, groups fed diet VCO and CO expressed highly in LPL, whereas, elongase of very long-chain fatty acids (ELOVL-5) was not influenced by the lipid sources. Histological representations in the liver were highly impacted in vegetable diets where lipid accumulation was higher except those fed VCO. However, in the digestive tract from distal to middle and posterior, the same group (VCO) exhibited altered morphological structure as those fed diet 3FCO were similar to FO. The study shows that, corn oil in diets relates positively to growth and enzymatic activities which becomes evident in their depositions in liver and functional intestinal tracts. This study indicates dietary alternatives may cause alterations in lipid metabolic pathways (LPL and SCD1) involved in fatty acid transport. As such, polyunsaturated fatty acid (PUFA) rich diets (CO) based on this study results increases metabolic activities involving especially the production, distribution and consumption of adenosine triphosphate (ATP) in O. niloticus.


Asunto(s)
Cíclidos/fisiología , Grasas Insaturadas en la Dieta/farmacología , Proteínas de Peces/genética , Hígado/enzimología , Músculos/enzimología , Adenosina Trifosfato/metabolismo , Alimentación Animal , Animales , Peso Corporal/efectos de los fármacos , Cíclidos/genética , Cíclidos/crecimiento & desarrollo , Aceite de Coco/farmacología , Aceite de Maíz/farmacología , Enzimas/metabolismo , Aceites de Pescado/farmacología , Proteínas de Peces/metabolismo , Regulación de la Expresión Génica/efectos de los fármacos , Intestinos/citología , Intestinos/efectos de los fármacos , Metabolismo de los Lípidos/efectos de los fármacos , Metabolismo de los Lípidos/genética , Hígado/citología , Hígado/efectos de los fármacos , Músculos/efectos de los fármacos
4.
Oxid Med Cell Longev ; 2018: 5763256, 2018.
Artículo en Inglés | MEDLINE | ID: mdl-29636849

RESUMEN

The aim of this study was to determine whether oxidative stress markers are influenced by low-intensity laser therapy (LLLT) in rats subjected to a high-intensity resistive exercise session (RE). Female Wistar rats divided into three experimental groups (Ctr: control, 4J: LLLT, and RE) and subdivided based on the sampling times (instantly or 24 h postexercise) underwent irradiation with LLLT using three-point transcutaneous method on the hind legs, which was applied to the gastrocnemius muscle at the distal, medial, and proximal points. Laser (4J) or placebo (device off) were carried out 60 sec prior to RE that consisted of four climbs bearing the maximum load with a 2 min time interval between each climb. Lipoperoxidation levels and antioxidant capacity were obtained in muscle. Lipoperoxidation levels were increased (4-HNE and CL markers) instantly post-RE. LLLT prior to RE avoided the increase of the lipid peroxidation levels. Similar results were also notified for oxidation protein assays. The GPx and FRAP activities did not reduce instantly or 24 h after RE. SOD increased 24 h after RE, while CAT activity did not change with RE or LLLT. In conclusion, LLLT prior to RE reduced the oxidative stress markers, as well as, avoided reduction, and still increased the antioxidant capacity.


Asunto(s)
Terapia por Luz de Baja Intensidad , Estrés Oxidativo/efectos de la radiación , Condicionamiento Físico Animal , Animales , Femenino , Peroxidación de Lípido/efectos de la radiación , Músculos/enzimología , Músculos/patología , Músculos/efectos de la radiación , Ratas Wistar
5.
PLoS One ; 12(11): e0189001, 2017.
Artículo en Inglés | MEDLINE | ID: mdl-29190764

RESUMEN

The current NRC selenium (Se) requirement for turkeys is 0.2 µg Se/g diet. We previously fed turkey poults a Se-deficient diet (0.005 µg Se/g) supplemented with 10 graded levels of Se (0, 0.025, 0.05, 0.1, 0.2, 0.3, 0.4, 0.5, 0.75, 1.0 µg Se/g as Na2SeO3, 5/treatment) for 4 wk, and found that the minimum dietary Se requirement was 0.3 µg Se/g based on selenoprotein enzyme activity in blood, liver, gizzard and pancreas. Because the turkey is primarily a production animal, we expanded this analysis to kidney, heart, breast and thigh. Se concentrations in Se-deficient poults were 5.0, 9.8, 33, and 15% of levels in poults fed 0.4 µg Se/g in liver, kidney, thigh and breast, respectively. Increasing Se supplementation resulted in hyperbolic response curves for all tissues; breakpoint analysis indicated minimum Se requirements of 0.34-0.36 µg Se/g based on tissue Se levels in liver, kidney and thigh. Similarly, GPX1 activity in muscle tissues and kidney responded hyperbolically to increasing dietary Se, reaching well-defined plateaus with breakpoints at 0.30-0.36 µg Se/g. Minimum Se requirements based on GPX4 activity were 0.30-0.32 µg Se/g for breast and thigh. Selenoprotein transcript expression decreased significantly in Se deficiency for only 2, 3, 5, and 6 mRNA in breast, thigh, heart, and kidney, respectively, out of 24 known avian selenoproteins. Se response curves for regulated selenoprotein transcripts were hyperbolic, and reached well-defined plateaus with breakpoints in a narrow range of 0.08-0.19 µg Se/g. No selenoprotein transcript was altered by supernutritional Se. In summary, these results clearly indicate that the NRC dietary Se requirement should be raised to 0.4 µg Se/g, at least for poults, to meet the nutritional needs of the young turkey. The Se response curve plateaus further show that limits for turkey supplementation with selenite could safely be raised to 0.5 µg Se/g diet.


Asunto(s)
Enzimas/metabolismo , Riñón/enzimología , Músculos/enzimología , ARN Mensajero/genética , Selenoproteínas/metabolismo , Animales , Enzimas/genética , Turquía
6.
J Nutr ; 147(5): 781-788, 2017 05.
Artículo en Inglés | MEDLINE | ID: mdl-28356434

RESUMEN

Background: Nucleotides have been used as functional nutrients to improve the growth and health of animals, including fish. The mechanism involved in the growth-promotion effect of nucleotides is still unclear.Objective: We investigated the bioenergetic mechanism underlying the growth-promotion effect of nucleotides in zebrafish and the associated roles played by the intestinal microbiota.Methods: Larval zebrafish were fed a control or a 0.1% mixed nucleotides-supplemented diet for 2 wk. Standard metabolic rate, the minimal rate of energy expenditure by animals at rest, was evaluated by oxygen consumption with the use of a respirometer. The expressions of fasting-induced adipose factor (Fiaf), inflammatory cytokines, and genes involved in fatty acid (FA) oxidation were tested by quantitative reverse transcriptase-polymerase chain reaction. The intestinal microbiota from the nucleotide-fed fish (NT fish) or control fish was transferred to 3-d postfertilization germ-free zebrafish in which oxygen consumption and expression of cytokines and fiaf were evaluated.Results: Compared with controls, nucleotide supplementation at 0.1% increased the weight and energy gains of zebrafish by 10% and 25%, respectively (P < 0.01). Standard metabolic rate was 28% lower in NT fish than in controls (P < 0.001). Nucleotide supplementation downregulated the inflammatory tone in the head kidney of the fish. Moreover, NT fish had a 51% lower intestinal expression of fiaf than did controls (P < 0.05), which was consistent with decreased expression of key genes involved in FA oxidation [carnitine:palmitoyl transferase 1a (cpt1a) and medium-chain acyl coenzyme A dehydrogenase (mcad)] in liver and muscle. Germ-free zebrafish colonized with microbiota from NT fish had a 25% lower standard metabolic rate than did those colonized by control microbiota (P < 0.01), whereas direct nucleotide feeding of germ-free zebrafish did not affect standard metabolic rate relative to germ-free controls that were not fed nucleotides. Furthermore, germ-free zebrafish colonized with nucleotide microbiota exhibited downregulated inflammatory tone and 33% lower fiaf expression compared with their control microbiota-colonized counterparts.Conclusions: The growth-promoting effect of dietary nucleotides in zebrafish involves 2 intestinal microbiota-mediated mechanisms that result in reduced standard metabolic rate: 1) lower inflammatory tone and 2) reduced FA oxidation associated with increased microbial suppression of intestinal fiaf.


Asunto(s)
Metabolismo Basal/efectos de los fármacos , Suplementos Dietéticos , Microbioma Gastrointestinal , Intestinos/efectos de los fármacos , Nucleótidos/farmacología , Pez Cebra , Proteína 4 Similar a la Angiopoyetina , Angiopoyetinas/metabolismo , Crianza de Animales Domésticos , Fenómenos Fisiológicos Nutricionales de los Animales , Animales , Citocinas/metabolismo , Inflamación/metabolismo , Mucosa Intestinal/metabolismo , Intestinos/microbiología , Riñón/efectos de los fármacos , Riñón/metabolismo , Lipólisis/genética , Hígado/efectos de los fármacos , Hígado/enzimología , Músculos/efectos de los fármacos , Músculos/enzimología , Consumo de Oxígeno , Descanso , Pez Cebra/metabolismo , Pez Cebra/microbiología , Proteínas de Pez Cebra/metabolismo
7.
Ann Nutr Metab ; 68 Suppl 3: 15-20, 2016.
Artículo en Inglés | MEDLINE | ID: mdl-27931032

RESUMEN

Alterations in muscle fatty acid metabolism have been implicated in mediating the severity of insulin resistance. In the insulin resistant heart fatty acids are favored as an energy source over glucose, which is thus associated with increased fatty acid oxidation, and an overall decrease in glycolysis and glucose oxidation. In addition, excessive uptake and beta-oxidation of fatty acids in obesity and diabetes can compromise cardiac function. In animal studies, mice fed a high fat diet (HFD) show cardiac insulin resistance in which the accumulation of intra-myocardial diacylglycerol has been implicated, likely involving parallel signaling pathways. A HFD also results in accumulation of fatty acid oxidation byproducts in muscle, further contributing to insulin resistance. Carnitine acetyltransferase (CrAT) has an essential role in the cardiomyocyte because of its need for large amounts of carnitine. In the cardiomyocyte, carnitine switches energy substrate preference in the heart from fatty acid oxidation to glucose oxidation. This carnitine-induced switch in fatty acid oxidation to glucose oxidation is due to the presence of cytosolic CrAT and reverse CrAT activity. Accordingly, inhibition of fatty acid oxidation, or stimulation of CrAT, may be a novel approach to treatment of insulin resistance.


Asunto(s)
Carnitina Aciltransferasas/metabolismo , Carnitina/metabolismo , Diabetes Mellitus/metabolismo , Ácidos Grasos no Esterificados/metabolismo , Resistencia a la Insulina , Miocardio/metabolismo , Obesidad/metabolismo , Animales , Carnitina/deficiencia , Carnitina/uso terapéutico , Carnitina Aciltransferasas/química , Enfermedades Carenciales/dietoterapia , Enfermedades Carenciales/metabolismo , Enfermedades Carenciales/fisiopatología , Enfermedades Carenciales/prevención & control , Diabetes Mellitus/dietoterapia , Diabetes Mellitus/etiología , Diabetes Mellitus/fisiopatología , Dieta Alta en Grasa/efectos adversos , Suplementos Dietéticos , Diglicéridos/metabolismo , Corazón/fisiopatología , Humanos , Músculos/enzimología , Músculos/metabolismo , Miocardio/enzimología , Obesidad/dietoterapia , Obesidad/etiología , Obesidad/fisiopatología , Oxidación-Reducción , Disfunción Ventricular/etiología , Disfunción Ventricular/prevención & control
8.
J Trace Elem Med Biol ; 35: 7-17, 2016 May.
Artículo en Inglés | MEDLINE | ID: mdl-27049122

RESUMEN

The green synthesized Mn3O4 nanoparticles (manganese-oxide nanoparticles) using Ananas comosus (L.) peel extract was characterized by various techniques. HR-SEM photograph showed that manganese-oxide nanoparticles (Mn-oxide NPs) were spherical in shape, with an average size of 40-50 nm. The Zeta potential revealed the surface charge of Mn-oxide NPs to be negative. Further, the Mn-oxide NPs were dietary supplemented for freshwater prawn Macrobrachium rosenbergii. The experimental basal diets were supplemented with Mn-oxide NPs at the rates of 0 (control), 3.0, 6.0, 9.0, 12, 15 and 18 mg/kg dry feed weight. The as-supplemented Mn-oxide NPs were fed in M. rosenbergii for a period of 90 days. The experimental study demonstrated that prawns fed with diet supplemented with 3-18 mg Mn-oxide NPs/kg shows enhanced (P<0.05) growth performance, including final weight and weight gain (WG). Significant differences (P<0.05) in feed conversion ratio (FCR) were observed in prawn fed with different diets. Additionally, prawns fed with 3.0-18 mg/kg Mn-oxide NPs supplemented diets achieved significant (P<0.05) improvement in growth performance, digestive enzyme activities and muscle biochemical compositions, while, the prawns fed with 16 mg/kg of Mn-oxide NPs showed enhanced performance. Prawns fed on diet supplemented with 16 mg/kg Mn-oxide NPs showed significantly (P<0.05) higher total protein level. The antioxidants enzymatic activity (SOD and CAT) metabolic enzymes status in muscle and hepatopancreas showed no significant (P>0.05) alterations in prawns fed with 3.0-18 mg/kg of Mn-oxide NPs supplemented diets. Consequently, the present work proposed that 16 mg/kg of Mn-oxide NPs could be supplemented for flexible enhanced survival, growth and production of M. rosenbergii. Therefore, the data of the present study recommend the addition of 16 mg/kg of Mn-oxide NPs diet to developed prawn growth and antioxidant defense system.


Asunto(s)
Suplementos Dietéticos , Digestión/efectos de los fármacos , Agua Dulce , Tecnología Química Verde/métodos , Compuestos de Manganeso/farmacología , Nanopartículas/química , Óxidos/farmacología , Palaemonidae/enzimología , Palaemonidae/crecimiento & desarrollo , Animales , Antioxidantes/metabolismo , Dispersión Dinámica de Luz , Minerales/análisis , Músculos/efectos de los fármacos , Músculos/enzimología , Nanopartículas/ultraestructura , Palaemonidae/efectos de los fármacos , Espectroscopía de Fotoelectrones , Espectrometría por Rayos X , Espectroscopía Infrarroja por Transformada de Fourier , Propiedades de Superficie
9.
Cell Metab ; 22(1): 65-76, 2015 Jul 07.
Artículo en Inglés | MEDLINE | ID: mdl-26154055

RESUMEN

Acylcarnitine metabolites have gained attention as biomarkers of nutrient stress, but their physiological relevance and metabolic purpose remain poorly understood. Short-chain carnitine conjugates, including acetylcarnitine, derive from their corresponding acyl-CoA precursors via the action of carnitine acetyltransferase (CrAT), a bidirectional mitochondrial matrix enzyme. We show here that contractile activity reverses acetylcarnitine flux in muscle, from net production and efflux at rest to net uptake and consumption during exercise. Disruption of this switch in mice with muscle-specific CrAT deficiency resulted in acetyl-CoA deficit, perturbed energy charge, and diminished exercise tolerance, whereas acetylcarnitine supplementation produced opposite outcomes in a CrAT-dependent manner. Likewise, in exercise-trained compared to untrained humans, post-exercise phosphocreatine recovery rates were positively associated with CrAT activity and coincided with dramatic shifts in muscle acetylcarnitine dynamics. These findings show acetylcarnitine serves as a critical acetyl buffer for working muscles and provide insight into potential therapeutic strategies for combatting exercise intolerance.


Asunto(s)
Acetilcoenzima A/metabolismo , Carnitina O-Acetiltransferasa/metabolismo , Carnitina/análogos & derivados , Fatiga Muscular , Músculos/enzimología , Animales , Carnitina/sangre , Carnitina/metabolismo , Ejercicio Físico , Humanos , Ratones Endogámicos C57BL , Músculos/metabolismo , Condicionamiento Físico Animal
10.
Biochim Biophys Acta ; 1850(1): 97-106, 2015 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-25316288

RESUMEN

BACKGROUND: The North American wood frog, Rana sylvatica, is able to overcome subzero conditions through overwintering in a frozen state. Freezing imposes ischemic and oxidative stress on cells as a result of cessation of blood flow. Superoxide dismutases (SODs) catalyze the redox reaction involving the dismutation of superoxide (O(2)(-)) to molecular oxygen and hydrogen peroxide. METHODS: The present study investigated the regulation of CuZnSOD and MnSOD kinetics as well as the transcript, protein and phosphorylation levels of purified enzyme from the muscle of control and frozen R. sylvatica. RESULTS: CuZnSOD from frozen muscle showed a significantly higher V(max) (1.52 fold) in comparison to CuZnSOD from the muscle of control frogs. MnSOD from frozen muscle showed a significantly lower Km for O(2)(-) (0.66 fold) in comparison to CuZnSOD from control frogs. MnSOD from frozen frogs showed higher phosphorylation of serine (2.36 fold) and tyrosine (1.27 fold) residues in comparison to MnSOD from control animals. Susceptibility to digestion via thermolysin after incubation with increasing amount of urea (C(m)) was tested, resulting in no significant changes for CuZnSOD, whereas a significant change in MnSOD stability was observed between control (2.53 M urea) and frozen (2.92 M urea) frogs. Expressions of CuZnSOD and MnSOD were quantified at both mRNA and protein levels in frog muscle, but were not significantly different. CONCLUSION: The physiological consequence of freeze-induced SOD modification appears to adjust SOD function in freezing frogs. GENERAL SIGNIFICANCE: Augmented SOD activity may increase the ability of R. sylvatica to overcome oxidative stress associated with ischemia.


Asunto(s)
Radicales Libres/metabolismo , Congelación , Ranidae/metabolismo , Superóxido Dismutasa/metabolismo , Adaptación Fisiológica , Secuencia de Aminoácidos , Animales , Western Blotting , ADN Complementario/química , ADN Complementario/genética , Estabilidad de Enzimas , Regulación Enzimológica de la Expresión Génica , Isoenzimas/genética , Isoenzimas/aislamiento & purificación , Isoenzimas/metabolismo , Cinética , Masculino , Datos de Secuencia Molecular , Músculos/enzimología , América del Norte , Fosforilación , Ranidae/genética , Ranidae/fisiología , Reacción en Cadena de la Polimerasa de Transcriptasa Inversa , Análisis de Secuencia de ADN , Homología de Secuencia de Aminoácido , Superóxido Dismutasa/genética , Superóxido Dismutasa/aislamiento & purificación
11.
Mol Nutr Food Res ; 58(10): 1931-40, 2014 Oct.
Artículo en Inglés | MEDLINE | ID: mdl-25066301

RESUMEN

SCOPE: Dietary polyphenols are suggested to play a role in the prevention of Alzheimer's disease, of which accumulation of aggregated beta amyloid (Aß) is a key histopathological hallmark. We used the transgenic Caenorhabditis elegans strain CL2006, which expresses human Aß1₋42 under control of a muscle-specific promoter and responds to Aß1₋42 aggregation with paralysis, to test effects of the polyphenol quercetin on the phenotype. METHODS AND RESULTS: Quercetin dose-dependently decreased the amount of aggregated proteins in solution and also paralysis in CL2006. The knockdown of key components of unfolded protein response in mitochondria or the endoplasmic reticulum by RNA-interference (RNAi) enhanced paralysis in CL2006 but did not prevent the paralysis reducing activities of quercetin. RNAi for essential members of proteasomal protein degradation or macroautophagy also significantly increased paralysis but prevented quercetin from being effective. Quercetin increased proteasomal activity and, moreover, enhanced the flow of proteins through the macroautophagy pathway as reflected by reduced lysosome staining. CONCLUSION: The proteostasis network, including unfolded protein response, defines the aggregation of Aß1₋42 and the associated paralysis phenotype in a nematode model for Alzheimer's disease. The polyphenol quercetin, by specifically activating macroautophagy and proteasomal degradation pathways, proved able to prevent Aß1₋42 agregation and paralysis.


Asunto(s)
Enfermedad de Alzheimer/prevención & control , Péptidos beta-Amiloides/antagonistas & inhibidores , Antioxidantes/uso terapéutico , Caenorhabditis elegans , Modelos Animales de Enfermedad , Proteínas del Tejido Nervioso/antagonistas & inhibidores , Fragmentos de Péptidos/antagonistas & inhibidores , Quercetina/uso terapéutico , Enfermedad de Alzheimer/metabolismo , Péptidos beta-Amiloides/genética , Péptidos beta-Amiloides/metabolismo , Animales , Animales Modificados Genéticamente , Antioxidantes/administración & dosificación , Autofagia , Proteínas de Caenorhabditis elegans/antagonistas & inhibidores , Proteínas de Caenorhabditis elegans/genética , Proteínas de Caenorhabditis elegans/metabolismo , Suplementos Dietéticos , Humanos , Lisosomas/enzimología , Lisosomas/metabolismo , Músculos/enzimología , Músculos/metabolismo , Proteínas del Tejido Nervioso/genética , Proteínas del Tejido Nervioso/metabolismo , Parálisis/inducido químicamente , Parálisis/prevención & control , Fragmentos de Péptidos/genética , Fragmentos de Péptidos/metabolismo , Complejo de la Endopetidasa Proteasomal/metabolismo , Agregación Patológica de Proteínas/enzimología , Agregación Patológica de Proteínas/metabolismo , Agregación Patológica de Proteínas/prevención & control , Proteolisis , Quercetina/administración & dosificación , Interferencia de ARN , Respuesta de Proteína Desplegada
12.
Br J Nutr ; 112(3): 285-94, 2014 Aug 14.
Artículo en Inglés | MEDLINE | ID: mdl-24787366

RESUMEN

The pulp of jussara açaí (Euterpe edulis Martius) fruit is rich in anthocyanins that exert antioxidant and anti-inflammatory effects similar to those exerted by aerobic exercise. In the present study, we investigated the effects of jussara açaí fruit pulp consumption, either alone or in combination with aerobic exercise, on the hepatic oxidative and inflammatory status of ApoE-deficient (ApoE - / - ) mice. Male mice were divided into four groups (control (C), control plus açaí, exercise plus açaí (EXA) and exercise (EX)) and fed the AIN-93M diet or the AIN-93M diet formulated to contain 2 % freeze-dried açaí pulp. Mice in the EX and EXA groups were subjected to a progressive running programme (5 d/week, 60 min/d, 16 m/min) for 12 weeks. Mice that were made to exercise exhibited reduced (40·85 %; P< 0·05) hepatic superoxide dismutase activity when compared with the C mice, independent of the açaí diet. Mice in the EX group exhibited a lower (42 %; P< 0·05) mRNA expression of monocyte chemotactic protein-1 in the liver compared with the C mice. Mice in the EXA and EX groups had lower percentages of hepatic lipid droplets (70 % and 56 %, respectively; P< 0·05) when compared with the C mice. Mice in the EX group had smaller (58 %; P< 0·05) area of lesions in the aorta when compared with the C mice. Serum lipid profile was not affected (P>0·05). In conclusion, aerobic exercise training rather than açaí fruit pulp consumption or a combination of both enhances the hepatic oxidative and inflammatory status of ApoE - / - mice.


Asunto(s)
Antocianinas/administración & dosificación , Apolipoproteínas E/deficiencia , Arecaceae , Frutas/química , Hígado/química , Condicionamiento Físico Animal , Animales , Antiinflamatorios/administración & dosificación , Antioxidantes/administración & dosificación , Apolipoproteínas E/fisiología , Biomarcadores/análisis , Quimiocina CCL2/genética , Citrato (si)-Sintasa/metabolismo , Dieta , Suplementos Dietéticos , Inflamación/patología , Hígado/patología , Masculino , Ratones , Ratones Noqueados , Músculos/enzimología , Oxidación-Reducción , ARN Mensajero/análisis , Superóxido Dismutasa/metabolismo
13.
Biotechnol Lett ; 36(9): 1819-25, 2014 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-24863289

RESUMEN

Nanoporous alumina membranes were silanized with aminopropylsilane and iminodiacetic acid (IDA) groups were generated in situ by reaction with iodoacetate. The membranes were mounted in standard filter holders, connected to a HPLC system and saturated with selected metal ions. Cu(II) allowed the capture of chicken muscle lactate dehydrogenase with such stability, repeatability and reproducibility that Michaelis-Menten kinetics could be studied. The IDA surface was stable for months and could be depleted and regenerated with metal ions multiple times without appreciable loss of capacity. The binding of lactate dehydrogenase influenced the backpressure to the extent that could be expected for a monolayer according to Poiseuilles law.


Asunto(s)
Óxido de Aluminio/metabolismo , Enzimas Inmovilizadas/metabolismo , Iminoácidos/metabolismo , Nanoporos , Animales , Pollos , Estabilidad de Enzimas , L-Lactato Deshidrogenasa/metabolismo , Músculos/enzimología
14.
Gene ; 538(2): 235-43, 2014 Apr 01.
Artículo en Inglés | MEDLINE | ID: mdl-24491503

RESUMEN

Calcium-calmodulin dependent protein kinase I is a component of a calmodulin-dependent protein kinase cascade and involved in many physiological processes. The full-length cDNA of calcium-calmodulin dependent protein kinase I (MnCaMKI) was cloned from the freshwater prawn Macrobrachium nipponense and its expression pattern during the molt cycle and after eyestalk ablation is described. The full-length cDNA of MnCaMKI is 3,262 bp in length and has an open reading frame (ORF) of 1,038 bp, encoding a 345 amino acid protein. The expression of MnCaMKI in three examined tissues was upregulated in the premolt stage of the molt cycle. Its expression was induced after eyestalk ablation (ESA): the highest expression level was reached 1 day after ESA in hepatopancreas, and 3 days after ESA in muscle. By dsRNA-mediated RNA interference assay, expression of MnCaMKI and ecydone receptor gene (MnEcR) was significantly decreased in prawns treated by injection of dsMnCaMKI, while expression of these two genes was also significantly decreased in prawns treated by injection of dsMnEcR, demonstrating a close correlation between the expression of these two genes. These results suggest that CaMKI in M. nipponense is involved in molting.


Asunto(s)
Proteína Quinasa Tipo 1 Dependiente de Calcio Calmodulina/fisiología , Palaemonidae/enzimología , Palaemonidae/genética , Secuencia de Aminoácidos , Animales , Secuencia de Bases , Proteína Quinasa Tipo 1 Dependiente de Calcio Calmodulina/genética , Clonación Molecular , ADN Complementario/genética , Regulación del Desarrollo de la Expresión Génica , Regulación Enzimológica de la Expresión Génica , Hepatopáncreas/enzimología , Datos de Secuencia Molecular , Muda/genética , Muda/fisiología , Músculos/enzimología , Sistemas de Lectura Abierta , Palaemonidae/crecimiento & desarrollo , Filogenia , Interferencia de ARN , ARN Mensajero/genética , ARN Mensajero/metabolismo , Receptores de Esteroides/genética , Receptores de Esteroides/fisiología , Homología de Secuencia de Aminoácido
15.
Fish Physiol Biochem ; 40(3): 659-71, 2014 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-24174167

RESUMEN

The dietary lysine requirement of sub-adult grass carp (460 ± 1.5 g) was assessed by feeding diets supplemented with grade levels of lysine (6.6, 8.5, 10.8, 12.9, 15.0 and 16.7 g kg(-1) diet) for 56 days. The test diets (28% CP) contained fish meal, casein and gelatin as sources of intact protein, supplemented with crystalline amino acids. Weight gain (WG), feed intake and feed efficiency were significantly improved with increasing levels of lysine up to 12.9 g kg(-1) diet and thereafter declined (P < 0.05). Quadratic regression analysis of WG at 95% maximum response indicated lysine requirement was 10.9 g kg(-1) diet. Activities of trypsin, chymotrypsin, lipase, Na(+), K(+)-ATPase and alkaline phosphatase in intestine, creatine kinase activity in proximal and mid-intestine responded similar to WG (P < 0.05). In addition, lipid and protein oxidation decreased with increasing levels of lysine up to certain values and increased thereafter (P < 0.05); the anti-hydroxyl radical capacity, dismutase, catalase, glutathione peroxidase, glutathione reductase, glutathione-S-transferase (GST) activities and glutathione content were increased with increasing dietary lysine levels up to certain values in the detected tissues, except for hepatopancreatic GST. Requirement estimated on the basis of malondialdehyde content in intestine and hepatopancreas was 10.6 and 9.53 g lysine kg(-1) diet, respectively.


Asunto(s)
Antioxidantes/metabolismo , Carpas/metabolismo , Proteínas de Peces/metabolismo , Intestinos/enzimología , Lisina/administración & dosificación , Transferasas Alquil y Aril/metabolismo , Animales , Acuicultura , Carpas/crecimiento & desarrollo , Dieta , Intestinos/crecimiento & desarrollo , Microvellosidades/enzimología , Músculos/enzimología , Transferasas (Grupos de Otros Fosfatos Sustitutos)/metabolismo
16.
Mol Biol Rep ; 40(12): 7017-25, 2013 Dec.
Artículo en Inglés | MEDLINE | ID: mdl-24178343

RESUMEN

Adiponectin is an adipokine hormone that influences glucose utilization, insulin sensitivity and energy homeostasis. To investigate the effect of adiponectin on lipids deposition in broilers, rosiglitazone and dexamethasone were used to treat broilers. A total of 120 twenty-three-day-old male Cobb broilers were randomly divided into 3 groups for 3 weeks of drug treatment. Serum adiponectin level and fatty acid composition in muscles were measured. Adiponectin, adiponectin receptors (adipoR1, adipoR2) and lipid metabolism-related genes expression levels in muscles were measured using real-time PCR. Western blot was used to measure the expression levels of lipid metabolism-related proteins and the phosphorylation of p38 mitogen-activated protein kinase (p38 MAPK)/activating transcription factor 2 (ATF2) pathway marker proteins. Rosiglitazone increased serum adiponectin concentration and the expression levels of adiponectin and adipoR1 (P < 0.05), while dexamethasone had the opposite effect. Intramuscular fat content, total fatty acid, saturated fatty acid and monounsaturated fatty acid reduced in the rosiglitazone treatment group (P < 0.05). In the rosiglitazone treatment group, the expression levels of lipogenic genes and proteins decreased in the muscles, whereas the expression levels of lipolysis genes increased. Meanwhile, the phosphorylation levels of p38MAPK and ATF2 increased with supplementation of rosiglitazone and decreased in the dexamethasone treatment group (P < 0.01). These results indicated that rosiglitazone and dexamethasone could regulate adiponectin expression in muscle of broilers and adiponectin had an anti-lipogenic effect by p38 MAPK/ATF2 signaling pathway.


Asunto(s)
Factor de Transcripción Activador 2/metabolismo , Adiponectina/metabolismo , Pollos/metabolismo , Metabolismo de los Lípidos , Músculos/metabolismo , Transducción de Señal , Proteínas Quinasas p38 Activadas por Mitógenos/metabolismo , Adiponectina/sangre , Adiponectina/genética , Animales , Pollos/sangre , Pollos/genética , Pollos/crecimiento & desarrollo , Extremidades , Ácidos Grasos/metabolismo , Metabolismo de los Lípidos/genética , Masculino , Músculos/efectos de los fármacos , Músculos/enzimología , Fosforilación/efectos de los fármacos , ARN Mensajero/genética , ARN Mensajero/metabolismo , Receptores de Adiponectina/metabolismo , Rosiglitazona , Transducción de Señal/efectos de los fármacos , Transducción de Señal/genética , Tiazolidinedionas/farmacología
17.
Food Chem ; 141(3): 2666-74, 2013 Dec 01.
Artículo en Inglés | MEDLINE | ID: mdl-23871009

RESUMEN

Tea polyphenols (TP) are known to be important for the post-mortem deterioration of fish muscle and can enhance food quality. To shed light on the influence of TP on the status of large yellow croaker muscle proteins, control and treated fillets (0.1% TP, 0.2% TP and 0.3% TP, w/v) were analysed periodically for myofibrillar protein functional properties (Ca(2+)-ATPase activity, surface hydrophobicity, total sulfhydryl content, emulsion stability index and rheological behaviour). Degradation of the myofibrillar protein myosin could be clearly observed; several proteins were also observed to vary in abundance following post-mortem storage for 25 days. The present study offers new evidence that TP have an effective impact on muscle protein integrity post-mortem.


Asunto(s)
Camellia sinensis/química , Productos Pesqueros/análisis , Proteínas de Peces/química , Conservación de Alimentos/métodos , Conservantes de Alimentos/farmacología , Proteínas Musculares/química , Extractos Vegetales/farmacología , Polifenoles/farmacología , Adenosina Trifosfatasas/análisis , Animales , Interacciones Hidrofóbicas e Hidrofílicas , Músculos/química , Músculos/efectos de los fármacos , Músculos/enzimología , Perciformes/metabolismo , Estabilidad Proteica/efectos de los fármacos
18.
Carbohydr Polym ; 93(1): 31-7, 2013 Mar 01.
Artículo en Inglés | MEDLINE | ID: mdl-23465898

RESUMEN

An in vitro enzyme-catalyzed tandem reaction using the enzymes phosphorylase b from rabbit muscle and Deinococcus geothermalis glycogen branching enzyme (Dg GBE) to obtain branched polyglucans with tunable degree of branching (2% ÷ 13%) is presented. The tunable degree of branching is obtained by varying the reaction conditions such as pH value, the choice of reducing agent and its concentration and reaction time. Linear amylose is formed by the phosphorylase-catalyzed propagation of glucose-1-phosphate while Dg GBE introduces branching points on the α-(1→6) position by relocating short oligosaccharide chains. Our results show that the best way to obtain different degrees of branching with this set of enzymes is by regulation of the reaction time.


Asunto(s)
Glucanos/síntesis química , Polimerizacion , Enzima Ramificadora de 1,4-alfa-Glucano/química , Animales , Deinococcus/enzimología , Activación Enzimática , Glucanos/química , Glucofosfatos/química , Concentración de Iones de Hidrógeno , Músculos/enzimología , Fosforilasa b/química , Proteínas de Plantas/química , Conejos , Solanum tuberosum/química , Solanum tuberosum/enzimología , Factores de Tiempo
19.
Physiol Genomics ; 45(9): 367-76, 2013 May 01.
Artículo en Inglés | MEDLINE | ID: mdl-23512741

RESUMEN

Carnitine palmitoyl-CoA transferase-1B is a mitochondrial enzyme in the fatty acid oxidation pathway. In a previous study, CPT1B was identified as differentially expressed in the hypothalamus of two lines of chickens established by long-term selection for high (HWS) or low (LWS) body weight. Mammals have three paralogs (CPT1a, b and c) while nonmammalian vertebrates only have two (CPT1A, B). CPT1A is expressed in liver and CPT1B in muscle. CPT1c is expressed in hypothalamus, where it regulates feeding and energy expenditure. We identified an intronic length polymorphism, fixed for different alleles in the two populations, and mapped the hitherto missing CPT1B locus in the chicken genome assembly, to the distal tip of chromosome 1p. Based on molecular phylogeny and gene synteny we suggest that chicken CPT1B is pro-orthologous of the mammalian CPT1c. Chicken CPT1B was differentially expressed in both muscle and hypothalamus but in opposite directions: higher levels in hypothalamus but lower levels in muscle in the HWS than in the LWS line. Using an advanced intercross population of the lines, we found CPT1B expression to be influenced by a cis-acting expression quantitative trait locus in muscle. The increased expression in hypothalamus and reduced expression in muscle is consistent with an increased food intake in the HWS line and at the same time reduced fatty acid oxidation in muscle yielding a net accumulation of energy intake and storage. The altered expression of CPT1B in hypothalamus and peripheral tissue is likely to be a mechanism contributing to the remarkable difference between lines.


Asunto(s)
Peso Corporal/genética , Carnitina O-Palmitoiltransferasa/genética , Pollos/genética , Regulación Enzimológica de la Expresión Génica , Sitios de Carácter Cuantitativo/genética , Animales , Secuencia de Bases , Carnitina O-Palmitoiltransferasa/metabolismo , Mapeo Cromosómico , Cromosomas/genética , Cruzamientos Genéticos , Evolución Molecular , Femenino , Genotipo , Humanos , Hipotálamo/enzimología , Masculino , Proteínas Mitocondriales/metabolismo , Familia de Multigenes/genética , Músculos/enzimología , Especificidad de Órganos/genética , Filogenia , Polimorfismo Genético , ARN Mensajero/genética , ARN Mensajero/metabolismo , Sintenía/genética
20.
Asian Pac J Trop Med ; 5(12): 966-9, 2012 Dec.
Artículo en Inglés | MEDLINE | ID: mdl-23199715

RESUMEN

OBJECTIVE: To explore the effect of AIBL on Oncomelania hupensis, the intermediate snail host of Schistosoma japonicum. METHODS: The enzyme histochemical profiles of cholinesterase, cytochrome oxidase, lactate dehydrogenase, nitric oxide synthase, and succinate dehydrogenase in the soft tissues of Oncomelania hupensis, the intermediate host snail of Schistosoma japonicum, were analyzed before and after treatment with the active ingredient of Buddleia lindleyana (AIBL), a potent and safe plant molluscicide. RESULTS: Treatment with AIBL induced a notable decrease in the activities of the five enzymes (P<0.01). CONCLUSIONS: The results indicate that AIBL impairs the activities of the enzymes, thereby influencing the transfer of neurotransmitter and energy supply in Oncomelania hupensis and ultimately harming their various physiological functions, which are considered to cause death of the species.


Asunto(s)
Buddleja/química , Oxidorreductasas/análisis , Extractos Vegetales/farmacología , Caracoles/efectos de los fármacos , Caracoles/enzimología , Animales , Reservorios de Enfermedades , Ganglios/química , Ganglios/enzimología , Histocitoquímica , Hígado/química , Hígado/enzimología , Músculos/química , Músculos/enzimología , Oxidorreductasas/química , Extractos Vegetales/química , Esquistosomiasis Japónica
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