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PubMed1987

Regulation of xanthine oxidase activity and immunologically detectable protein in rats in response to dietary protein and iron.

To investigate the mechanism for changes in xanthine oxidase activity in response to dietary protein and iron, we fed rats diets containing 50, 20 or 5% casein with either normal iron (35 mg Fe/kg diet) or low iron (5 mg Fe/kg diet). Xanthine oxidase activity changed in liver and intestinal mucosa in response to protein and iron, but immunologically detectable xanthine oxidase protein did not change. When total liver RNA isolated from these rats was translated by a rabbit reticulocyte lysate, we found no difference in the amount of xanthine oxidase that was translated. These results demonstrated that the changes in xanthine oxidase activity were not accompanied by changes in the amount of protein. Since xanthine oxidase can exist in an inactive desulfo form, we asked if xanthine oxidase activity was changed by the content of sulfur-containing amino acids in the diet. Xanthine oxidase activity in intestinal mucosa of the rats fed the 5% casein + methionine diet was significantly greater than that of the rats fed the 5% casein diet alone. These findings suggest that xanthine oxidase activity may be regulated by interconversion of active and inactive desulfo enzyme.

Animals↗
PubMed1976

Protein absorption and ammonia production: the effects of dietary protein and removal of the colon.

1. The effect of increasing dietary protein content on the amount of faecal nitrogen was measured in six normal subjects and five subjects without functioning colons (three with ileostomy and two with ileo-rectal anastomosis). 2. There was a significant inontent in the subjects without functioning colons. 3. In normal subjects with intact colons, faceal N content was found to be lower than that in subjects without colons, and furthermore there was no significant variation with diet. 4. The source of the increase in faecal N with increased dietary protein content in subjects without functioning colons is discussed and the significance of these findings in relation to the efficiency of protein absorption is considered.

Ammonia↗
PubMed2003

Dietary protein, calcium metabolism, and skeletal homeostasis revisited.

High dietary protein intakes are known to increase urinary calcium excretion and, if maintained, will result in sustained hypercalciuria. To date, the majority of calcium balance studies in humans have not detected an effect of dietary protein on intestinal calcium absorption or serum parathyroid hormone. Therefore, it is commonly concluded that the source of the excess urinary calcium is increased bone resorption. Recent studies from our laboratory indicate that alterations in dietary protein can, in fact, profoundly affect intestinal calcium absorption. In short-term dietary trials in healthy adults, we fixed calcium intake at 20 mmol/d while dietary protein was increased from 0.7 to 2.1 g/kg. Increasing dietary protein induced hypercalciuria in 20 women [from 3.4 +/- 0.3 ( +/- SE) during the low-protein to 5.4 +/- 0.4 mmol/d during the high-protein diet]. The increased dietary protein was accompanied by a significant increase in intestinal calcium absorption from 18.4 +/- 1.3% to 26.3 +/- 1.5% (as determined by dual stable isotopic methodology). Dietary protein intakes at and below 0.8 g/kg were associated with a probable reduction in intestinal calcium absorption sufficient to cause secondary hyperparathyroidism. The long-term consequences of these low-protein diet-induced changes in mineral metabolism are not known, but the diet could be detrimental to skeletal health. Of concern are several recent epidemiologic studies that demonstrate reduced bone density and increased rates of bone loss in individuals habitually consuming low-protein diets. Studies are needed to determine whether low protein intakes directly affect rates of bone resorption, bone formation, or both.

Adult↗
PubMed1983

Effects of dietary protein level on hepatic microsomal mixed-function oxidase systems during aging in two generations of Syrian hamsters.

Syrian hamsters were fed one of three levels of lactalbumin (10, 20, or 40%) from 4 weeks of age. Parents (F0 generation) and their offspring (F1 generation) remained for life on the parental diet. Randomly selected hamsters from both generations were killed at 0, 6, 18, 30, and 60 weeks to evaluate hepatic microsomal drug metabolism systems. Microsomal protein content rose with increased dietary protein in both generations of females at 30 and 60 weeks and in both generations of males at 18 weeks. Microsomal protein rose during life, but the timing and magnitude of the increase varied with sex, diet, and generation. Cytochrome P-450 content increased with elevation in dietary protein at most measurement times in females and at all measurement times in F1 generation males. Hepatic aryl hydrocarbon hydroxylase (AHH) and aniline hydroxylase (ANH) activities were influenced by dietary protein, primarily at 6, 18, and 30 weeks, and these values tended to decline between maturity and senescence. AHH generally increased as dietary protein rose, except at 30 weeks, at which time the group fed the medium protein level usually had the highest activity. ANH activity was either elevated in groups fed the 20 or 40% lactalbumin levels or depressed in these groups at 6 and 18 weeks when these values were influenced by dietary protein. The effects depended upon sex and generation. Age effects on hepatic microsomal metabolism in hamsters varied by sex and dietary protein and were somewhat different than those reported for other rodents.

Aging↗
PubMed1999

Adaptation of protein metabolism in relation to limits to high dietary protein intake.

Studies of the effects of dietary protein level on human metabolism have usually concentrated on the effects of protein deprivation and on establishing a minimum dietary requirement. By contrast, less is known about the effects of very high protein diets, although general levels of protein intake in the developed world are increasing, and high protein diets have been advocated for maintaining or increasing muscle mass in certain groups of the population. This article, therefore, examines the response of protein metabolism to high dietary protein, studied in adults by nitrogen balance and isotopic tracer techniques, and concentrating on the evidence for increased lean body mass. It is concluded that high protein feeding initially results in protein retention, with greater cycling of body protein in response to meals, but that neither N-balance nor isotopic tracer methods possess sufficient sensitivity to detect whether a long term increase in functional lean tissue ensues. Improved methods of body composition measurement will be needed to establish this. Moreover, the absence of strong evidence that high protein diets confer any advantage in terms of strength or health must be weighed against potentially injurious consequences.

Adaptation, Physiological↗
PubMed2004

Isoenergetic dietary protein restriction decreases myosin heavy chain IIx fraction and myosin heavy chain production in humans.

The synthesis of muscle protein is restrained during dietary protein restriction. This is widely understood to vary quantitatively with the degree of nutritional deprivation, but there has been little discussion of qualitative changes in muscle protein deriving from dietary protein restriction. We studied 14 healthy subjects in a 2-sample study. Subjects were randomly assigned to a diet providing an ample, American-style protein intake (1.67 g. kg fat-free mass(-1). d(-1)) or a diet approximating the mean minimum adult protein requirement (0.71 g. kg fat-free mass(-1). d(-1)). We found that consumption of an isoenergetic diet at the mean adult minimum protein requirement for 4 wk produced an 81% lower fractional synthesis rate of myosin heavy chain (MHC) proteins in vastus lateralis muscle than did consumption of an ample protein diet (P = 0.05). Protein deprivation altered the skeletal muscle myosin composition such that the proportion of the total myosin content represented by fast-twitch MHC IIx was 51% lower than with ample intake (P = 0.013). The steady state content of MHC IIx messenger RNA (mRNA) did not differ in subjects consuming the minimum requirement of protein, suggesting that the reduced proportion of MHC IIx arises from posttranscriptional events. A 68% lower rate of 3-methylhistidine excretion with protein restriction (P < 0.01) suggests that myofibrillar protein degradation was lower. We conclude that dietary amino acid scarcity produces a change in myosin isoform distribution via posttranscriptional mechanisms. The relative contribution of inhibited myosin synthesis and inhibited degradation to the altered myosin isoform composition remains unknown. This has implications for the mechanisms by which amino acids govern muscle protein composition in vivo, and further exploration is required.

Adult↗
PubMed1988

The role of insulin and thyroid hormones in the regulation of muscle growth and protein turnover in response to dietary protein in the rat.

1. We have investigated the relations between changes in plasma insulin and 3,5,3'-triiodothyronine (T3), and muscle growth and protein turnover in the rat in response to diets of varying protein concentrations. 2. Young rats were fed ad lib. on a control (180 g casein/kg) diet or low-protein diets containing 80, 45 and 0 g casein/kg in four separate experiments. Measurements were made of food intakes, muscle and body-weight growth rates, muscle protein turnover in vivo, plasma insulin, and plasma free and total T3. 3. The food intakes of the 80 and 45 g casein/kg diet groups were variable, with the 80 g casein/kg diet group consuming either the same or more than the controls, and the 45 g casein/kg diet group consuming less or more than the controls. Body-weight and skeletal-muscle growth rates varied with the protein but not energy intakes, which in turn reflected both dietary composition and the food intake, with the hyperphagic 80 g casein/kg diet group of rats growing almost normally and the 0 g casein/kg diet group losing body-weight and muscle mass. 4. Changes in rates of muscle growth were accompanied by parallel changes in rates of protein synthesis and degradation, as well as parallel changes in concentrations of plasma insulin and free T3, to the extent that all these variables were highly correlated with each other. 5. Partial correlation analysis was used to separate interactions between variables. This indicated that dietary energy had no identifiable influence on muscle growth. In contrast dietary protein appeared to stimulate muscle growth directly by increasing muscle RNA content and inhibiting proteolysis, as well as increasing insulin and free T3 levels. Insulin and free T3 stimulated each other as well as muscle protein turnover; insulin stimulating the RNA activity particularly at low insulin levels, free T3 stimulating the RNA content and both hormones stimulating proteolysis. 6. These apparent relations are shown to be consistent in the main part with previous studies of the mechanism of action of insulin and T3, but the possibility cannot be discounted that other anabolic hormones not measured in these studies are involved, particularly in the apparent direct influence of dietary protein on muscle.

Animals↗
PubMed1978

Dietary protein and lead retention.

The effects of dietary protein content on lead retention were studied in young rats. In experiments lasting between 3 and 6 weeks, rats given diets containing lead and 20% casein were fed ad libitum or were pair fed with rats given diets containing 6.5 or 7.5% casein. Among rats given 20% casein, lead retention was inversely related to growth rate. A reduction of dietary protein either had no effect or reduced lead retention. In other experiments lasting 4 days and using 203Pb, given orally or intraperitoneally, the recovery of isotope in the gutfree carcass was unaffected or reduced by a reduction in dietary protein. Blood and liver lead often increased when kidney and carcass lead decreased in response to a reduction of dietary protein. Conflicting observations on the effect of low-protein diets on lead retention may thus be due to opposing effects of low dietary protein and decreases of growth rate and to different responses of different tissues.

Animals↗
PubMed1989

Protein digestion in weanling pigs: effect of dietary protein source.

The digestion and absorption of dietary protein was measured in weanling pigs (5 wk of age). Diets containing corn and either dried skim milk (DSM), soybean meal (SBM) or corn gluten meal (CGM) were fed for 7 d, and the contents of the stomach and six segments of the small intestine were collected. Nitrogen digestibility increased linearly from the proximal duodenum to the distal ileum, and was highest for DSM, intermediate for SBM and lowest for CGM diets at the distal ileum. The content of free amino acids in digesta increased 8-fold (SBM and CGM) to 12-fold (DSM) between the stomach and the proximal duodenum and reached a maximum concentration in the distal jejunum. Digestion of DSM was more proximal than was that of SBM. Although there was some accumulation of small peptides in the duodenum with a subsequent decrease in the jejunum, the molecular weight profiles of the soluble proteins were relatively constant throughout the small intestine. Protein solubility and the rate of proteolysis in the stomach and upper small intestine were the primary factors that limited the digestion of SBM and CGM.

Absorption↗
PubMed1989

In vitro Na+,K+-ATPase (EC 3.6.1.3)-dependent respiration and protein synthesis in skeletal muscle of pigs fed at three dietary protein levels.

1. Eighteen pigs were offered diets containing 130, 170 or 210 g protein/kg with three barrows and three gifts per diet from 20 to 60 kg live weight. Oxygen consumption, Na+,K+-ATPase (EC 3.6.1.3)-dependent and -independent respiration and protein synthesis were measured in vitro in intercostal and sartorius muscle preparations from these pigs. 2. Increasing dietary protein concentration increased (P less than 0.01) daily gain and dissectible muscle in carcass. 3. O2 consumption and Na+,K+-ATPase-dependent respiration of the intercostal and sartorius muscles increased linearly (P less than 0.01) with increase in dietary protein concentration. The requirement for the support of the transport of Na+ and K+ across the cell membrane in these muscles, on average, accounted for 22-25% of the O2 consumption. 4. Synthesis rate (mg/g per d) of protein in the sartorius muscle increased (P less than 0.05) from 3.05 to 5.07 and increased (P less than 0.1) from 2.57 to 4.06 in the intercostal muscle as dietary protein increased from 130 to 210 g/kg diet. 5. Regression of Na+,K+-ATPase-dependent respiration against protein synthesis in each of intercostal and sartorius muscles showed a linear relation, an attestation of a close link between productive processes and auxiliary energy expenditure.

Animals↗
PubMed1999

Influence of dietary protein on insulin-like growth factor binding proteins in the chicken.

We determined the effect of dietary protein on the distribution of insulin-like growth factor (IGF) binding proteins in chicken plasma. Three groups of male broilers (n = 6 per group) were fed (ad libitum) isocaloric diets containing 12, 21 or 30% dietary protein. Birds were fed respective diets beginning at 7 days of age and killed at 28 days. No differences were observed between adequate (21%) and high (30%) protein intakes for any of the parameters investigated (growth criteria, plasma levels of IGF-I, growth hormone or IGF-binding proteins). Feeding protein deficient diets (12%) resulted in a 34% decrease in body weight, 17% decrease in feed intake and a 39% increase in feed/gain ratio. IGF-binding proteins in plasma samples were separated by SDS-PAGE and transferred to nitrocellulose sheets. Nitrocellulose blots were probed with [125I]chicken IGF-II. Four regions of binding activity corresponding to 70, 43, 30 and 24 kDa were observed in all samples. Birds consuming 12% dietary group protein had less than 50% of the 43-kDa binding activity of birds consuming 21 or 30% dietary protein. The 30-kDa binding activity was 42% lower in the 12% dietary protein group compared to birds consuming adequate protein. In contrast, 70- and 24-kDa binding activities were not influenced by dietary protein. Chickens consuming 12% dietary protein had higher levels of growth hormone and lower levels of IGF-I than those consuming 21 or 30% dietary protein. These data indicate that in chickens, the circulating levels of at least two independent IGF-binding proteins are influenced by dietary protein.

Animals↗
PubMed1989

Dietary protein requirements of physically active individuals.

The dietary protein requirement of physically active individuals has received considerable scrutiny in recent years. Because the current United States Recommended Daily Allowance (USRDA) for protein (0.8 g/kg/day) already contains a safety margin (0.35 g/kg/day) to assure adequate protein intake, no increment in the USRDA was thought necessary to meet the demands of physical activity. Recently, collective evidence from research techniques utilising nitrogen balance, labelled amino acid isotopes, urea production and 3-methylhistidine excretion indicates that exercise (endurance and weightlifting) can significantly alter protein metabolism and that the dietary protein needs of physically active individuals may exceed the current USRDA. During endurance exercise, protein synthesis is depressed and protein degradation increases. Thus, amino acids become available for oxidation in energy-yielding processes. Amino acid catabolism has been estimated to contribute between 5 and 15% of the energy required during endurance exercise. Definitive conclusions regarding the changes that occur in protein synthesis and protein degradation during weightlifting exercise must await further research. The net contribution of amino acids to the energy required during weightlifting exercise is unknown but, due to the anaerobic nature of the event, it is most likely less than during endurance exercise. However, following both endurance and weightlifting exercise, protein synthesis increases. Based on current research, it is not yet possible to make recommendations for the daily protein needs of exercising individuals. It does appear that physically active individuals require more dietary protein per kilogram of bodyweight than sedentary individuals. However, when protein intake is expressed as a percentage of daily energy intake, physically active and sedentary individuals have similar requirements (approximately 12 to 15% of total energy as protein). Therefore, to cover the protein requirements of both physically active individuals and sedentary individuals it is suggested that future protein allowances be based on a percentage of the daily energy requirements. Protein consumption in excess of the current USRDA may minimise changes in body nitrogen stores, particularly during the first few weeks of training. However, further research is needed before a definitive conclusion can be made regarding protein ingestion and athletic performance.

Adult↗
PubMed1990

Dietary proteins, cholesterol and thyroxine: a proposed mechanism.

The effects of dietary protein sources on plasma cholesterol concentrations are well-documented: animal proteins are hypercholesterolemic relative to plant proteins. While this effect of dietary proteins has been shown in many species, the mechanism is not known. This review will explore the relation between dietary proteins and plasma thyroxine concentrations. Data will be presented showing that feeding dietary animal proteins consistently depresses plasma thyroxine levels. Furthermore, the effects of thyroxine on cholesterol metabolism is consistent with the effects of dietary proteins on cholesterol metabolism. Although evidence is not conclusive, data support the hypothesis that dietary proteins may affect plasma cholesterol levels through changes in plasma thyroxine concentrations. To elucidate the mechanism by which this happens will be the basis for future research.

Animals↗
PubMed2005

Protein synthesis and translation initiation factor activation in neonatal pigs fed increasing levels of dietary protein.

Limited data suggest that the growth of low-birth-weight infants is enhanced by feeding a high-protein diet; however, the mechanisms involved in the effect have not been delineated. To identify these mechanisms, 34 pigs were fed from 2 to 7 d of age [60 g dry matter/(kg body weight . d)] isocaloric milk diets that contained levels of dietary protein that were marginal, adequate, and in excess of the piglets protein requirement (21, 33, and 45% of dry matter, respectively). Dietary protein replaced lactose and fat on an isocaloric basis. Fractional protein synthesis rates, various biomarkers of translational regulation, and plasma glucose and insulin levels were measured in overnight food-deprived and fed pigs. Mean daily weight gain of pigs fed the 33 and 45% protein diets was greater than that of pigs fed the 21% protein diet (P < 0.01). Plasma glucose (P = 0.07) and insulin (P < 0.01) levels decreased as dietary protein increased 60 min after feeding. Protein synthesis rates in longissimus dorsi, gastrocnemius, masseter, heart, liver, kidney, jejunum, and pancreas were greater in the fed than in the food-deprived state (P < 0.01). Protein synthesis in skeletal muscle did not change with protein intake in the fed state, but decreased quadratically (P < 0.01) with increasing dietary protein in the food-deprived state. Protein kinase B, ribosomal protein S6 kinase 1(S6K1), and eukaryotic initiation factor (eIF) 4E binding protein-1 (4E-BP1) were more phosphorylated, and assembly of the inactive eukaryotic initiation factor 4E . 4E-BP1 complex in muscle and liver was reduced in the fed state (P < 0.001) and were not consistently affected by dietary protein level. The results suggest that feeding stimulates protein synthesis, and this is modulated by the activation of initiation factors that regulate mRNA binding to the ribosomal complex. However, the provision of a high-protein diet that exceeds the protein requirement does not further enhance protein synthesis or translation initiation factor activation.

Amino Acids, Branched-Chain↗
PubMed1990

Effect of dietary protein on bed-rest-related changes in whole-body-protein synthesis.

To determine whether increasing dietary protein could exert a beneficial effect on bed-rest-related protein catabolism, two groups of normal subjects were subjected to 7 d of bed rest while taking isocaloric diets containing either 0.6 or 1.0 g protein.kg body wt-1.d-1. Whole-body-leucine turnover, leucine oxidation, and nonoxidative leucine disappearance were measured by use of a constant infusion of 1-13C-leucine. Before bed rest, the higher-protein diet resulted in a 14% decrease in whole-body-leucine turnover and a 28% decrease in leucine oxidation, but net nonoxidative leucine disappearance was not different on the two diets. A 24% decrease in nonoxidative leucine disappearance was seen in subjects assigned to the lower-protein diet, who had been on bed rest, but on the higher-protein diet, leucine kinetics were unchanged by bed rest. Bed rest does not cause an increase in whole-body-protein breakdown, but decreased whole-body-protein synthesis is demonstrable when dietary protein is low. This decrease is prevented by a higher dietary amount of protein.

Adult↗
PubMed1982

Responses of skeletal muscle protein synthesis and breakdown to levels of dietary protein and fat during growth in weaning rats.

Skeletal muscle growth, muscle nucleic acids, and muscle protein synthesis and breakdown were measured to evaluate the protein requirement of weanling rats. Male Sprague-Dawley rats were fed purified diets that differed in protein and energy contents. Diets ranged from 5 to 30% casein, 5 to 15% corn oil, and all were methionine fortified. All diets were provided for 14 days beginning at 24 days of age. At 38 days of age, animals were killed and the soleus, plantaris, gastrocnemius, extensor digitorum longus (EDL), and biceps brachii muscles and the inguinal, epididymal, and perirenal fat pads were removed and weighed. The soleus and EDL were used to determine protein synthesis and breakdown and nucleic acid contents. Body weight, muscle weight, protein synthesis, DNA and RNA/DNA increased as the casein content of the diet increased to 15%. Casein levels up to 30% failed to cause any additional increases in any of these parameters. These findings indicate that for growing rats maximum protein synthesis defines the minimum about of dietary protein necessary to achieve maximum growth.

Adipose Tissue↗
PubMed1979

Diurnal variations in plasma neutral amino acid concentrations among patients with cirrhosis: effect of dietary protein.

The effect of varying dietary protein content on the daily rhythms in plasma neutral amino acid concentrations was studied in patients with chronic cirrhosis. For two consecutive 5-day periods, subjects consumed diets containing either 0 or 75 g of protein per day. Blood samples were drawn at 4-hr intervals on the 4th and 5th days of each dietary period. For most of the neutral amino acids, the changes in plasma concentration associated with time of day or with variations in dietary protein content were similar to those observed previously in normal subjects. Ingestion of the protein-free diet caused significant reductions in the daytime level of all amino acids studied, except for tryptophan, the concentration of which did not change during the 24-hr period. Ingestion of the 75-g protein diet caused plasma levels of most of theamino acids to increase slightly during the day; these increments were not statistically significant for tryptophan, tyrosine, leucine, and methionine. The absolute plasma concentrations of most of the neutral amino acids were also in the normal range; exceptions included methonine, tyrosine, and phenylalanine, whose plasma levels were significantly elevated above normal valves. The plasma ratios of tryptophan, tyrosine, and phenylalanine concentrations to the sum of the concentrations of other large neutral amino acids increased during the day uhen the protein-free diet was ingested; this effect was moderated by the addition of protein to the food. The plasma ratios for the branched-chain amino acids were depressed below normal; those for tyrosine, phenylalanine, and methionine were significantly increased. The plasma tryptophan ratio was within the normal range. These findings provide a basis for anticipating that the uptake from blood into brain of several of the large neutral amino acids may be modified in patients with chronic cirrhosis.

Adult↗