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ABSTRACT: OBJECTIVE: To determine whether upregulated whole body de novo arginine synthesis and protein breakdown are present as a compensatory mechanism to meet the increased demand for arginine and nitric oxide (NO) production in pediatric patients with cystic fibrosis (CF) and nutritional failure. STUDY DESIGN: In 16 children with CF, studied at the end of antibiotic treatment for a pulmonary exacerbation, and 17 healthy controls, whole body arginine, citrulline (Cit), and protein turnover were assessed by stable isotope methodology and de novo arginine synthesis, arginine clearance, NO synthesis, protein synthesis and breakdown, and net protein balance were calculated. The plasma isotopic enrichments and amino acid concentrations were measured by liquid chromatography-tandem mass spectrometry. RESULTS: Increased arginine clearance was found in patients with CF (P < .001), whereas whole body NO production rate and plasma arginine levels were not different. Whole body arginine production (P < .001), de novo arginine synthesis, and protein breakdown and synthesis (P < .05) were increased in patients with CF, but net protein balance was comparable. Patients with CF with nutritional failure (n = 7) had significantly higher NO production (P < .05), de novo arginine synthesis, Cit production (P < .001), and plasma Cit concentration (P < .05) and lower plasma arginine concentration (P < .05) than those without nutritional failure (n = 9). CONCLUSIONS: Nutritional failure in CF is associated with increased NO production. However, up-regulation of de novo arginine synthesis and Cit production was not sufficient to meet the increased arginine needs leading to arginine deficiency.
The Journal of pediatrics 02/2013; · 4.02 Impact Factor
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ABSTRACT: BACKGROUND: Current nutritional approaches have been partially successful in Cystic Fibrosis (CF). Essential amino acids mixtures with high Leucine levels (EAA) have anabolic properties in catabolic conditions, however data in CF are lacking. METHODS: On two days according a randomized crossover design, 15 pediatric CF patients ingested 6.7g EAA versus mixture of total amino acids as present in whey. Whole body protein and Arginine metabolism (as EAA lack Arginine) were assessed by stable isotope methodology. RESULTS: Protein synthesis (P<0.05) but not protein breakdown was higher after EAA and 70% higher values for net anabolism (P<0.001)were found both in patients with and without nutritional failure. Arginine turnover was lower (P<0.001) and de novo Arginine synthesis tended lower (P=0.09) after EAA. Nitric oxide synthesis was not different. CONCLUSIONS: CF patients are highly responsive to EAA intake independent of their nutritional status. Addition of Arginine to the EAA mixture may be warranted in CF.
Journal of cystic fibrosis: official journal of the European Cystic Fibrosis Society 01/2013; · 3.19 Impact Factor
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ABSTRACT: Arginine is derived from dietary protein intake, body protein breakdown or endogenous de novo arginine production. The latter may be linked to availability of citrulline, which is the immediate precursor of arginine and limiting factor for de novo arginine production. Arginine metabolism is highly compartmentalized due to the expression of enzymes involved in arginine metabolism in various organs. A small fraction of arginine enters the NO synthase (NOS) pathway. Tetrahydrobiopterin (BH4) is an essential and rate-limiting cofactor for the production of NO. Depletion of BH4 in oxidative stressed endothelial cells can result in so-called NOS3 'uncoupling', resulting in production of superoxide instead of NO. Moreover, distribution of arginine between intracellular transporters and arginine-converting enzymes, as well as between the arginine-converting and arginine-synthesizing enzymes, determines the metabolic fate of arginine. Alternatively, NO can be derived from conversion of nitrite. Reduced arginine availability from reduced de novo production and elevated arginase activity have been reported in various conditions of acute and chronic stress, often characterized by increased NOS2 and reduced NOS3 activity. Cardiovascular and pulmonary disorders such as atherosclerosis, diabetes, hypercholesterolemia, ischemic heart disease and hypertension are characterized by NOS3 uncoupling. Therapeutic applications to influence (de novo) arginine and NO metabolism aim at increasing substrate availability or influencing the metabolic fate of specific pathways related to NO bioavailability and prevention of NOS3 uncoupling. These include supplementation of arginine or citrulline, provision of NO donors including inhaled NO and nitrite, NOS3 modulating agents, or the targeting of endogenous NO inhibitors like asymmetric dimethylarginine.
AJP Endocrinology and Metabolism 09/2012; · 4.75 Impact Factor
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ABSTRACT: In a variety of chronic and acute disease states, alterations in protein synthesis, breakdown and protein turnover rates occur that are related to the loss of body protein and skeletal muscle wasting. A key observation is the stimulation of protein breakdown in muscle and the stimulation of protein synthesis in the splanchnic area; mainly liver. An altered splanchnic extraction of amino acids as well as an anabolic resistance to dietary protein, related to stress, disuse and aging play a key role in the pathogenesis of muscle wasting in these conditions. To overcome these factors, specific dietary protein and amino acid diets have been introduced. The main focus of these diets is the quantity and quality of dietary proteins and whether a balanced mixture or solely dietary essential amino acids are required with or without higher intake levels of specific amino acids. Specifically in cancer patients, stimulated muscle protein synthesis has been obtained by increasing the amount of protein in a meal and by providing additional leucine. Also in other chronic diseases such as chronic obstructive pulmonary disease and cystic fibrosis, meals with specific dietary proteins and specific combinations of dietary essential amino acids are able to stimulate anabolism. In acute diseases, a special role for the amino acid arginine and its precursor citrulline as anabolic drivers has been observed. Thus, there is growing evidence that modifying the dietary amino acid composition of a meal will positively influence the net balance between muscle protein synthesis and breakdown, leading to muscle protein anabolism in a variety of chronic and acute disease states. Specific amino acids with anabolic potential are leucine, arginine and citrulline.
The British journal of nutrition 08/2012; 108(S2):S139-S148. · 3.45 Impact Factor
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ABSTRACT: BACKGROUND & AIMS: Nutritional failure in children with cystic fibrosis (CF) has a negative effect on their morbidity and survival. It is unknown if determination of fat-free mass is a better screening method for nutritional failure than the currently recommended body mass index (BMI) alone. METHODS: This cross-sectional study in 77 children with CF (age: 14.8 ± 2.9 y) measured fat-free mass, fat mass, bone mineral content and density using dual-energy X-ray absorptiometry. Nutritional failure was defined as BMI <10 percentile and/or fat-free mass index <5th percentile. Statistics were done using ANOVA and t-tests. RESULTS: Thirty-one percent (31%) of the patients with CF was characterized by nutritional failure, and 14% had low fat-free mass index with preserved values for BMI (hidden depletion). Only 52% of the patients with fat-free mass depletion was detected when using the criteria BMI <10 percentile. Patients with fat-free mass depletion had reduced values for forced expiratory volume in 1 s (FEV(1)), independent of body mass index (P < 0.05), and lower values for bone mineral density in whole body, spine and hip, and spine bone mineral apparent density (P < 0.01). BMI ≤20 percentile was associated with a large drop in fat-free mass, a reduced FEV(1), and in bone mineral loss. CONCLUSIONS: Depletion of fat-free mass enhances morbidity in children with CF and is undetected in many of these children when only BMI percentile is used as screening method. BMI percentile of 20 should be considered as the new critical threshold for nutritional failure in CF if body composition techniques are not available.
Clinical nutrition (Edinburgh, Scotland) 05/2012; · 3.27 Impact Factor
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ABSTRACT: Exercise is known to improve physical functioning and health status in Chronic Obstructive Pulmonary Disease (COPD). Recently, disturbances in protein turnover and amino acid kinetics have been observed after exercise in COPD. The objective was to investigate which dairy protein is able to positively influence the protein metabolic response to exercise in COPD. 8 COPD patients and 8 healthy subjects performed a cycle test on two days while ingesting casein or whey protein. Whole body protein breakdown (WbPB), synthesis (WbPS), splanchnic amino acid extraction (SPE), and NetWbPS (=WbPS-WbPB) were measured using stable isotope methodology during 20 min of exercise (at 50% peak work load of COPD group). The controls performed a second exercise test at the same relative workload. Exercise was followed by 1 h of recovery. In the healthy group, WbPS, SPE, and NetPS were higher during casein than during whey feeding (P<.01). WbPS and NetPS were higher during exercise, independent of exercise intensity (P<.01). NetPS was higher during casein feeding in COPD due to lower WbPB (P<.05). Higher SPE was found during exercise during casein and whey feeding in COPD (P<.05). Lactate levels during exercise were higher in COPD (P<.05) independent of the protein. Post-exercise, lower NetPS values were found independent of protein type in both groups. Casein resulted in more protein anabolism than whey protein which was maintained during and following exercise in COPD. Optimizing protein intake might be of importance for muscle maintenance during daily physical activities in COPD.
Metabolism: clinical and experimental 04/2012; 61(9):1289-300. · 2.59 Impact Factor
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Vikram Sharma,
Gabriella A M Ten Have,
Lars Ytrebo,
Sambit Sen,
Christopher F Rose,
R Neil Dalton,
Charles Turner,
Arthur Revhaug,
Hans M H van-Eijk, Nicolaas E P Deutz,
Rajiv Jalan,
Rajeshwar P Mookerjee,
Nathan A Davies
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ABSTRACT: In acute liver failure (ALF), the hyperdynamic circulation is believed to be the result of overproduction of nitric oxide (NO) in the splanchnic circulation. However, it has been suggested that arginine concentrations (the substrate for NO) are believed to be decreased, limiting substrate availability for NO production. To characterize the metabolic fate of arginine in early-phase ALF, we systematically assessed its interorgan transport and metabolism and measured the endogenous NO synthase inhibitor asymmetric dimethylarginine (ADMA) in a porcine model of ALF. Female adult pigs (23-30 kg) were randomized to sham (N = 8) or hepatic devascularization ALF (N = 8) procedure for 6 h. We measured plasma arginine, citrulline, ornithine levels; arginase activity, NO, and ADMA. Whole body metabolic rates and interorgan flux measurements were calculated using stable isotope-labeled amino acids. Plasma arginine decreased >85% of the basal level at t = 6 h (P < 0.001), whereas citrulline and ornithine progressively increased in ALF (P < 0.001 and P < 0.001, vs. sham respectively). No difference was found between the groups in the whole body rate of appearance of arginine or NO. However, ALF showed a significant increase in de novo arginine synthesis (P < 0.05). Interorgan data showed citrulline net intestinal production and renal consumption that was related to net renal production of arginine and ornithine. Both plasma arginase activity and plasma ADMA levels significantly increased in ALF (P < 0.001). In this model of early-phase ALF, arginine deficiency or higher ADMA levels do not limit whole body NO production. Arginine deficiency is caused by arginase-related arginine clearance in which arginine production is stimulated de novo.
AJP Gastrointestinal and Liver Physiology 03/2012; 303(3):G435-41. · 3.43 Impact Factor
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ABSTRACT: Gut health relates to a diet with a high digestibility and quality. Limited data are available on the acute effects of low quality foods on gut metabolism and the consequences for liver metabolism.
A meal with the low quality protein gelatin (tryptophan deficient and low amount of essential amino acids) was compared to a meal with the high quality protein Whey and a tryptophan supplemented gelatin meal (Gel + TRP) in healthy pigs with chronic implanted catheters. In a conscious state, amino acid, ammonia, urea, glucose and lactate fluxes across the portal drained viscera (PDV) and liver were studied for 6 h after administration of the protein meal.
The average net portal appearance of amino acids was 99.8 ± 14.6% of the intake in the Gel group as compared to 61.4 ± 9.0% (p = 0.022) in the Whey group. In addition, a net portal appearance of tryptophan was observed in the Gel group (p = 0.005) of about 42% of tryptophan released in the Whey group. Intestinal energy metabolism and citrulline production was not affected. Adding tryptophan to the Gel meal diminished net portal AA appearance to 41.6 ± 24.0% of the intake (p = 0.012), but did not reduce the stimulated liver urea production.
In the post-prandial phase after intake of a low protein quality meal, net anabolism in the healthy intestine is absent. It is likely that the intestine responds with a net breakdown of endogenous (labile) proteins to secure amino acid availability for the body. Addition of the first limiting essential amino acid to this meal improved protein anabolism in the intestine. Protein quality of a meal is related to the anabolic response of the intestine during the meal.
Clinical nutrition (Edinburgh, Scotland) 10/2011; 31(2):273-82. · 3.27 Impact Factor
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ABSTRACT: Maintenance of muscle mass is crucial to improving outcome and quality of life in cancer patients. Stimulating muscle protein synthesis is the metabolic basis for maintaining muscle mass, but in cancer patients normal dietary intake has minimal effects on muscle protein synthesis. Adding leucine to high protein supplements stimulates muscle protein synthesis in healthy older subjects. The objective was to determine if a specially formulated medical food, high in leucine and protein, stimulates muscle protein synthesis acutely in individuals with cancer to a greater extent than a conventional medical food.
A randomized, controlled, double-blind, parallel-group design was used in 25 patients with radiographic evidence of cancer. Patients were studied before their cancer treatment was started or 4 weeks after their treatment was completed or halted. The fractional rate of muscle protein synthesis (FSR) was measured using the tracer incorporation technique with L-[ring-(13)C(6)]-phenylalanine. The experimental group (n = 13) received a medical food containing 40 g protein, based on casein and whey protein and enriched with 10% free leucine and other specific components, while the control group (n = 12) was given a conventionally used medical food based on casein protein alone (24 g). Blood and muscle samples were collected in the basal state and 5h hours after ingestion of the medical foods.
The cancer patients were in an inflammatory state, as reflected by high levels of C-reactive protein (CRP), IL-1 β and TNF-α, but were not insulin resistant (HOMA). After ingestion of the experimental medical food, plasma leucine increased to about 400 μM as compared to the peak value of 200 μM, after the control medical food (p < 0.001). Ingestion of the experimental medical food increased muscle protein FSR from 0.073 (SD: 0.023) to 0.097 (SD: 0.033) %/h (p = 0.0269). In contrast, ingestion of the control medical food did not increase muscle FSR; 0.073 (SD: 0.022) and 0.065 (SD: 0.028) %/h.
In cancer patients, conventional nutritional supplementation is ineffective in stimulating muscle protein synthesis. This anabolic resistance can be overcome with a specially formulated nutritional supplement.
Clinical nutrition (Edinburgh, Scotland) 06/2011; 30(6):759-68. · 3.27 Impact Factor
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ABSTRACT: Partial flap loss is caused by the incapability of the vascular pedicle to provide sufficient microvascular perfusion in distal segments of the flap in addition to the reperfusion injury that occurs in the whole flap after free tissue transfer. In experimental studies, the amino acid arginine reduces reperfusion injury and improves microvascular perfusion. The purpose of this clinical study was to explore the effect of arginine in free flap surgery.
In this randomized, double blind, placebo-controlled trial, 20 patients with unilateral breast reconstruction using the free transverse rectus abdominis myocutaneous flap were included. Patient and flap data were recorded. Patients received a continuous intravenous infusion of arginine or the control amino acid alanine for 5 days. Microcirculation was recorded in the flap in a standardized fashion using laser Doppler flowmetry (Perimed).
Zone IV microcirculatory blood flow postoperatively was higher in the arginine group than in the alanine control group (p = 0.04).
The authors' study shows beneficial effects of intravenous therapy with arginine to improve microcirculation in the free transverse rectus abdominis myocutaneous flap.
Plastic and reconstructive surgery 06/2011; 127(6):2216-23. · 2.74 Impact Factor
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AJP Endocrinology and Metabolism 05/2011; 301(2):E264-6. · 4.75 Impact Factor
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ABSTRACT: Dietary protein intake is known to affect whole body and interorgan protein turnover. We examined if moderate-nitrogen and carbohydrate casein and soy meals have a different effect on skeletal muscle protein and amino acid kinetics in healthy young subjects.
Muscle protein and amino acid kinetics were measured in the postabsorptive state and during 4-h enteral intake of isonitrogenous [0.21 g protein/(kg body weight. 4 h)] protein-based test meals, which contained either casein (CAPM; n = 12) or soy protein (SOPM; n = 10) in 2 separate groups. Stable isotope and muscle biopsy techniques were used to study metabolic effects.
The net uptake of glutamate, serine, histidine, and lysine across the leg was larger during CAPM than during SOPM intake. Muscle concentrations of glutamate, serine, histidine, glutamine, isoleucine and BCAA changed differently after CAPM and SOPM (P < 0.05). Muscle net protein breakdown decreased significantly (P < 0.05) to zero during feeding of both CAPM and SOPM, but differences in their (net) breakdown rates were not significant. Muscle protein synthesis was not different between CAPM and SOPM.
Moderate-nitrogen casein and soy protein meals differently alter leg amino acid uptake without a significant difference in influencing acute muscle protein metabolism.
Clinical nutrition (Edinburgh, Scotland) 02/2011; 30(1):65-72. · 3.27 Impact Factor
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AJP Endocrinology and Metabolism 10/2010; 299(4):E683; author reply E684. · 4.75 Impact Factor
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John E Morley,
Josep M Argiles,
William J Evans,
Shalender Bhasin,
David Cella, Nicolaas E P Deutz,
Wolfram Doehner,
Ken C H Fearon,
Luigi Ferrucci,
Marc K Hellerstein, [......],
Neil MacDonald,
Kathleen Mulligan,
Maurizio Muscaritoli,
Piotr Ponikowski,
Mary Ellen Posthauer,
Filippo Rossi Fanelli,
Morrie Schambelan,
Annemie M W J Schols,
Michael W Schuster,
Stefan D Anker
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ABSTRACT: The Society for Sarcopenia, Cachexia, and Wasting Disease convened an expert panel to develop nutritional recommendations for prevention and management of sarcopenia. Exercise (both resistance and aerobic) in combination with adequate protein and energy intake is the key component of the prevention and management of sarcopenia. Adequate protein supplementation alone only slows loss of muscle mass. Adequate protein intake (leucine-enriched balanced amino acids and possibly creatine) may enhance muscle strength. Low 25(OH) vitamin D levels require vitamin D replacement.
Journal of the American Medical Directors Association 07/2010; 11(6):391-6. · 4.64 Impact Factor
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Youji He,
Theodorus B M Hakvoort,
S Eleonore Köhler,
Jacqueline L M Vermeulen,
D Rudi de Waart,
Chiel de Theije,
Gabrie A M ten Have,
Hans M H van Eijk,
Cindy Kunne,
Wilhelmina T Labruyere,
Sander M Houten,
Milka Sokolovic,
Jan M Ruijter, Nicolaas E P Deutz,
Wouter H Lamers
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ABSTRACT: The main endogenous source of glutamine is de novo synthesis in striated muscle via the enzyme glutamine synthetase (GS). The mice in which GS is selectively but completely eliminated from striated muscle with the Cre-loxP strategy (GS-KO/M mice) are, nevertheless, healthy and fertile. Compared with controls, the circulating concentration and net production of glutamine across the hindquarter were not different in fed GS-KO/M mice. Only a approximately 3-fold higher escape of ammonia revealed the absence of GS in muscle. However, after 20 h of fasting, GS-KO/M mice were not able to mount the approximately 4-fold increase in glutamine production across the hindquarter that was observed in control mice. Instead, muscle ammonia production was approximately 5-fold higher than in control mice. The fasting-induced metabolic changes were transient and had returned to fed levels at 36 h of fasting. Glucose consumption and lactate and ketone-body production were similar in GS-KO/M and control mice. Challenging GS-KO/M and control mice with intravenous ammonia in stepwise increments revealed that normal muscle can detoxify approximately 2.5 micromol ammonia/g muscle.h in a muscle GS-dependent manner, with simultaneous accumulation of urea, whereas GS-KO/M mice responded with accumulation of glutamine and other amino acids but not urea. These findings demonstrate that GS in muscle is dispensable in fed mice but plays a key role in mounting the adaptive response to fasting by transiently facilitating the production of glutamine. Furthermore, muscle GS contributes to ammonia detoxification and urea synthesis. These functions are apparently not vital as long as other organs function normally.
Journal of Biological Chemistry 03/2010; 285(13):9516-24. · 4.77 Impact Factor
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Youji He,
Theodorus B. M. Hakvoort,
S. Eleonore Köhler,
Jacqueline L. M. Vermeulen,
D. Rudi de Waart,
Chiel de Theije,
Gabrie A. M. ten Have,
Hans M. H. van Eijk,
Cindy Kunne,
Wilhelmina T. Labruyere,
Sander M. Houten,
Milka Sokolovic,
Jan M. Ruijter, Nicolaas E. P. Deutz,
Wouter H. Lamers
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ABSTRACT: The main endogenous source of glutamine is de novo synthesis in striated muscle via the enzyme glutamine synthetase (GS). The mice in which GS is selectively but completely
eliminated from striated muscle with the Cre-loxP strategy (GS-KO/M mice) are, nevertheless, healthy and fertile. Compared
with controls, the circulating concentration and net production of glutamine across the hindquarter were not different in
fed GS-KO/M mice. Only a ∼3-fold higher escape of ammonia revealed the absence of GS in muscle. However, after 20 h of fasting,
GS-KO/M mice were not able to mount the ∼4-fold increase in glutamine production across the hindquarter that was observed
in control mice. Instead, muscle ammonia production was ∼5-fold higher than in control mice. The fasting-induced metabolic
changes were transient and had returned to fed levels at 36 h of fasting. Glucose consumption and lactate and ketone-body
production were similar in GS-KO/M and control mice. Challenging GS-KO/M and control mice with intravenous ammonia in stepwise
increments revealed that normal muscle can detoxify ∼2.5 μmol ammonia/g muscle·h in a muscle GS-dependent manner, with simultaneous
accumulation of urea, whereas GS-KO/M mice responded with accumulation of glutamine and other amino acids but not urea. These
findings demonstrate that GS in muscle is dispensable in fed mice but plays a key role in mounting the adaptive response to
fasting by transiently facilitating the production of glutamine. Furthermore, muscle GS contributes to ammonia detoxification
and urea synthesis. These functions are apparently not vital as long as other organs function normally.
Journal of Biological Chemistry 03/2010; 285(13):9516-9524. · 4.77 Impact Factor
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Lars M. Ytrebø,
Sambit Sen,
Christopher Rose,
Nathan A. Davies,
Geir I. Nedredal,
Ole-Martin Fuskevaag,
Gabrie A. M. Ten Have,
Frits W. Prinzen,
Roger Williams, Nicolaas E. P. Deutz,
Rajiv Jalan,
Arthur Revhaug
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ABSTRACT: Objective. Acute liver failure (ALF) is haemodynamically characterized by a hyperdynamic circulation. The aims of this study were to investigate the systemic and regional haemodynamics in ALF, to measure changes in nitric oxide metabolites (NOx) and to evaluate whether these haemodynamic disturbances could be attenuated with albumin dialysis. Material and methods. Norwegian Landrace pigs (23–30 kg) were randomly allocated to groups as controls (sham-operation, n=8), ALF (hepatic devascularization, n=8) and ALF + albumin dialysis (n=8). Albumin dialysis was started 2 h after ALF induction and continued for 4 h. Systemic and regional haemodynamics were monitored. Creatinine clearance, nitrite/nitrate and catecholamines were measured. A repeated measures ANOVA was used to analyse the data. Results. In the ALF group, the cardiac index increased (PGT<0.0001), while mean arterial pressure (PG=0.02) and systemic vascular resistance decreased (PGT<0.0001). Renal resistance (PG=0.04) and hind-leg resistance (PGT=0.003) decreased in ALF. There was no difference in jejunal blood flow between the groups. ALF pigs developed renal dysfunction with increased serum creatinine (PGT=0.002) and decreased creatinine clearance (P=0.02). Catecholamines were significantly higher in ALF, but NOx levels were not different. Albumin dialysis did not attenuate these haemodynamic or renal disturbances. Conclusions. The haemodynamic disturbances during the early phase of ALF are characterized by progressive systemic vasodilatation with no associated changes in metabolites of NO. Renal vascular resistance decreased and renal dysfunction developed independently of changes in renal blood flow. After 4 h of albumin dialysis there was no attenuation of the haemodynamic or renal disturbances.
07/2009; 41(11):1350-1360.
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ABSTRACT: Previous research has shown that low central serotonin, induced by acute tryptophan depletion (ATD), results in depressed mood and impairs cognition in healthy volunteers with a predisposition for depression. It remains unknown whether ATD affects emotional processing via mood changes or directly. In the present study we investigated the interaction between vulnerability for depression and the effect of ATD on mood, cognition and the associated brain activation. In a previous functional MRI study, we tested the effect of ATD during a combined cognitive and emotional Stroop task in healthy women without a family history of depression (FH-). In this study, we present the data of an additional group of 12 healthy women with a positive family history of unipolar depression (FH+). The effect of ATD on mood and Stroop performance was different for the FH+ group as compared with the FH- group. Scores on the depression sub-scale of the Profile of Mood States (POMS) did not correlate with performance changes, but did correlate with the anterior cingulate cortex response during Stroop interference. This study showed that a family history of unipolar depression interacts with the effect of ATD.
Psychiatry Research 06/2009; 173(1):52-8. · 2.52 Impact Factor
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ABSTRACT: Dietary protein plays a role in body weight regulation, partly because of its effects on appetite. The objective was to compare the effects of high or normal casein-, soy-, or whey-protein breakfasts on appetite, specific hormones, amino acid responses and subsequent energy intake. Twenty-five healthy subjects (mean+/-SEMBMI:23.9+/-0.3 kg/m2; age:22+/-1 years) received standardized breakfasts: custards with either casein-, soy, or whey-protein with either 10/55/35 (normal) or 25/55/20 (high)En% protein/carbohydrate/fat in a randomized, single-blind design. Appetite profile (Visual Analogue Scales) and amino acid concentrations were determined for 4 h whereas plasma glucose, insulin, active Glucagon-like Peptide 1 (GLP-1), and active ghrelin concentrations were determined for 3 h; the sensitive moment for lunch was determined. Subjects returned for a second set of experiments and received the same breakfasts, ad lib lunch was offered 180 min later; energy intake (EI) was assessed. At 10En%, whey decreased hunger more than casein or soy (p <0.05), coinciding with higher leucine, lysine, tryptophan, isoleucine, and threonine responses (p<0.05). At 25En% there were no differences in appetite ratings. Whey triggered the strongest responses in concentrations of active GLP-1 (p<0.05) and insulin (p<0.05) compared with casein and/or soy. There were no differences in EI. In conclusion, differences in appetite ratings between different proteins appeared at a normal concentration; at 10En% whey-protein decreased hunger more than casein- or soy-protein. At 25En% whey-protein triggered stronger responses in hormone concentrations than casein- or soy-protein. The results suggest that a difference in appetite ratings between types of protein appears when certain amino acids are above and below particular threshold values.
Physiology & Behavior 04/2009; 96(4-5):675-82. · 2.87 Impact Factor
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ABSTRACT: Dietary protein plays a role in body weight regulation, partly due to its effects on satiety. The objective was to compare the effects of casein-, soy-, whey-, whey without glycomacropeptide (GMP)-, alpha-lactalbumin-, gelatin-, or gelatin with tryptophan (TRP)-protein breakfasts at two concentrations on subsequent satiety and energy intake (EI).
Twenty-four healthy subjects (mean+/-SEM BMI: 24.8+/-0.5 kg/m(2); age: 25+/-2 years) received a breakfast; a custard with casein, soy, whey, whey-GMP, alpha-lactalbumin, gelatin, or gelatin+TRP as protein source with either 10/55/35 (normal) or 25/55/20 (high) En% protein/carbohydrate/fat in a randomized, single-blind design. At the precedingly determined time point for lunch, 180 min, subjects were offered an ad lib lunch. Appetite profile (Visual Analogue Scales, VAS) and EI were determined.
Both at the level of 10 and 25 En% from protein, EI at lunch was approximately 20% lower after an alpha-lactalbumin or gelatin (+TRP) breakfast (2.5+/-0.2 MJ) compared with after a casein, soy, or whey-GMP breakfast (3.2+/-0.3 MJ, p<0.05). Appetite ratings at 180 min differed 15-25 mm (approximately 40%, p<0.05) between types of protein. Differences in EI were a function of differences in appetite ratings (R(2)=0.4, p<0.001).
Different proteins (alpha-lactalbumin, gelatin, gelatin+TRP) that are approximately 40% more satiating than other proteins (casein, soy, whey, whey-GMP) induce a related approximately 20% reduction of subsequent energy intake.
Clinical nutrition (Edinburgh, Scotland) 01/2009; 28(2):147-55. · 3.27 Impact Factor
