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At least 163 records · Page 9Linked to original sources
PubMed1978

Transport of large breakdown products of dietary protein through the gut wall.

Ferritin or tritium labelled immunoglobulin G may, by electron microscopy, be demonstrated entering, within, and leaving the epithelial cells. Quantitative studies using various proteins labelled with radioiodine show that large amounts of protein bound radioactivity may be demonstrated in the tissues after feeding the labelled protein to adult rats by stomach tube. The molecular size of this material as determined by sugar gradient ultracentrifugation of tissue extracts ranges when IgG is fed from 50,000-20,000 Daltons. The material retains its ability to react as antigen with antisera specific to the original molecule: precipitation reactions may be obtained in gels and quantitative studies show that cnosiderable amounts of the protein-bound radioactivity are still specifically precipitable. Such studies have been carried out with alpha-gliadin as well as bovine IgG. At 100 days old rats may absorb as much as 40% of a dose of bovine IgG in the form of these large molecular breakdown products.

Animals↗
PubMed1986

Effect of dietary protein levels on urea utilization in Papua New Guinea highlanders.

Ability to utilize urea nitrogen for body protein synthesis was examined with Papua New Guinea (PNG) highlanders and Japanese (JPN). Eight male PNG highlanders and 8 male JPN were fed on a low protein diet containing 0.55 g protein/kg or an adequate protein diet containing 1.34 g protein/kg for 1 or 2 weeks. The fate of 15N was measured after oral administration of 15N-labelled urea. There was no difference in 15N incorporation into serum protein between PNG highlanders and JPN receiving low protein diets. On the other hand, on the adequate protein diet, 15N incorporation in PNG highlanders was similar to that on the low protein diet, in contrast to that in JPN which was hardly detected in the adequate protein diet. When PNG highlanders take more protein than protein in their usual diet, they effectively incorporate ingested protein into their body protein and urea nitrogen is utilized for synthesis of body protein.

Adolescent↗
PubMed2002

Feeding intensity and dietary protein level affect adipocyte cellularity and lipogenic capacity of muscle homogenates in growing pigs, without modification of the expression of sterol regulatory element binding protein.

Muscle fat stores at slaughter partly determine the dietetic and sensory quality traits of pork meat. Nutritional strategies during the growing-finishing period are able to modify intramuscular fat content; however, the underlying mechanisms remain largely unknown. The objective of this study was to determine some of the cellular, biochemical, and molecular bases of muscle fat content variation in response to feeding regimen in pigs. Crossbred pigs of 30 kg BW were allocated to three feeding groups: free access ([C], n = 10) to a standard diet (3.25 kcal of DE/kg, 9.5 g of lysine/kg), standard diet at 75% of the spontaneous voluntary intake ([FR], n = 10), or both low protein and energy intakes ([PR], n = 10) in order to get the same growth rate as the FR pigs and the same body composition as the C pigs. At slaughter (110 kg BW), FR and PR pigs were 30 d older than C pigs (P < 0.001). In agreement with the protocol, carcass adiposity was similar in PR and reduced (P < 0.01) in FR pigs compared with C animals. Lipid content in longissimus lumborum muscle was reduced by 25% in FR pigs and increased by 40% in PR pigs compared to C pigs (P < 0.001). Commensurate variations in the diameter of muscle adipocytes were observed between the three feeding groups (P < 0.001). The muscle activities of malic enzyme and glucose-6-phosphate dehydrogenase, generating reduced nicotinamide adenine dinucleotide phosphate for fatty acid synthesis, were depressed (P < 0.05) in both FR and PR groups, compared to the C group. The expression level of the sterol regulatory element binding protein that was chosen as the putative candidate at the molecular level was not modified by the feeding regimen. No variations in the oxidative enzyme markers were denoted, whereas lactate dehydrogenase activity was reduced by 13% (P < 0.05) in PR group compared to other groups. In conclusion, moderate long-term feed restriction results in decreased lipogenic capacity of muscle adipocytes and intramuscular fat content. In contrast, the reduction of both protein and energy intakes more likely results in an imbalance between multiple aspects of muscle energy metabolism, in favor of intramuscular fat accretion.

Adipocytes↗
PubMed2000

The role of dietary protein restriction in Indian patients with chronic renal failure.

OBJECTIVE: To determine dietary protein intake in Indian patients with chronic renal failure and the impact of prescribing protein restricted diets to these patients. METHODS: Baseline dietary protein intake was estimated in forty five patients with chronic renal failure on an unrestricted diet. Of these 45 patients, 27 were vegetarian and 18 were non-vegetarian. Then the patients were divided into 2 comparable groups. Twenty group I patients were allowed to continue unrestricted diet while 25 group II patients were advised 0.6 g/kg/day (50% high biological value) protein. Protein intake was estimated at 1 and 2 month follow up. RESULTS: The baseline dietary protein intake in 45 patients was 0.65 +/- 0.15 (mean +/- 1 SD) g/kg/day. There was no significant difference in protein intake of group I and group II patients at 1 and 2 month follow up. Also, the protein intake in group II patients was not different at 1 and 2 month follow up compared to baseline value. CONCLUSION: Protein intake of Indian patients with CRF is usually low even on an unrestricted diet. The usual practice of advising dietary protein restriction has no significant impact on the protein intake.

Adult↗
PubMed1994

Effect of dietary protein on the liver content and subunit composition of the branched-chain alpha-ketoacid dehydrogenase complex.

Levels of expression of two subunits of the liver branched-chain alpha-ketoacid dehydrogenase complex in response to extremes of dietary protein intake (50% versus 0% protein diet) were determined by quantitative immunoblotting. Dietary protein deficiency decreased the amount of E1 alpha protein to a greater extent than E2 protein. The ratio of E1 alpha to E2 was below 1 in the liver of animals starved for protein and above 1 in the liver of animals fed the high-protein diet. Supplementation of the 0% protein diet with 5% leucine (but not 5% valine) had the same effect as the 50% protein diet. The extremes of dietary protein also resulted in a divergent pattern of expression of the mRNAs for the subunits of the complex. The E1 beta message showed the expected corollary of being greater in the liver of the high-protein-fed rats than the no-protein-fed rats. In contrast, the E2 message was not affected by the two extremes of dietary protein and the E1 alpha message was greater in the liver of the no-protein-fed rats than the high-protein-fed rats. Thus, coordinate regulation of gene expression of the subunits of the complex does not occur in response to dietary protein. Post-transcriptional regulatory mechanisms most likely determine the amount of the complex and the ratio of its subunits. The decrease in E1 alpha/E2 protein ratio that occurs in dietary protein deficiency may increase sensitivity of the complex to phosphorylation-mediated inhibition by branched-chain alpha-ketoacid dehydrogenase kinase.

3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)↗
PubMed1996

Metabolism of lysine, threonine, and leucine in growing rats on gluten or zein diets at various dietary protein levels.

The metabolic fates of the carbon skeletons of leucine, lysine, and threonine were studied in growing rats on the diets containing graded levels of protein calorie percentages (10, 20, 30, and 40 PC%) by use of either gluten or zein at 4100 kcal of metabolizable energy per kg of diets. In growth experiment for 21 days, body weight gain, food intake, and body fat increased at higher PC% in the gluten diets, but rats given zein did not maintain their initial weight even at 40 PC%. The concentration of plasma free lysine remained low with the zein diets, but plasma threonine increased at 10 and 20 PC% in the gluten and zein diets, respectively. Plasma leucine increased as the protein level increased either dietary protein. More than 70% of 14C was incorporated into body protein 12 h after an intraperitoneal injection of labeled lysine in all groups, but little 14CO2 was expired in rats on the gluten and zein diets. About 79% of 14C-threonine was incorporated into body protein in rats given the gluten and zein diets at 10 PC%, but the values were gradually decreased with increasing the dietary protein levels. Some 40-50% of 14C-leucine was incorporated into the body protein in rats given the gluten diets, and the values for the zein diets were extensively decreased in the higher PC% groups where the expired 14CO2 was inversely increased to a great extent. These results showed that, when a specific amino acid was limiting or deficient in the diet, the major portion of the labeled amino acid was utilized for body protein synthesis and little was oxidized to carbon dioxide, whereas the oxidative degradation of essential amino acid other than limiting one was increased and the efficiency of the amino acid utilization was relatively decreased.

Animals↗
PubMed1995

Maintenance requirements for dietary protein in 11- and 18-month-old male rats.

Body weight, lean body mass (total weight less body fat), carcass protein, and serum protein were examined as potential parameters by which to assess the effect of age on protein requirements for maintenance in male rats, aged 11 months and 18 months, fed diets containing 1.53, 3.41, 4.98, 6.52, or 8.05% dietary protein, casein plus methionine, for a 5-week period. Body weight change was maintained in older animals at 6.52% dietary protein and in younger animals at 4.98% dietary protein. Older animals consuming the two diets highest in protein had a greater percent body fat and less percent body protein than younger animals. Significant effects of diet and the interaction of diet and age on serum protein were also observed. As dietary protein level increased, serum protein increased gradually in younger rats, but only between 3.41 and 4.98% dietary protein in older rats. Lean body mass and total carcass protein increased as dietary protein level increased, but there were no significant differences due to age or the interaction of diet and age. Changes in body weight indicate a greater protein requirement for 18-month-old rats compared with 11-month-old rats, although complicated by greater food intake and fat deposits in older animals. Measures of body protein indicate that age has some influence on protein needs for maintenance purposes.

Aging↗
PubMed2007

Dietary protein, endurance exercise, and human skeletal-muscle protein turnover.

PURPOSE OF REVIEW: Whereas diet and exercise have been shown to influence whole-body protein utilization, little is known about the impact of these factors on skeletal-muscle protein turnover. We highlight the role of dietary protein in modulating skeletal-muscle protein turnover in response to endurance exercise. Effects of endurance exercise on skeletal-muscle protein metabolism are presented and the influence of habitual protein intake on exercise-related protein responses is discussed. RECENT FINDINGS: Skeletal-muscle protein turnover increases in response to endurance exercise training and following a single endurance exercise bout. Nutritional supplementation postexercise favorably affects skeletal-muscle protein synthesis and demonstrates amino acid availability as pivotal to the skeletal-muscle synthetic response following exercise. The level of habitual protein intake influences postexercise skeletal-muscle protein turnover. SUMMARY: Dietary protein and exercise are powerful stimuli affecting protein turnover. Since variation in habitual protein intake influences skeletal-muscle protein turnover postexercise, investigations are needed to determine what role protein intake has in regulating skeletal-muscle protein metabolism. Long-term, well controlled diet and exercise intervention studies are essential for clarification of the relation between protein intake, endurance exercise, and skeletal-muscle protein turnover. Studies designed to characterize this relationship should be attentive to habitual macronutrient and energy intakes.

Biological Availability↗
PubMed1997

Low dietary protein impairs blood coagulation in BHE/cdb rats.

The influence of dietary protein on blood coagulation tests was evaluated in BHE/cdb rats. Three experiments were conducted in order to compare effects of diets with low (8 g/100 g diet) or high (38 g/100 g diet) protein, to establish values for coagulation tests at intermediate (12-30 g/100 g diet) concentrations of dietary protein, and to compare feeding identical quantities of diets with 8 g protein/100 g diet vs. 18 g protein/100 g diet. After 4 wk of feeding the semipurified diets, bleeding time exceeded 15 min in the groups fed low protein diets, compared to a range of 3-6 min for the groups fed high protein diets. Several in vitro tests of coagulation were abnormal in the rats fed low protein diets. For example, prothrombin time averaged 27 +/- 8 s in rats fed 8 g protein/100 g diet plus beef tallow, but 17 +/- 1 s in rats fed 38 g protein/100 g diet plus tallow. The coagulation deficit in rats fed low protein was not affected by fat source (tallow vs. menhaden oil), but fibrinogen was elevated in rats fed diets with menhaden oil. Conversely, no differences in coagulation tests were observed among rats fed 12-30 g protein/100 g diet. Bleeding times ranged from 7 to 9 min, and prothrombin time was 17-18 s. Significant differences in plasma fibrinogen concentration and prothrombin time were observed in rats fed 8 vs. 18 g protein/100 g diet at a fixed rate of 6 g/100 g body weight. Platelet and blood cell numbers were unaffected by dietary protein. The evidence for multiple deficits in the coagulation system suggests that hepatic function in BHE/cdb rats may become impaired when the rats are fed low protein diets of the composition used here.

Animals↗
PubMed1991

Influence of dietary protein intake on whole-body protein turnover in humans.

Methods for measuring rates of protein synthesis and degradation in the whole body of humans with isotopes of carbon and nitrogen are described and attention is drawn to their relative merits and drawbacks for studying the nutritional control of protein metabolism. A review of published work on dietary protein and protein metabolism leads to the conclusion that protein is the major dietary determinant of whole-body protein turnover rates, and that energy intake is comparatively unimportant. Dietary protein affects protein turnover at two levels: an immediate response to the intake of protein in meals and a longer-term adaptation after a change in protein intake. An increase in the level of dietary protein enhances the response to meals, which mainly consists of a decrease in the rate of protein degradation. The adaptation to higher protein intakes involves an increase in the basal (postabsorptive) rates of both synthesis and degradation. Suggestions for future investigation include more detailed studies of the acute and adaptive responses, to facilitate understanding of dietary protein requirements, and the effects of very-high-protein intakes with continued development of techniques for studying protein turnover in individual tissues in humans.

Adult↗
PubMed2004

Synthesis of erythrocyte glutathione in healthy adults consuming the safe amount of dietary protein.

BACKGROUND: The finding that plasma glutathione turnover decreases as dietary protein intake decreases suggests that the safe amount of dietary protein, although sufficient for maintenance of nitrogen balance, may be insufficient for maintenance of cellular glutathione. OBJECTIVE: Our objective was to determine the effect of the safe protein intake on the erythrocyte glutathione synthesis rate and its relation with urinary 5-L-oxoproline excretion. DESIGN: Erythrocyte glutathione synthesis and urinary 5-L-oxoproline excretion were measured in young adults (6 men and 6 women) by using an infusion of [(13)C(2)]glycine on 3 occasions: initially during the subjects' habitual protein intake (1.13 g.kg(-1).d(-1)) and on days 3 and 10 of consumption of a diet providing the safe protein intake (0.75 g.kg(-1).d(-1)). RESULTS: Compared with baseline values, the fractional synthesis rate of erythrocyte glutathione was significantly lower (P < 0.05) on days 3 and 10 of the diet with the safe protein intake. Urinary 5-L-oxoproline excretion increased significantly (P < 0.05) above baseline by the third day of the diet with the safe protein intake and remained elevated. Erythrocyte glutathione concentrations and absolute synthesis rates decreased by day 3 but recovered to baseline values by day 10. Erythrocyte concentrations of cysteine, methionine, and serine remained unchanged, whereas erythrocyte concentrations of glycine, glutamic acid, and glutamine increased significantly by day 10. CONCLUSION: During adaptation to the safe amount of dietary protein, there are changes in the concentration and kinetics of erythrocyte glutathione that suggest a reduced antioxidant capacity and possible increased susceptibility to oxidant stress.

Adaptation, Physiological↗
PubMed1998

Nutritional effects of dietary protein restriction in insulin-dependent diabetes mellitus.

The effects of dietary protein deprivation in insulin-dependent diabetes mellitus (IDDM) have been investigated in a merely rudimentary fashion in human subjects. Moderate dietary protein restriction of 0.6 g/(kg ideal body weight.d) over 3 mo in free-living IDDM patients produces increased adiposity during weight maintenance and decreased muscle strength. These effects might have been predicted from studies of protein deprivation in diabetic subjects, indicating impairment of nitrogen retention. The clinical consequences of dietary protein restriction in IDDM may be more complex than described to date. This is suggested by the overriding paradox that the actions of insulin on protein synthesis are inconsistent among in vitro, animal and human in vivo models. The inconsistency and the observation that insulin deficiency in humans accelerates both proteolysis and protein synthesis imply that knowledge about insulin, diabetes and protein metabolism in humans is inadequate and should be studied in increasing detail. Better understanding of the clinical consequences of dietary protein restriction in diabetes, both beneficial and adverse, is likely to come from future studies incorporating clinically relevant levels of insulin deficiency and protein deprivation into studies of bodily function, clinical outcomes and specific examination of the metabolism of individual proteins.

Diabetes Mellitus, Type 1↗
PubMed1981

The role of dietary protein in hepatic lipogenesis in the young rat.

1. The effect of varying dietary levels of casein (40-140 g/kg) on hepatic lipogenesis and the levels of hepatic fatty acid synthetase (FAS), glucose-6-phosphate dehydrogenase (EC 1.1.1.49; G6PD), malic enzyme (EC 1.1.1.40; ME), citrate cleavage enzyme (EC 4.1.3.8; CCE), acetyl CoA carboxylase (EC 6.4.1.2; AcCx), glucokinase (EC 2.7.1.2; GK), and pyruvate dehydrogenase (PDH) was examined in young, growing rats. 2. The activities of AcCx, FAS, G6PD and in vivo fatty acid synthesis were generally found to increase with increased dietary protein. 3. The levels of GK and PDH were not related to dietary protein. 4. ME decreased with increasing dietary protein. 5. The results demonstrate a dissociation between hepatic fatty acid synthesis and ME and suggest that when rats consume low-protein diets the NADPH needed for fatty acid synthesis is generated primarily by ME but that as the level of dietary protein is increased the contribution of ME is reduced while that of the phosphogluconate pathway becomes more important.

ATP Citrate (pro-S)-Lyase↗