Dietary pectin stimulates protein metabolism in the digestive tract

OBJECTIVE: The aim of this study was to determine if protein metabolism was altered in small and large intestines by feeding pectin, a soluble fiber known to stimulate cecal production of short-chain fatty acids (SCFAs) and to have a trophic effect in these tissues. METHODS: Twenty-four weanling male Sprague-Dawley rats were fed ad libitum for 14 d with a balanced control diet or an isoproteic, isocaloric pectin (citrus) diet (80 g/kg). SCFA production, intestinal histomorphometry, and protein synthesis were determined in the proximal and distal parts of the small intestine, the cecum, and the colon. Protein synthesis rates were determined by measuring the (13)C valine incorporation rate in tissue proteins. RESULTS: Pectin feeding slightly decreased food intake and growth rate. It increased the acetate, propionate, and butyrate pools in the cecum. Pectin feeding resulted in heavier intestinal tissues corresponding to higher villus height in the small intestine and crypt depth in the small and large intestines compared with feeding of the control diet. Compared with the control group, the rats fed the pectin diet had significantly higher protein synthesis rates in all the parts of their intestines. CONCLUSION: Supplementation of pectin, as a soluble fiber, in the diets, stimulated SCFA production, had a trophic effect on the different parts of the intestines, and greatly stimulated protein synthesis in those tissues.     

Decreased whole-body and splanchnic glutamate metabolism in healthy elderly men and patients with chronic obstructive pulmonary disease in the postabsorptive state and in response to feeding

Decreased plasma and muscle glutamate concentrations have been observed in patients with chronic obstructive pulmonary disease (COPD), suggesting disturbances in glutamate metabolism. The present study was conducted to further examine glutamate metabolism in 8 male COPD patients (68 +/- 4 y) by measurement of whole-body (WB) glutamate production and splanchnic glutamate extraction in the postabsorptive state as well as in response to feeding. Because COPD is particularly prevalent in the elderly and aging per se may also affect glutamate metabolism, 2 male control groups were included: 8 healthy elderly (63 +/- 3 y) and 8 young (22 +/- 1 y) subjects. On 2 test days, the stable isotope L-15N-glutamate was infused i.v. or enterally according to a primed constant and continuous infusion protocol. After 90 min of infusion, subjects ingested a carbohydrate-protein drink (28% milk protein, 72% maltodextrin) every 20 min for 2 h. Arterialized-venous blood samples were taken at the end of the postabsorptive and feeding periods. Postabsorptive WB glutamate production and splanchnic glutamate extraction were significantly lower in the elderly and COPD patients than in the young (P < 0.01). Feeding further decreased WB endogenous glutamate production in the elderly and COPD patients, with COPD patients tending (P = 0.07) to have a greater decrease. Splanchnic glutamate extraction increased during feeding in the elderly (P < 0.05) but did not change in COPD patients. In conclusion, aging reduces postabsorptive WB endogenous glutamate production and splanchnic glutamate extraction. COPD does not affect postabsorptive WB glutamate metabolism but may influence splanchnic glutamate metabolism during feeding.     

Casein and soy protein meals differentially affect whole-body and splanchnic protein metabolism in healthy humans

Dietary protein quality is considered to be dependent on the degree and velocity with which protein is digested, absorbed as amino acids, and retained in the gut as newly synthesized protein. Metabolic animal studies suggest that the quality of soy protein is inferior to that of casein protein, but confirmatory studies in humans are lacking. The study objective was to assess the quality of casein and soy protein by comparing their metabolic effects in healthy human subjects. Whole-body protein kinetics, splanchnic leucine extraction, and urea production rates were measured in the postabsorptive state and during 8-h enteral intakes of isonitrogenous [0.42 g protein/(kg body weight . 8 h)] protein-based test meals, which contained either casein (CAPM; n = 12) or soy protein (SOPM; n = 10) in 2 separate groups. Stable isotope techniques were used to study metabolic effects. With enteral food intake, protein metabolism changed from net protein breakdown to net protein synthesis. Net protein synthesis was greater in the CAPM group than in the SOPM group [52 +/- 14 and 17 +/- 14 nmol/(kg fat-free mass (FFM) . min), respectively; P < 0.02]. Urea synthesis rates decreased during consumption of both enteral meals, but the decrease tended to be greater in the subjects that consumed CAPM (P = 0.07). Absolute splanchnic extraction of leucine was higher in the subjects that consumed CAPM [306 +/- 31 nmol/(kg FFM . min)] vs. those that consumed SOPM [235 +/- 29 nmol/(kg FFM . min); P < 0.01]. In conclusion, a significantly larger portion of soy protein is degraded to urea, whereas casein protein likely contributes to splanchnic utilization (probably protein synthesis) to a greater extent. The biological value of soy protein must be considered inferior to that of casein protein in humans.     

Enhanced anabolic response to milk protein sip feeding in elderly subjects with COPD is associated with a reduced splanchnic extraction of multiple amino acids

BACKGROUND & AIMS: We previously observed in elderly subjects with Chronic Obstructive Pulmonary Disease (COPD) an enhanced anabolic response to milk protein sip feeding, associated with reduced splanchnic extraction (SPE) of phenylalanine. Milk proteins are known for their high Branched-chain Amino Acids (BCAA) content, but no information is present about splanchnic extraction and metabolism of the individual BCAA in COPD. OBJECTIVE: To investigate whether BCAA metabolism and SPE of the individual BCAA are altered in COPD during milk protein sip feeding. DESIGN: In elderly subjects with COPD and in healthy age-matched elderly SPE, endogenous rate of appearance (Raendo) of the leucine (LEU), isoleucine (ILE) and valine (VAL) were measured before and during sip feeding of a Whey protein meal. To study the effect of aging, the healthy elderly were compared to a group of healthy young subjects. Stable isotopes of l-[(2)H(3)]-LEU, l-[1-(13)C]-ILE and l-[1-(13)C]-VAL were given on two separate test days orally or intravenously. Simultaneously, l-[ring-(2)H(5)]-phenylalanine (PHE) and l-[ring-(2)H(2)]-tyrosine (TYR) were given to determine the whole body protein breakdown (WbPB), synthesis (WbPS) and NetPS. RESULTS: SPE of all BCAA, TYR, and PHE (p?相似文献   

Approaches to quantifying protein metabolism in response to nutrient ingestion

The investigation of protein metabolism under various nutritional and physiological conditions has been made possible by the use of indirect, principally tracer-based methods. Most studies were conducted at the whole-body level, mainly using steady-state isotopic techniques and equations based on simple two-pool models, in which amino acids are either free or protein bound. Because whole-body methods disregard regional contributions to protein metabolism, some regional approaches have tried to distinguish the distribution of protein kinetics in the different tissues. The organ-balance tracer technique, involving the arteriovenous catheterization of regions or organs with concomitant isotopic tracer infusion, distinguishes between amino acid uptake and release in the net amino acid balance and measures protein synthesis and degradation under steady-state conditions. Last, the importance has become clear of the difference in dietary and endogenous amino acids recycled from proteolysis for anabolic and catabolic pathways. In humans, the dual tracer technique, which consists of the simultaneous oral/enteral administration and intravenous infusion of different tracers of the same amino acid, allows an estimate of the splanchnic uptake of amino acids administered. Furthermore, the whole-body retention of labeled dietary nitrogen after the ingestion of a single protein meal has enabled a clearer understanding of the metabolic fate of dietary amino acids. Based on such data, a newly developed compartmental model provides a simulation of the regional distribution and metabolism of ingested nitrogen in the fed state by determining its dynamic fate through free and protein-bound amino acids in both the splanchnic and peripheral areas in humans.     

Brain nucleic acid composition and fractional rates of protein synthesis in response to chronic ethanol feeding: Comparison with skeletal muscle

Brain atrophy is a common feature of chronic alcohol misuse, although the pathogenic mechanisms are unknown. We propose that defects in protein synthesis are contributing events. To test this hypothesis the experimental effects of chronic (i.e., 2 and 3 weeks) ethanol feeding on brain nucleic acid composition and rates of protein synthesis in vivo were investigated. These were compared with those of skeletal muscle (represented by the plantaris). Male Wistar rats, used at mean body weights of either 82 g (first study for 2 weeks) or 93 g (second study for 3 weeks) were fed a nutritionally complete liquid diet in which ethanol comprised a third of the total calories. Control rats were pair-fed identical amounts of the same diet, in which ethanol was substituted by isoenergetic glucose. At 2 weeks there were small reductions (i.e., approximately 5–10%) in the weight of the whole brain, cortex, and brain stem. Ethanol-induced reductions in the total protein content of the brain stem was found at 2 weeks, although these changes did not achieve significance. At 3 weeks the weights of whole brain were significantly reduced compared to a greater reduction in skeletal muscle weights. Total protein contents were reduced at 3 weeks in the whole brain and skeletal muscle. At 2 weeks there were decreases in the RNA contents of the cortex, brain stem, and entire brain. There were also reductions in cerebellum RNA composition only when expressed relative to DNA. The DNA composition of the brain was relatively unaffected by chronic ethanol feeding. At 3 weeks, total RNA and DNA were reduced in the whole brain and muscle. Fractional rates of protein synthesis (i.e., the percentage of tissue protein pool renewed each day) in the brain were unaltered after 3 weeks of ethanol feeding, but were reduced in skeletal muscles, largely as a consequence of reduced RNA composition. In conclusion, only moderate changes in the brain were found in ethanol feeding. These data can be compared to skeletal muscle, which shows that ethanol induces profound reductions in protein, RNA, and protein synthesis rates.     

The effect of protein levels on the response of weanling rats to dietary pectin

We have previously proposed that the inhibiting effects of pectin on feed consumption and growth might be due in part to the reduction it causes in protein digestibility. The present work was intended to test this hypothesis by feeding higher levels of protein in order to compensate for the lower digestibility. We fed diets containing 10, 20 and 30% casein (initial levels) and 0, 4.8, 16.7 and 28.6% pectin (by diet dilution). Despite the higher casein levels, pectin strongly inhibited the animals' feed intake, growth, protein efficiency ratio (PER), net protein ratio (NPR) and net protein utilization (NPU) as well as protein and energy digestibilities. Apart from determining the base (zero pectin) level of the various parameters measured, the dietary casein level in itself did not influence the effect of pectin on feed intake, digestible energy intake, protein digestibility, body weight growth or parameters of protein utilization such as PER, NPR and NPU. We thus cannot conclude that these effects of pectin were to any major extent secondary to the reduction in protein digestibility observed in these animals.     

The effect of intake on protein metabolism across splanchnic tissues in growing beef steers

The contribution of the total splanchnic tissue (TSP; portal-drained viscera (PDV) plus liver) to whole-body protein metabolism was estimated in relation to intake (0.6, 1.0 and 1.6 x maintenance requirements), in six multicatheterized growing beef steers used in a double 3 x 3 Latin square design. At the end of each 21 d experimental period, [1-13C]leucine was infused into a jugular vein (1.05 mmol/h for 5 h, preceded by a priming dose of 1.05 mmol). Arterial, portal and hepatic blood samples were collected hourly during the infusion. The increment in TSP leucine irreversible loss rate (ILR) observed with increasing intake reached significance (P < 0.10) only for PDV, while whole-body ILR increased markedly (P < 0.001) with intake. The relative contribution of TSP to whole-body leucine ILR averaged 44% (25% from PDV and 19% from the liver). Although these proportions were not affected by intake, on an incremental basis more than 70% of the increase of whole-body leucine ILR between the 0.6 and 1.0 x maintenance originated from the changes in TSP ILR, while the corresponding value was below 13% between 1.0 and 1.6 x maintenance. Total whole-body leucine oxidation and fractional oxidation increased (P < 0.05) with intake. Protein retention increased with intake (P < 0.01), as a result of a greater increase in protein synthesis compared with protein degradation. Protein breakdown had a major impact on protein turnover as 65% of the protein synthesized was degraded when intake varied from 1.0 to 1.6 x maintenance. Net leucine portal absorption increased (P < 0.001) with intake and represented 1, 16 and 23% of whole body leucine ILR, for 0.6, 1.0 and 1.6 x maintenance, respectively. Although leucine oxidation was not a major component of whole body ILR (9.3-19.9%), it represented 69% of the net available leucine (portal absorption) even at 1.6 x maintenance. The lower relative contribution of the TSP to whole-body leucine ILR at higher intake indicates the proportional increase in the metabolic activity of peripheral tissues as the animals moved into positive protein balance.     

Pulse protein feeding pattern restores stimulation of muscle protein synthesis during the feeding period in old rats

Muscle loss during aging could be related to a lower sensitivity of muscle protein synthesis to feeding. To overcome this decrease without increasing protein intake, we proposed to modulate the daily protein feeding pattern. We showed that consuming 80% of dietary proteins at noon (pulse pattern) improved nitrogen balance in elderly women. The present study was undertaken in rats to determine which tissues are the targets of the pulse pattern and what mechanisms are involved. Male Sprague-Dawley 11- and 23-mo-old rats (n = 32 per age) were fed 4 isoproteic (18% protein) meals/d for 10 d. Then half of the rats at each age were switched to a 11/66/11/11% repartition of daily proteins (pulse pattern) for 21 d. On d 21, rats were injected with a flooding dose of L-(13)C-valine (50 atom% excess, 150 micromol/100 g body) and protein synthesis rates were measured in liver, small intestine and gastrocnemius muscle in either the postabsorptive or the fed state. Epitrochlearis muscle degradation rates and plasma amino acid concentrations were measured at the same times. The pulse pattern had the following effects: 1) it significantly increased liver protein synthesis response to feeding and postprandial plasma amino acid concentrations at both ages; 2) it restored a significant response to feeding of gastrocnemius muscle protein synthesis in old rats; and 3) it had no effect in small intestine or on muscle breakdown. Thus, using a pulse pattern could be useful in preventing the age-related loss of muscle by increasing feeding-induced stimulation of muscle protein synthesis.     

Skeletal muscle protein metabolism and resistance exercise

Stable isotope tracer techniques have been developed to quantify rates of muscle protein synthesis and breakdown in human subjects. These methods were applied to the study of the response to resistance exercise as well as to amino acid intake. The fractional synthetic rate (FSR) of muscle protein is stimulated for as long as 48 h following exercise. However, the anabolic effect of the stimulation of FSR after exercise is blunted by a simultaneous increase in muscle protein breakdown, such that the net balance between synthesis and breakdown remains negative in the fasted state. Elevation of plasma amino acids stimulates muscle protein synthesis. The extent of the stimulation is dependent on the dose, the profile of amino acids given, the pattern of ingestion (bolus vs. constant intake), the age of the subject, and the hormonal profile. Importantly, there is an interactive effect between resistance exercise and amino acids, such that the net anabolic response to amino acids following exercise is greater than the sum of the amino acid effects and the exercise effects alone.     

Chronic inflammation alters protein metabolism in several organs of adult rats

Despite the prevalence of chronic inflammatory diseases in developed countries, few studies have considered the metabolic alterations observed in these disorders. To determine which perturbations in protein metabolism occur during chronic inflammation, and the consequences they have on nutritional requirements, a model of ulcerative colitis was adapted for use in adult rats. Adult Sprague-Dawley male rats (9 mo old) received dextran sulfate sodium (DSS) in their drinking water at 50 g/L for 9 d, then at 20 g/L for 18 d. A group of control rats, matched for age and weight, was pair-fed to the treated rats. DSS induced body weight loss and chronic inflammation characterized by an increase of spleen, liver, ileum and colon weights, of blood leukocytes and acute-phase protein levels. The main inflammatory site was the colon, which presented characteristic histological alterations and increased myeloperoxydase activity. Inflammation was accompanied by oxidative stress, characterized by increased plasma protein carbonyl content and increased liver glutathione concentration, but decreased glutathione concentration in muscle. This DSS-induced colitis led to a stimulation of protein synthesis in spleen (+223%), ileum (+40%) and colon (+63%). By contrast, protein synthesis in muscle slowed down (-23%). In conclusion, like acute inflammation, chronic inflammation induced a stimulation of protein metabolism in several splanchnic organs. In muscle, both protein synthesis and degradation were reduced. Taken together, these data are consistent with inadequate amino acid supply to meet the increased requirement resulting from chronic inflammation.     

Adrenergic control of protein metabolism in skeletal muscle

This review summarizes evidence indicating that the sympathetic nervous system, through hormonal and neurotransmitter actions, produces anabolic, protein-sparing effects on skeletal muscle protein metabolism. Studies are reviewed which indicate that catecholamines secreted by the adrenal medulla have an inhibitory effect on muscle Ca(2+)-dependent protein degradation independently of other hormones. In addition, norepinephrine released from adrenergic terminals may increase the rate of protein synthesis in oxidative muscles, leading to increased protein accretion. Evidence is also presented that these effects seem to be mediated by beta(2)-adrenoceptors and cyclic adenosine monophosphate-dependent pathways. The understanding of the precise mechanisms by which endogenous catecholamines promote muscle anabolic effects may bring new perspectives for efficient treatment of muscle-wasting conditions and enhancement of growth efficacy in farm species.     

Exercise, protein metabolism, and muscle growth

Exercise has a profound effect on muscle growth, which can occur only if muscle protein synthesis exceeds muscle protein breakdown; there must be a positive muscle protein balance. Resistance exercise improves muscle protein balance, but, in the absence of food intake, the balance remains negative (i.e., catabolic). The response of muscle protein metabolism to a resistance exercise bout lasts for 24-48 hours; thus, the interaction between protein metabolism and any meals consumed in this period will determine the impact of the diet on muscle hypertrophy. Amino acid availability is an important regulator of muscle protein metabolism. The interaction of postexercise metabolic processes and increased amino acid availability maximizes the stimulation of muscle protein synthesis and results in even greater muscle anabolism than when dietary amino acids are not present. Hormones, especially insulin and testosterone, have important roles as regulators of muscle protein synthesis and muscle hypertrophy. Following exercise, insulin has only a permissive role on muscle protein synthesis, but it appears to inhibit the increase in muscle protein breakdown. Ingestion of only small amounts of amino acids, combined with carbohydrates, can transiently increase muscle protein anabolism, but it has yet to be determined if these transient responses translate into an appreciable increase in muscle mass over a prolonged training period.     

Regulation of skeletal muscle protein metabolism in catabolic states

PURPOSE OF REVIEW: This review highlights recent publications dealing with the nature of the in-vivo response of skeletal muscle to critical illness and approaches to attenuating this response. Studies focused on molecular mechanisms of muscle catabolism are not reviewed. RECENT FINDINGS: The general areas covered are the metabolic response to stress, particularly regarding the relationship between muscle protein breakdown, amino acid availability, and muscle protein synthesis. The impact of the profile of amino acids in the context of protein/amino acid intake is also discussed. Advances in our understanding of the hormonal response are considered, and use of insulin therapy to slow muscle catabolism is discussed. SUMMARY: Muscle catabolism is a fundamental response to severe stress, and the resulting amino acid efflux from muscle provides important precursors for protein synthesis in other parts of the body. The nature of this response (i.e. transport kinetics favoring efflux of amino acids from muscle) makes amelioration of the catabolic response of muscle with nutrition alone very difficult. Many approaches have been used to reverse catabolism, mostly involving various anabolic hormones. Recent studies using insulin therapy are particularly intriguing because of the low cost and powerful anabolic stimulus of insulin.