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

4 children with ketotic hypoglycemia (KH) showed during a fasting period over 24 hours significant higher decreases of serum alanine levels than normal controls. Insulin induced hypoglycemia was followed by only minimal increase of urine epinephrine secretion, while all controls showed more than 6 times higher increases. 2-desoxy-glucose-tests were pathological in all cases with KH. One can speculate, that there is a connection between the reduced availability of alanine and the adrenal medullary hyporesponsiveness. Epinephrine stimulates glycogenolysis in muscle cells. Lack of epinephrine reduces pyruvate production and subsequently alanine synthesis. Alanine however is essential for gluconeogenesis in liver cells especially during starvation. After some days administration of diazoxide the 2-desoxy-glucose-test was normalised in all patients. This observation could probably be of some interest in therapy of KH.
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PMID:[Pathogenesis of ketotic hypoglycemia (author's transl)]. 41 97

We studied the effects of glucose, alanine, and saline infusion in newborn guinea pigs. After acute (24-30 h after delivery) or prolonged (96-100 h after delivery) starvation, alanine or glucose infusion significantly increased liver glycogen concentration. Alanine infusion increased plasma glucose concentration and urea production rate (UrP). After acute starvation, a continuous 12-hour glucose infusion did not affect either plasma alanine concentration or UrP; however, after prolonged starvation, glucose infusion significantly reduced both variables. After prolonged starvation, the newborn guinea pig mobilizes alanine for gluconeogenesis. Increased protein catabolism is a consequence of this process. Glucose infusion negates the need for gluconeogenesis and spares body protein.
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PMID:The effects of glucose and alanine infusion on urea production and gluconeogenesis in the starved newborn guinea pig. 65 23

In vitro studies have suggested that catabolism of branched chain amino acids is linked with alanine and glutamine formed in, and released from, muscle. To explore this possibility in vivo, static and kinetic studies were performed in three patients with classical, and one patient with partial, branched chain alpha-ketoacid decarboxylase deficiency (maple syrup urine disease, MSUD) and compared to similar studies in eight age-matched controls. The subjects underwent a 24-30-h fast, and a glucose-alanine flux study using stable isotopes. Basal plasma leucine concentrations were elevated (P <0.001) in patients with MSUD (1,140+/-125 muM vs. 155+/-18 muM in controls); and in contrast to the controls, branched chain amino acid concentrations in plasma increased during the fast in the MSUD patients. Basal plasma alanine concentrations were lower (P <0.01) in patients with classical MSUD (153+/-8 muM vs. 495+/-27 muM in controls). This discrepancy was maintained throughout the fast despite a decrease in alanine concentrations in both groups. Plasma alanine and leucine concentrations in the patient with partial MSUD were intermediate between those of the controls and the subjects with the classical form of the disease. Circulating ketone bodies and glucoregulatory hormones concentrations were similar in the MSUD and normal subjects during the fast. Alanine flux rates in two patients with classical MSUD (3.76 and 4.00 mumol/Kg per min) and the patient with partial MSUD (5.76 mumol/Kg per min) were clearly lower than those of the controls (11.72+/-2.53 [SD] mumol/Kg per min). After short-term starvation, glucose flux and fasting concentrations were similar in the MSUD patients and normal subjects.These data indicate that branched chain amino acid catabolism is an important rate limiting event for alanine production in vivo.
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PMID:Glucose and alanine metabolism in children with maple syrup urine disease. 67 Apr

Experiments were conducted to investigate plasma free amino acid concentrations in the chick. After one hour of fasting, total plasma amino acid concentration decreased to approximately half of the full-fed value. Within three to six hours, most amino acids had returned toward the full-fed level but did not exceed it throughout a 48 hour period of starvation. However, after 48 hours fasting lysine, threonine, and isoleucine accumulated three-fold, two-fold and two-fold of the full-fed level, respectively. Serine and glutamic acid exceeded the full-fed level at three hours and then declined. Alanine reached its highest level after six hours of fasting and then declined. In full-fed chicks diurnal variations of plasma free amino acid concentrations were observed. The lowest and highest concentrations were observed at 11 a.m. and 8 to 11 p.m., respectively under a 24 hr-lighting. Reference plasma amino acid patterns are reported for chicks fed a practical diet ad libitum. In day-old chicks, concentrations of total amino acids, methionine plus one half cystine, lysine, and arginine were high. Alanine and glutamic acid concentrations were low. Most amino acid concentrations declined gradually during the first four weeks of life, but methionine plus one half cystine, phenylalaine, threonine and serine concentrations decreased sharply between two and four weeks. Lysine concentration continued to decrease in chicks fed the starter diet. At 20 weeks, plasma amino acid concentrations had decreased considerably except for methionine plus one half cystine and basic amino acids. The plasma amino acid pattern for chicks fed an isolated soybean protein diet was similar to that of chicks fed the practical diet.
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PMID:Conditions affecting plasma amino acid patterns in chickens fed practical and purified diets. 103 38

A reduction in the release of substrate amino acids from skeletal muscle largely explains the decrease in gluconeogenesis characterizing prolonged starvation. Brief starvation is associated with an increase in gluconeogenesis, suggesting increased release of amino acids from muscle. In the present studies, accelerated amino acid release from skeletal muscle induced by brief starvation was sought to account for the accompanying augmentation of gluconeogenesis. To do this amino acid balance across forearm muscles was quantified in 15 postabsorptive (overnight fasted) subjects and in 7 subjects fasted for 60 h. Fasting significantly reduced basal insulin (11.3-7.5 muU/ml) and increased glucagon (116-134 pg/ml). Muscle release of the principal glycogenic amino acids increased. Alanine release increased 59.4%. The increase in release for all amino acids averaged 69.4% and was statistically significant for threonine, serine, glycine, alanine, alpha-aminobutyrate, methionine, tyrosine, and lysine. Thus, with brief starvation, muscle release of glycogenic amino acids increases strikingly. This contrasts with the reduction of amino acid release characterizing prolonged starvation. The adaptation of peripheral tissue metabolism to brief starvation is best explained by the decrease in insulin.
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PMID:Effects of brief starvation on muscle amino acid metabolism in nonobese man. 125 28

Following an oral 14C-alanine load, obese Zucker rats showed the same rate of intestinal amino acid absorption as their lean counterparts. Alanine absorption was unchanged by a 24 h starvation period. The whole-body oxidation of the absorbed tracer was lower in the fa/fa rats and was significantly decreased in both lean and obese groups when the animals were submitted to starvation. The incorporation of the 14C-tracer into 14C-lipid was significantly higher in the carcass, skeletal muscle, white adipose tissue and liver of the obese animals, while that of brown adipose tissue was decreased as compared to that of the lean rats. Starvation induced no variation in 14C-lipid incorporation in the lean (+/?) animals while it sharply decreased this parameter in the obese. The incorporation of the tracer into 14C-glycogen and 14C-protein was also increased in the liver of the obese rats while no changes in incorporation into these fractions were observed in skeletal muscle. It is concluded that dietary amino acids significantly contribute to the hyperlipogenesis found in the liver and adipose tissue of the fa/fa rats.
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PMID:The metabolic fate of an oral 14C-alanine load in the obese Zucker rat. 131 31

Kinetics of intestinal transport of L-alanine and L-valine (substrates of the A-system and the L-system, respectively, in mammals) across the brush-border membrane in sea bass, Dicentrarchus labrax, were studied on intact mucosa using a short-term uptake technique. When fish were starved for 4-8 weeks, total influx (mucosa-to-cell) of valine fell owing to disappearance or modification of the diffusion component. The maximum influx rate of saturable component increased but its affinity (reflected by the Michaelis constant) decreased. Alanine transport by Na(+)-dependent and diffusion pathways was unchanged after starvation. Fasting also induced an almost 20% decrease in the length of intestinal microvilli.
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PMID:Effects of starvation on valine and alanine transport across the intestinal mucosal border in sea bass, Dicentrarchus labrax. 140 35

400 MHz 1H NMR spectroscopy was used to analyze methyl group-containing metabolites in perchloric acid extracts of livers of rats treated with carbon tetrachloride or fed with ethanol-containing liquid diets, and sacrificed with carbon dioxide anoxic euthanasia or pentobarbital euthanasia (with or without 12-18 hour fasting). In all cases, coenzyme A was detected using 1H NMR spectroscopy, but at higher levels for chronic ethanol-treated rats. Propionate was also detected in livers 6 hours after treatment with carbon tetrachloride. The assignments of the 1H NMR resonances in a spectrum of biological origin to these two metabolites have not been previously reported. Another unusual metabolite, 1,2-propanediol, was also observed in dramatically elevated levels in starved rats. The methyl groups for coenzyme A, propionate, and 1,2-propanediol have 1H NMR chemical shifts at 0.73 and 0.87 ppm, 1.18 ppm, and 1.14 ppm (from tetramethylsilane) respectively. In addition to the above mentioned resonances, glutamine, glutamate, proline, acetate, leucine, alanine, lactate, ethanol, beta-hydroxybutyrate, and valine were also observed in the 0.5-2.3 ppm methyl region of the 1H NMR spectra. Biochemical changes were also observed in these latter metabolites. beta-Hydroxybutyrate was increased by chronic ethanol administration; this increase was exacerbated by starvation. Alanine was decreased by chronic ethanol administration. Acetate was increased by chronic ethanol administration except when glycerol was added to the liver or when the rat was starved. We also observed an unassigned triplet at 0.81 ppm, and its appearance seems to be correlated with that of 1,2-propanediol.
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PMID:1H NMR analyses of methyl group-containing metabolites in rat liver extracts--effects of starvation, anoxia, acute glycerol and carbon tetrachloride treatment and chronic ethanol administration on hepatic metabolism. 181 3

An approach to broaden the product range of the ethanologenic, gram-negative bacterium Zymomonas mobilis by means of genetic engineering is presented. Gene alaD for L-alanine dehydrogenase (EC 1.4.1.1.) from Bacillus sphaericus was cloned and introduced into Z. mobilis. Under the control of the strong promoter of the pyruvate decarboxylase (pdc) gene, the enzyme was expressed up to a specific activity of nearly 1 mu mol . min -1 . mg of protein -1 in recombinant cells. As a results of this high L-alanine dehydrogenase activity, growing cells excreted up to 10 mmol of alanine per 280 mmol of glucose utilized into a mineral salts medium. By the addition of 85 mM NH4+ to the medium, growth of the recombinant cells stopped, and up to 41 mmol alanine was secreted. As alanine dehydrogenase competed with pyruvate decarboxylase (PDC) (EC 4.1.1.1.) for the same substrate (pyruvate), PDC activity was reduced by starvation for the essential PDC cofactor thiamine PPi. A thiamine auxotrophy mutant of Z. mobilis which carried the alaD gene was starved for 40 h in glucose-supplemented mineral salts medium and then shifted to mineral salts medium with 85 mM NH4+ and 280 mmol of glucose. The recombinants excreted up to 84 mmol of alanine (7.5 g/liter) over 25 h. Alanine excretion proceeded at an initial velocity of 238 nmol . min-1 . mg [dry weight]-1. Despite this high activity, the excretion rate seemed to be a limiting factor, as the intracellular concentration of alanine was as high as 260 mM at the beginning of the excretion phase and decreased to 80 to 90 mM over 24 h.
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PMID:Expression of an L-alanine dehydrogenase gene in Zymomonas mobilis and excretion of L-alanine. 185 97

Alanine metabolism in 24 hour starved 20-day pregnant rats, following intravenously administered C14-alanine, in trace dose that does not affect the normal availability of this amino acid, has been studied. The steady state levels of alanine and glucose in blood, liver and skeletal muscle, together with the tissue glycogen, metabolites and amino acid composition pools, are given in both the maternal and foetal compartments compared with the virgin control rats. The utilization of alanine as a gluconeogenetic precursor is not increased in late pregnancy under 24-hour starvation and it depends on the lower blood substrate availability.
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PMID:In vivo alanine metabolism in late pregnant rats. 207 92


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