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)

1. The maximum activity of hexokinase in lymphocytes is similar to that of 6-phosphofructokinase, but considerably greater than that of phosphorylase, suggesting that glucose rather than glycogen is the major carbohydrate fuel for these cells. Starvation increased slightly the activities of some of the glycolytic enzymes. A local immunological challenge in vivo (a graft-versus-host reaction) increased the activities of hexokinase, 6-phosphofructokinase, pyruvate kinase and lactate dehydrogenase, confirming the importance of the glycolytic pathway in cell division. 2. The activities of the ketone-body-utilizing enzymes were lower than those of hexokinase or 6-phosphofructokinase, unlike in muscle and brain, and were not affected by starvation. It is suggested that the ketone bodies will not provide a quantitatively important alternative fuel to glucose in lymphocytes. 3. Of the enzymes of the tricarboxylic acid cycle whose activities were measured, that of oxoglutarate dehydrogenase was the lowest, yet its activity (about 4.0mumol/min per g dry wt. at 37 degrees C) was considerably greater than the flux through the cycle (0.5mumol/min per g calculated from oxygen consumption by incubated lymphocytes). The activity was decreased by starvation, but that of citrate synthase was increased by the local immunological challenge in vivo. It is suggested that the rate of the cycle would increase towards the capacity indicated by oxoglutarate dehydrogenase in proliferating lymphocytes. 4. Enzymes possibly involved in the pathway of glutamine oxidation were measured in lymphocytes, which suggests that an aminotransferase reaction(s) (probably aspartate aminotransferase) is important in the conversion of glutamate into oxoglutarate rather than glutamate dehydrogenase, and that the maximum activity of glutaminase is markedly in excess of the rate of glutamine utilization by incubated lymphocytes. The activity of glutaminase is increased by both starvation and the local immunological challenge in vivo. This last finding suggests that metabolism of glutamine via glutaminase is important in proliferating lymphocytes.
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PMID:Maximum activities of some enzymes of glycolysis, the tricarboxylic acid cycle and ketone-body and glutamine utilization pathways in lymphocytes of the rat. 716 29

The glucose replacement rate, plasma glucose concentration, glucose body mass, and amino acid gluconeogenesis were determined in vivo in fed and fasted kelp bass (Paralabrax clathratus) using [6-3H]glucose administered with [U-14C]glutamate, [U-14C]aspartate, or [U-14C]alanine. Fasting (14 days) and prolonged starvation (72 days) do not produce changes in the replacement rate, body mass, or plasma concentration of glucose. The removal of amino acids from the circulation is rapid in both fed and fasting states with nearly 50% of the administered 14Ctracer disappearing by 5 min. The incorporation of [14C]amino acid carbon into the body glucose mass is also rapid with significant amounts of tracer appearing within 15 min after administration. Gluconeogenesis from alanine and glutamate is increased by fasting whereas that from aspartate is diminished. The gluconeogenic rate is comparable to that previously observed in rats (Dunn, A., M. Chenoweth, and J. G. Hemington. The relationship of adrenal glucocorticoids to transaminase activity and gluconeogenesis in the intact rat. Biochim. Biophys. Acta 237: 192-202, 1971), although the glucose replacement rate is significantly lower. We propose that the paradoxically high rate of gluconeogenesis in fish may serve to provide carbohydrate precursors for mucus synthesis in these carnivorous animals with limited carbohydrate intake.
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PMID:Amino acid gluconeogenesis and glucose turnover in kelp bass (Paralabrax sp.). 721 97

Amino acids adsorbed onto blood cell membranes represent about 8% of the total amino acids in blood. The aim of this study was to determine the in vitro adsorption kinetics of different amino acids (L-alanine, glycine, L-glutamate, L-glutamine, L-phenylalanine and L-leucine) onto rat erythrocyte membranes and to assess the effect of 24-hr starvation on these adsorption kinetics. Isolated red cell membranes were incubated at 37 degrees C for 10 sec in the presence of 14C-amino acids--with different specific radioactivity--the radioactivity retained in the membrane fraction measured and kinetic parameters of amino acid adsorption determined. With the exception of glutamate, where the adsorption was negligible, all amino acids studied were adsorbed onto isolated red cell membranes, adhering to simple Michaelis-Menten kinetics. Km' values of glycine, phenylalanine and leucine adsorption in control rats (14.7 +/- 3.8 mM, 8.41 +/- 0.95 mM and 4.65 +/- 0.46 mM respectively, SEM, n = 6-8) decreased in response to 24-hr starvation, giving the following values: 0.792 +/- 0.122 mM, 5.32 +/- 0.82 mM and 3.53 +/- 0.31 mM respectively (SEM, n = 6-8), Vmax' value of glycine adsorption of control rats decreased (from 61.0 +/- 15.5 mmol/mol P/sec to 4.25 +/- 0.70 mmol/mol P/sec, SEM, n = 7) and that of leucine increased (from 13.5 +/- 1.0 mmol/mol P/sec to 18.9 +/- 2.0 mmol/mol P/sec, SEM, n = 7) as an effect of 24-hr starvation. This study shows that alanine, glycine, glutamine, phenylalanine and leucine, but not glutamate, adsorbed onto erythrocyte membranes according to Michaelis-Menten-like kinetics.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:In vitro adsorption of amino acids onto isolated rat erythrocyte membranes. 758 9

This study has focused on the possible influence of microtubules for the regulation of Na(+)-dependent system A neutral amino acid transport in A10 cells, a cultured cell line derived from rat aortic vascular smooth muscle. When microtubules were disrupted by incubating cells for 5 h in serum-free medium containing colchicine, nocodazole, or vinblastine, there was a twofold increase in system A transport (Vmax change). The dose for the disruption of microtubules by colchicine was similar to the dose required for the stimulation of system A. The time course showed that system A stimulation did not occur until widespread disruption of microtubules was established. The stimulation was specific for system A; there were no changes in glucose transport and Na(+)-dependent transport of phosphate and glutamate. Serum refeeding of quiescent cells from 2 days of serum starvation led to stimulation of system A, glucose, and phosphate transport. However, only system A was activated when colchicine was added to the serum-free medium. Addition of colchicine during serum refeeding had no additive effect for the stimulation of system A. The stimulation by both colchicine and serum was blocked by cycloheximide and actinomycin D. These findings suggest that microtubule disruption may activate system A gene expression.
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PMID:Microtubule disruption stimulates system A transport in cultured vascular smooth muscle cells. 761 72

Nitrogen regulation of transcription in Escherichia coli requires sensation of the intracellular nitrogen status and control of the dephosphorylation of the transcriptional activator NRI-P. This dephosphorylation is catalyzed by the bifunctional kinase/phosphatase NRII in the presence of the dissociable PII protein. The ability of PII to stimulate the phosphatase activity of NRII is regulated by a signal transducing uridylyltransferase/uridylyl-removing enzyme (UTase/UR), which converts PII to PII-UMP under conditions of nitrogen starvation; this modification prevents PII from stimulating the dephosphorylation of NRI approximately P. We used purified components to examine the binding of small molecules to PII, the effect of small molecules on the stimulation of the NRII phosphatase activity by PII, the retention of PII on immobilized NRII, and the regulation of the uridylylation of PII by the UTase/UR enzyme. Our results indicate that PII is activated upon binding ATP and either 2-ketoglutarate or glutamate, and that the liganded form of PII binds much better to immobilized NRII. We also demonstrate that the concentration of glutamine required to inhibit the uridylyltransferase activity is independent of the concentration of 2-ketoglutarate present. We hypothesize that nitrogen sensation in E. coli involves the separate measurement of glutamine by the UTase/UR protein and 2-ketoglutarate by the PII protein.
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PMID:The Escherichia coli PII signal transduction protein is activated upon binding 2-ketoglutarate and ATP. 762 80

Glutamate excretion due to amino acid starvation was investigated in "stringent" and "relaxed" strains of Escherichia coli. The observed excretion process is relA-dependent, carrier-mediated, and glutamate-specific. After induction, excretion was detected within less than 2 min and continued for more than 5 h with a rate of 7-10 nmol (mg dry weight)-1 min-1. Using carbonyl cyanide m-chlorophenylhydrazone or polymyxin B nonapeptide, together with valinomycin, it was shown that glutamate excretion is driven by the membrane potential.
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PMID:Glutamate excretion in Escherichia coli: dependency on the relA and spoT genotype. 764 16

The mutant gene responsible for obesity in the ob/ob mouse was recently identified by positional cloning (Zhang Y., R. Proenca, M. Maffel, M. Barone, L. Leopold, and J.M. Friedman. 1994. Nature (Lond.) 372:425). The encoded protein and to represent and "adipostat" signal reflecting the state of energy stores. We confirm that the adipocyte is the source of ob mRNA and that the predicted 16-kD ob protein is present in rodent serum as detected by Western blot. To evaluate the hypothesis that it might represent an adipostat, we assessed serum levels of ob protein and expression of ob mRNA in adipose cells and tissue of rodents in response to a variety of perturbations which effect body fat mass. Both ob protein and ob mRNA expression are markedly increased in obesity. The levels of ob protein are approximately 5-10-fold elevated in serum of db/db mice, in mice with hypothalamic lesions caused by neonatal administration of monosodium glutamate (MSG), and in mice with toxigene induced brown fat ablation, (UCP-DTA). Very parallel changes are observed in adipocyte ob mRNA expression in these models and in ob/ob mice. As predicted however, no serum ob protein could be detected in the ob/ob mice. By contrast to obesity, starvation of normal rats and mice for 1-3 d markedly suppresses ob mRNA abundance, and this is reversed with refeeding. Similarly, ob protein concentration in normal mice falls to undetectable levels with starvation. In the ob/ob, UCP-DTA and MSG models, overexpression of ob mRNA is reversed by caloric restriction. These data support the hypothesis that expression of ob mRNA and protein are regulated as a function of energy stores, and that ob serves as a circulating feedback signal to sites involved in regulation of energy homeostasis.
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PMID:Expression of ob mRNA and its encoded protein in rodents. Impact of nutrition and obesity. 765 36

L-Glutamate stimulates the liberation of arachidonic acid from mouse striatal neurons via the activation of N-methyl-D-aspartic acid (NMDA) receptors and by the joint stimulation of alpha-amino-3-hydroxy-5-methylisoxazole-4-propionate (AMPA) and metabotropic receptors. In this study, we investigated whether starving cultured mouse striatal neurons of glucose would modify glutamatergic receptor-mediated arachidonic acid release. Glucose deprivation for 30 min led to enhancement of the NMDA-evoked release of arachidonic acid, compared with that observed in the presence of glucose. This enhanced response depended on both the concentration of glucose and the length of time of glucose deprivation. The enhanced NMDA response appeared to result from both a release of glutamate and the subsequent additional release of arachidonic acid due to the activation of AMPA and metabotropic receptors. Indeed, the increased NMDA response was completely reversed when extracellular glutamate was enzymatically removed. Moreover, glucose deprivation potentiated the combined AMPA/metabotropic receptor-evoked release of arachidonic acid, even in the absence of extracellular glutamate. However, removing glucose did not improve the calcium rise induced by AMPA or NMDA. The ATP-evoked release of arachidonic acid from striatal astrocytes was not altered by glucose starvation. In summary, glucose deprivation affected two properties of striatal neurons: (a) it induced an NMDA-evoked release of glutamate from striatal neurons and (b) it selectively potentiated the AMPA/(1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-evoked release of [3H]arachidonic acid without altering the authentic NMDA-mediated response.
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PMID:Glucose regulates glutamate-evoked arachidonic acid release from cultured striatal neurons. 779 Aug 66

Pathways of L-glutamate and L-aspartate import by HeLa S3 cells were investigated before and after the cells were depleted of internal amino acids by starvation. Two new regulations of transport were observed in starved cells. Aspartate entered nonstarved cells by two routes, one non-saturable and one, an apparent analog of saturable system X-AG, that was sodium-dependent and competitively inhibited by glutamate. Starvation for one hour in saline increased the efficiency of saturable aspartate import, increasing Vmax and decreasing Km, an effect not previously reported for system X-AG. Glutamate uptake by nonstarved cells appeared to occur through system X-AG; through an analog of system X-C, which was sodium-independent, cystine- and quisqualate-inhibitable; as well as through one or more nonsaturable pathways. Starvation in saline for one hour resulted in the appearance of a new low-affinity saturable glutamate uptake system. This new system was sodium-dependent but not inhibited by aspartate.
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PMID:Novel regulations of glutamate and aspartate uptake by HeLa cells. 786 40

Effects of starvation and glucose preincubation on membrane potential, ATPase-mediated acidification and glutamic acid transport were studied in yeast species Saccharomyces cerevisiae, Schizosaccharomyces pombe, Dipodascus magnusii, Lodderomyces elongisporus and Rhodotorula gracilis. The membrane potential was highest after preincubation with glucose in all species but L. elongisporus and R. gracilis. In all cases the membranes were depolarized in the presence of 20 mmol/L KCl and hyperpolarized with 50 mumol/L diethylstilbestrol (DES). The extracellular acidification caused by addition of glucose was highest after preincubation with glucose in all cases except in R. gracilis where there was none. In all cases except in R. gracilis addition of KCl caused a marked increase in the acidification rate. Addition of DES with glucose caused a large decrease in rate in S. cerevisiae but had much less effect on the other species. Transport of glutamic acid was clearly increased after pretreatment with glucose in S. cerevisiae, S. pombe and D. magnusii (mainly due to enhanced synthesis of the carrier) but actually decreased in R. gracilis and L. elongisporus. Addition of DES had an inhibitory effect in all species but much more pronounced in S. cerevisiae and S. pombe than in others. In general, both the acidification and the transport of glutamate were enhanced after preincubation with glucose but much more so in the semianaerobic species, such as S. cerevisiae, than in the strict aerobes (R. gracilis) where the effect was occasionally negative. There was no relationship between the ATPase-mediated acidification and the membrane potential.
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PMID:Effects of the physiological state of five yeast species on H(+)-ATPase-related processes. 790 55


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