Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0038187 (starvation)
 24,951 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

During the first half of gestation in the rat, maternal net body weight increases rapidly, whereas in the second half of gestation, the mass of maternal structures declines, coincident with the rate of maternal fat accumulation. Enhanced maternal food intake, extrahepatic tissue lipoprotein lipase (LPL) activity, and adipose tissue lipogenesis are responsible for the progressive accumulation of maternal fat. However, during late gestation, decreased fat synthesis in maternal adipose tissue, enhanced lipolytic activity, and decreased LPL activity deplete maternal fat depots. These changes, plus enhanced endogenous production of triglyceride-rich lipoproteins, are also responsible for maternal hypertriglyceridemia. This condition benefits the offspring in two ways: 1) enhanced LPL activity in maternal liver when fasting increases triglyceride consumption for ketone body synthesis, giving the basis for accelerated starvation; and 2) induction of LPL activity in the mammary gland before parturition diverts maternal circulating triglycerides to milk synthesis in preparation for lactation. The magnitude of the maternal-fetal glucose transfer was higher than that of any of the other substrates studied, including alanine, and despite actions to spare glucose, this transfer causes maternal hypoglycemia, which is especially intense in the fasting condition. This increases sympathoadrenal activity in the mother, which may contribute to her active gluconeogenesis. Glycerol was a more efficient glucose precursor than alanine and pyruvate, and whereas glycerol placental transfer is very small, it is proposed that the fetus benefits from this product of adipose tissue lipolysis when it is previously converted into glucose.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Intermediary metabolism in pregnancy. First theme of the Freinkel era. 174 73

In contrast to what it is observed during starvation, animals maintained on a protein-free isocaloric diet showed an increase in the rate of hepatic peptide chain elongation as determined by measuring the ribosomal transit time in vivo. The loss of body nitrogen per se is insufficient to generate the signal(s) which arrests hepatic peptide chain elongation. This observation suggests that it is an increase in gluconeogenic demand, and not the negative nitrogen balance, which is implicated in determining reciprocal changes in the rate of protein synthesis. The rate of protein synthesis, as expressed per mg of DNA, does not change in protein deprived animals, while the RNA to DNA ratio decreased. These data also agree with a higher ribosomal efficiency at the elongation step. The animals maintained on a protein-free diet have a decreased hepatic content of protein and an increased concentration of valine, indicating an increased proteolysis. The enhanced rate of polypeptide elongation observed in animals kept on a protein-free diet was accompanied by decreases in the state of aggregation of polyribosomes and in the ability of liver extracts to form eIF-2 catalyzed ternary complexes. These observations suggest that the activity of the hepatic initiation factor in vivo may not be rate limiting. The administration of alanine in vivo to animals maintained on a protein-free diet showed a preferential effect in reaggregating polyribosomes. This action was neither accompanied by detectable effects on the rate of eIF-2 catalyzed ternary complexes formation nor by significant changes in the rate of elongation.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effect of alanine supply on hepatic protein synthesis in animals maintained on a protein free diet. 177 57

Na(+)-dependent L-Alanine and Glycine uptake by rat red blood cells were best fit to a common model of two transport components, saturable transport and diffusion. 24 hours of food deprivation provoked statistically significant increases of the Km and Vmax red cells L-Alanine uptake, whereas the diffusion constant did not change in response to starvation. The Glycine uptake kinetics poorly follows the L-Alanine pattern and no significant response to starvation can be outlined. The physiological meaning of these adaptations has to be related to short term food deprivation regulation, independent of protein synthesis in the erythrocytes. Such mechanisms could be important to account for the previously described changes in the distribution patterns of amino acids between the blood plasma and blood cell compartments in response to short term starvation.
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PMID:Short term starvation-induced changes in the kinetic parameters of rat red cell L-alanine and glycine uptake. 181 Feb 54

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

Urine from mutant mice which lack D-amino-acid oxidase contained a large amount of D-alanine. The alanine content was not changed by changes in the dietary composition or by starvation. However, oral administration of an antibiotic, amoxicillin, decreased the urinary alanine to the normal level. These results suggest that the D-alanine is not of dietary origin but of intestinal bacterial origin.
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PMID:Intestinal bacterial origin of D-alanine in urine of mutant mice lacking D-amino-acid oxidase. 197 33

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

In the present study glucose kinetic parameters like pool size, distribution volume and rates of total entry and irreversible loss were determined in four castrated male African pygmy goats during hyperglycemia induced by an intravenous glucocorticoid injection (0.25 mg dexamethasone = DXM per kg body weight). Experiments were done at two different metabolic states, "fed" once daily and "fasted" after three days of starvation. The use of [U-14C]- together with [2-3H]- or [6-3H]-glucose made it possible to show changes in rates of gluconeogenesis, phosphorylation and specific recycling of glucose-C (e.g. lactate/alanine). During glucocorticoid induced hyperglycemia (+45%) in fed animals de novo synthesis of glucose (+5%) and lactate/alanine recycling increased (+4%). Rates of irreversible loss for all applied tracers in fasted animals formed only two thirds of the values of fed animals. During hyperglycemia (+40%) after DXM-injection de novo synthesis of glucose (+8%) and lactate/alanine recycling also increased (+27%). Furthermore the rate of phosphorylation of glucose decreased in fasted pygmy goats. The increase in availability of glucose both in fed and fasted animals is due to an increase in gluconeogenesis. In fasted animals additionally a decrease in the rate of phosphorylation and therefore of the peripheral glucose turnover has to be considered.
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PMID:[The effect of glucocorticoids on glucose metabolism in pygmy goats. 2. Glucose turnover and recycling]. 212 56

Absolute starvation during 2 days induces increased levels of taurine, phosphoethanolamine, ethanolamine, glycine, serine, threonine and decreased levels of aspartate, lysine, methionine and cystine in the rat liver. The ration of nonessential to essential, and glycogenic to ketogenic amino acids increased on the average by 30%. On day 4 of starvation the level of nonessential glycogenic amino acids is significantly lowered, while the concentration of essential ketogenic amino acids is increased. On day 6 essential ketogenic amino acid pool is more increased. On day 10 the shifts in the amino acid pool in the liver are retained, the reduction of alanine and serine content is most typical. The value of D2-Machalanobis, obtained during lineal discriminant analysis of amino acid pool and space distribution of the signs for the control and starving animals (during 10 days), was lower than that on day 4 and 6 of the experiment. The levels of glycine, serine lysine, leucine, glutamate, alanine and aspartate show the highest information content during such investigation of all the groups of animals.
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PMID:[Formation of free fatty acid pool in the liver of rats during starvation]. 227 22

The phoA503 mutant was identified as a mutant that shows a novel phoA regulatory phenotype. The phoA503 allele dramatically reduces the synthesis of bacterial alkaline phosphatase activity during Pi starvation in an otherwise wild-type host and during the logarithmic growth phase in a phoR or phoU background. Near-normal amounts of enzyme activity are found in phoR phoA503 or phoU phoA503 mutants when starved for carbon, nitrogen, or sulfur or during the stationary phase, however. Marker rescue and DNA sequence analysis located the phoA503 mutation to the phoA coding region. It is a C-to-T transition that would cause a substitution of Val for Ala-22 in the mature protein. Transcriptional and translational lacZ fusions to both wild-type and mutant alleles demonstrated that phoA gene expression is unaltered. Also, the mutant protein was secreted and processed as efficiently as the wild type. Furthermore, the subunits appeared to dimerize and to be stable in the periplasm. But, greater than 98% of the dimers were inactive and found exclusively as isozyme 1. An activation of preformed phoA503 dimers occurred during the stationary phase with the concomitant conversion into isozymes 2 and 3. We propose that the phoA503 mutation affects a late stage in the formation of active enzyme. An unknown change when Pi is present during stationary-phase growth leads to formation of active dimers, which is responsible for this new conditional phenotype.
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PMID:A phoA structural gene mutation that conditionally affects formation of the enzyme bacterial alkaline phosphatase. 234 42


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