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Query: UMLS:C0038187 (starvation)
 24,951 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We studied the effects of acute starvation and refeeding on muscle protein synthesis and degradation in young rats. As measures of synthesis, we determined muscle RNA concentration and the rate of incorporation of [14C]leucine into skeletal muscle protein (Sm). As an estimate of nitrogen retention we measured urea production (UrP). Starvation reduced these variables significantly. One refeeding period returned Sm to control values, only partially restored RNA concentration, and increased UrP. We determined the urinary excretion rate of 3-methylhistidine (3-MH) as a measure of the rate of myofibrillar protein degradation. Excretion of 3-MH was lowest in control and highest in starved rats. Refeeding decreased 3-MH excretion to a level midway between control and starved animals. Growth was attended by high rates of synthesis and low rates of degradation. Starvation depressed synthesis and increased degradation. With refeeding, synthesis increased and degradation decreased, compared with the starved state.
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PMID:The effects of starvation and refeeding on muscle protein synthesis and catabolism in the young rat. 64 92

Elective surgical operation in normally nourished patients is associated with an increase of up to 40 per cent in the urinary excretion of 3-methylhistidine during the first three postoperative days. This increase was statistically significant (P less than 0.01) on the second and third postoperative days. This probably represents a minor degree of increased muscle proteolysis, principally due to the operative trauma. The possible effect of postoperative starvation requires further elucidation.
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PMID:The effect of elective surgery on 3-methylhistidine excretion. 69 43

The daily flux of amino acids in the body is extensive. Protein synthesis is estimated to be 300 g daily in an adult man. This requires uptake and release of 150 g essential amino acids, yet the dietary requirement for essential amino acids in only 6 g. This indicates extensive and efficient recycling of essential amino acids released by protein breakdown. The catabolism of essential amino acids by the liver is sensitively regulated in relation to requirements. A study of availability of tryptophan to rats receiving various levels of tryptophan in the diet shows that plasma tryptophan increases only when intake exceeds requirements and at these higher levels of intake tryptophan oxygenase activity in the liver becomes increased shortly after meals. In addition, the carbohydrate content of the diet causes tryptophan to become deposited in the free amino acid pool of muscle through an insulin-dependent mechanism. Dietary carbohydrate also effects plasma tryptophan due to a fall in the plasma level of non-esterified fatty acids which compete with tryptophan for binding sites on serum albumin. Consequently, after carbohydrate the proportion of plasma tryptophan bound to serum albumin increases, so that there is less nonbound tryptophan in the plasma. The metabolic significance of this has yet to be demonstrated. Finally, protein metabolism in skeletal muscle exhibits considerable efficiency of reutilization of essential amino acids, since the main products passing into the blood are alanine and glutamine. It has been shown that 3-methylhistidine present in muscle protein in not reutilized for synthesis of protein and that its excretion in the urine can provide a useful index of muscle catabolism. In prolonged starvation of adults or protein deficiency in children, output of 3-methylhistidine is much reduced, suggesting an adaptive reduction in muscle protein catabolism. It is emphasized that, because of its function in monitoring dietary amino acid intake, liver protein metabolism responds rapidly to changes in protein intake and in consequence protein deficiency causes early depletion, whereas muscle protein undergoes depletion later and is subject to adaptive processes that restrict the loss.
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PMID:Regulation of protein metabolism in relation to adequacy of intake. 81 Apr 22

Muscle protein catabolism has been evaluated using the excretion of urinary 3-methylhistidine (3-MEH) is six normal male and six normal female subjects and in four surgical patients, two of whom developed febrile episodes during the course of their study. In addition, their nutritional status was also evaluated using percentage body weight losses before hospital admittance, creatinine-height ratios, and, in two patients, serum alkaline ribonuclease levels. The results indicate that: 1) prolonged starvation may produced decreased 3-MEH excretion because of an adaptive diminution of muscle breakdown in sustained starvation, decreased 3-MEH excretion also may simply reflect diminished lean body mass, 3-MEH excretion may be increased above basal levels because of superimposed stresses such as fever, and the acute phases of starvation produce increased levels of 3-MEH excretion until adaptive mechanisms occur; 2) creatinine-height ratios are low in starvation, and increase not only with improved nutrition but in response to fever and stress of operation, even when these are superimposed on malnutrition; and 3) alkaline RNAase levels are elevated in malnutrition and decrease with improved nutrition but in response to fever and stress of operation, even when these are superimposed on malnutrition; and 3) alkaline RNAase levels are elevated in malnutrition and decrease with improved nutrition. The enzyme may also be elevated by the stress of operations.
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PMID:Muscle protein catabolism in the septic patient as measured by 3-methylhistidine excretion. 88 85

Degradation rates of muscle proteins were determined in young rats allowed access to standard rat chow 12 h/day. degradation was assessed by determination of 3-methylhistidine (3MH) excretion rates. 3MH is a nonreutilized amino acid produced almost exclusively within the actin and myosin of skeletal and cardiac muscle. Because plasma levels of 3MH are low and renal clearance is high, excretion reflects myofibrillar degradative rates. Excretion of 3MH was determined for 4-h periods beginning 12 and 20 h after initiation of feeding and after 24-and 48-h fasts. Excretion of 3MH per 4-h period increased with time after the last feeding. Because creatinine excretion is a function of muscle mass dividing 3MH excretion by creatinine excretion represents myofibrillar degradation per unit muscle mass, the fractional degradative rate. Degradation rates rose from 4.6 to 14.5%/day between 12 and 16 and 60 and 64 h after the beginning of the last meal. These results support the presence of a diurnal pattern of protein degradation as well as increased muscle degradation during starvation.
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PMID:Protein degradation in muscle: response to feeding and fasting in growing rats. 88 48

We determined the effects of feeding, starvation, and glucose infusion after starvation in newborn guinea pigs. We determined the rate of 14C-leucine incorporation into skeletal muscle (KS) as a measure of muscle protein synthesis and the rate of excretion of 3-methylhistidine as a measure of muscle myofibrillar protein catabolism (Kc). Fed newborns, who were in positive nitrogen balance, had the highest Ks and lowest Kc, while starved newborns had the lowest Ks and highest Kc. Infusing glucose after starvation decreased net protein catabolism and Kc, but did not increase Ks. The magnitude of change of Kc in response to starvation and glucose infusion was much greater than Ks. Changes in catabolic rate may influence net muscle protein balance to a greater degree than changes in synthetic rate.
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PMID:The effects of starvation, glucose infusion, and normal feeding, on muscle protein synthesis and catabolism in the newborn guinea pig. 95 2

The effects of modified protein sparing therapy (PSP) and total parenteral nutrition (TPN) on total and wound metabolism were studied for 96 hours after laparotomy and a small gastric excision in 40 rabbits starved for seven days. A further eight starved and eight non-starved animals served as controls for the blood variables. Normal healing up to day 14 was studied in 20 non-starved animals. The difference in deaths and animals in poor condition, 42.1 per cent in PSP and 18.6 per cent in TPN, respectively, was clear but statistically non-significant. PSP led to a lower mean serum albumin concentration than TPN, 25.7 +/- 3.7 (SD) and 28.7 +/- 3.0 (p = 0.02), respectively. The animals receiving PSP excreted significantly more 3-methylhistidine. TPN maintained a positive nitrogen balance, but PSP produced a negative one. The collagen content of the skin scar was lower after PSP (3.1 +/- 0.7 mg) than after TPN (4.5 +/- 1.3 mg) (p less than 0.05), the latter coming close to the level for normal 4-day healing, 4.5 +/- 1.2 mg. Prolyl 4-hydroxylase (PPH) activity showed no difference. No inter-group differences in collagen were found in the stomach. Both regimens totally reversed the starvation-induced decrease in PPH activity in the stomach, but only partially in skin. Thus TPN produced better total and skin wound metabolism after laparotomy and starvation than did PSP. No differences in visceral wound healing were observed.
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PMID:Effect of intravenous feeding on wound healing in starvation: an experimental study on the rabbit. 193 25

In a study of the mechanism of adaptation to protein deficiency, 10 moderately obese women underwent a 3-wk fast followed by random allocation to a 1-wk refeeding regimen providing 80 g carbohydrate or protein. Protein metabolism was studied by means of nitrogen (N) balance, urinary 3-methylhistidine excretion, and postabsorptive plasma leucine flux using L-[1-13C]leucine infusions. After the 3-wk fast, plasma leucine flux and 3-methylhistidine excretion both decreased by 31% from control diet values (P less than 0.01), and N balance was -5.9 g/day. After protein refeeding, N balance was positive (+1.7 g/day, P less than 0.05) whereas leucine flux was unchanged from prolonged fasting values. After carbohydrate refeeding, N balance improved to -3.1 g N/day, whereas leucine flux decreased by a further 18% (P less than 0.05). Protein and carbohydrate refeeding were associated with further 23 and 31% reductions of 3-methylhistidine excretion compared with prolonged fasting (P less than 0.05). The results support the hypothesis that improved efficiency of protein retention in starvation is intimately associated with a decreased rate of protein turnover.
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PMID:Protein metabolic effects of a prolonged fast and hypocaloric refeeding. 218 64

Endogenous excretion of nitrogenous products was studied during early starvation in six healthy, nonobese subjects after six days on a well-defined diet, designed to achieve net protein balance and an adequate calorie supply. The diet contained 0.5 g myofibrillar-free protein and 35 kcal/kg body weight. The subjects then fasted for three days. Urine was collected for 24-hour periods and analyzed for urea, ammonia, 3-methylhistidine, and 1-methylhistidine. Blood glucose and serum urea levels were measured daily. In a second group of subjects, muscle biopsies for determination of free amino acid concentrations were taken in the overnight fasted state and after three days of fasting. During the period with a balanced diet, urea production fell initially and stabilized after two to three days at a level of 146 +/- 15 mmol/24 h. During the period of fasting, serum urea increased from 3.0 +/- 0.4 to a maximum value of 6.2 +/- 0.7 mmol/L and urea production rose markedly, to a peak of 293 +/- 16 mmol/24 h. Ammonia excretion was 24 +/- 2 mmol/24 h before and 71 +/- 13 mmol/24 h after three days of fasting. 3-Methylhistidine excretion was stable before fasting and then rose from 154 +/- 17 to 198 +/- 17 mumol/24 h. 1-Methylhistidine excretion was unchanged during fasting. Blood glucose levels were stable at 4.8 +/- 0.2 mmol/L before fasting and then fell to 3.7 +/- 0.3 mmol/L. Intracellular concentrations of amino acids in skeletal muscle decreased markedly during fasting; after three days of fasting the glutamine concentration had fallen by 34%.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Protein and amino acid metabolism during early starvation as reflected by excretion of urea and methylhistidines. 259 32

In order to examine the effects of streptozotocin-induced diabetes, dietary protein, and starvation on protein degradation in skeletal muscle of perfused rat hindquarters, rates of myofibrillar and total protein degradation were estimated from the release of 3-methylhistidine (N tau-methylhistidine, 3-MH) and tyrosine, respectively. In rats fed a 20% protein diet (controls), the fractional degradation rate of myofibrillar protein was approximately 56% of the total muscle protein. In streptozotocin-induced diabetic rats, 3-MH release by perfused muscle increased significantly on d 1 of treatment and sustained a high level thereafter. By contrast, tyrosine release did not change. Feeding a 50% protein diet for 1 wk altered neither 3-MH nor tyrosine release. Protein-free feeding, though, suppressed tyrosine release to 49% of controls, but did not affect 3-MH release. Starvation for 3 d did not affect tyrosine release, but did increase 3-MH release to 203% of controls. These results indicate that in diabetic and starved rats myofibrillar protein is preferentially degraded, while in protein-deficient rats, non-myofibrillar protein degradation is selectively suppressed. From these observations, we conclude that the degradation of myofibrillar and non-myofibrillar proteins in skeletal muscle can be differentially regulated.
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PMID:Differential regulation of the degradation of myofibrillar and total proteins in skeletal muscle of rats: effects of streptozotocin-induced diabetes, dietary protein and starvation. 264 2


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