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

The general control of amino acid biosynthesis was investigated in Candida spec. EH 15/D, using single and double mutant auxotrophic strains and prototrophic revertants starved for their required amino acids. These experiments show that starvation for lysine, histidine, arginine, leucine, threonine, proline, serine, methionine, homoserine, asparagine, glutamic acid or aspartic acid can result in derepression of enzymes. A correlation was found between the degree of derepression, growth of strains, and concentration of required amino acids. The amino acids pool pattern of mutants and revertants is different from that in the wild type strain.
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PMID:[General control of amino acid biosynthesis in mutants of Candida spec. EH 15/D]. 663 44

Chinese hamster ovary (CHO) cells were subjected to severe amino acid starvation for histidine, leucine, methionine, asparagine, tyrosine, glutamine, valine, and lysine, using amino acid analogs or mutations in specific aminoacyl-tRNA synthetases. At protein synthetic rates of less than 5%, in all cases, the newly synthesized proteins were found on two-dimensional electrophoretic gels to consist of a few intensely labeled spots, with the exception of lysine. This pattern could also be produced by strong inhibition of cytoplasmic protein synthesis with cycloheximide, and was abolished by preincubation with the mitochondrial protein synthesis inhibitor chloramphenicol. It appears therefore that the spots represent mitochondrial protein synthesis and that animal cells must have separate aminoacyl-tRNA synthetases for mitochondrial tRNAs corresponding to all these amino acids except, possibly, for lysine.
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PMID:Selective synthesis of mitochondrial proteins by Chinese hamster ovary cells severely starved for various amino acids. 671 12

Certain strains of Escherichia coli mistranslate at very high frequencies when starved for asparagine or histidine. This mistranslation is the result of misreading events on the ribosome. The introduction of a hisT mutation into such a strain decreases the frequency of mistranslation during histidine starvation but not during asparagine starvation. The most likely explanation is that the replacement of the pseudouridine residue in the anticodon loop of glutamine specific transfer ribonucleic acid by uridine in hisT mutants leads to an increase in fidelity of transfer ribonucleic acid function. The hisT gene in Escherichia coli has also been more accurately mapped, giving the gene order purF-hisT-aroC-fadL-dsdA.
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PMID:Specific mistranslation in hisT mutants of Escherichia coli. 675 59

Strains of Escherichia coli were starved for asparagine or lysine in order to increase the in vivo level of mistranslation. In a relA strain, asparagine starvation increased the error frequency in elongation factor Tu to 0.12 mistake per asparagine codon, while with lysine starvation in the same strain the error frequency per lysine codon was 0.008. The pattern of isoelectric point changes in the altered protein produced is consistent with third position misreading in the AAN codon group. This high level of mistranslation is not seen in streptomycin resistant (rpsL) strains or in most relA+ strains.
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PMID:"Two out of three" codon reading leading to mistranslation in vivo. 676 67

The coat protein of the bacteriophage MS2 was found to show an increased level of charge heterogeneity when synthesized in Escherichia coli starved for Asn or Lys. No such increase was found when the host was starved for Arg, His Ile or Pro. This is the pattern predicted by "two-out-of-three" codon misreading in the coat protein gene. In the case of Asn starvation, direct measurements of the relative incorporation of Lys demonstrate that the observed charge heterogeneity is the result of mistranslation. Asn starvation increased the error frequency in coat protein to over 0.3 mistake per asparagine codon. The small amount of charge heterogeneity seen in unstarved cells seems also to be the result of misreading Asn codons.
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PMID:Mistranslation in cells infected with the bacteriophage MS2: direct evidence of Lys for Asn substitution. 678 Jul 57

Amino acid starvation of a variety of different types of cells has been reported to induce protein degradation and also specific mistranslation. For certain amino acid starvations, the mistranslated protein, which contains specific amino acid substitutions, can be separated and quantified by two-dimensional polyacrylamide gel electrophoresis. In this paper, I show that this specifically mistranslated protein, made during amino acid starvation, does not seem to be preferentially degraded during continued starvation or renewed growth. Specifically mistranslated ribosomal protein is also assembled into ribosomes in the same proportion that it is made. These results imply that the amino acid substitutions apparently made (lysine for asparagine or glutamine or histidine) do not lead to proteins recognized as grossly "abnormal" by the cell's proteolysis systems.
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PMID:Mistranslated protein in Escherichia coli. 702 69

Stimulation of System N transport of glutamine by amino acid starvation of the rat hepatocyte can be repressed by one of its substrates, histidine, but not by two others, glutamine or asparagine. Furthermore, 2-(methylamino)isobutyric acid is also repressive, although it is not perceptibly a substrate or inhibitor of that system. The repression of System A by glutamine proves in contrast not to be dissociated from transport: relatively slow System A uptake of glutamine has now been shown in this cell. System A transport of glutamine is conspicuous in the hepatoma cell HTC and is increased after amino acid starvation of both hepatocytes and the hepatoma cells. Differential repression of the systems could be shown, although lowering the pH prevented the derepression of one system as much as the other on amino acid starvation.
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PMID:Incomplete correspondence between repressive and substrate action by amino acids on transport systems A and N in monolayered rat hepatocytes. 705 75

1. Urate synthesis was measured in hepatocytes from chickens after starvation or high-protein feeding. Adaptation occurred only on the high-protein diet. 2. The theoretical balances of reactions from alanine (5 alanine + 3 O2 = urate + 1.5 glucose + glycine) and asparagine (3 asparagine + 2 O2 = urate + ammonia + 0.5 glucose + glycine) agree reasonably well with the experimental results. 3. Enzymes directly involved in urate synthesis from these amino acids increase up to 12-fold on the high-protein diet; only amidophosphoribosyltransferase activity appears to be rate-limiting for urate synthesis. 4. The processes of nitrogen disposal in chicken and rat are compared and discussed.
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PMID:Adaptation of urate synthesis in chicken liver. 712 10

The utilisation (conversion to CO2 and/or glucose) of a series of amino acids by isolated trout hepatocytes was investigated and compared to the utilisation of lactate and palmitate. In fed fish, several amino acids (alanine, serine, asparagine and glycine) and lactate produced CO2 at considerably higher rates than palmitate. During starvation plus exercise, the rate of CO2 production from palmitate increased while that from lactate and most of the amino acids decreased. Gluconeogenesis from amino acids in fed fish was lower than from lactate. Serine and asparagine were the most effective substrates; alanine gave lower rates of incorporation. During prolonged starvation plus exercise, the rates of gluconeogenesis from amino acids increased twofold and, simultaneously, there was a corresponding increase in phosphoenolpyruvate carboxykinase activity in liver. It is concluded that several amino acids (dietary or released from muscle protein) are potentially major oxidative substrates in trout. In addition, amino acids appear to have the capability to maintain supplies of glucose during a period of prolonged starvation and exercise. No evidence could be found to support the contention that alanine is the most important glucogenic amino acid.
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PMID:Amino acid utilisation in isolated hepatocytes from rainbow trout. 720 13

In the rat hepatocyte, whether freshly separated or in primary culture, we do not find L-glutamine entry by Systems A and ASC as seen in cells previously studied. Instead the mediated entry of glutamine appears to occur exclusively by a Na+-dependent system ("N") apparently specific to amino acid amides and L-histidine; however, a portion of asparagine uptake occurs by System A. The simplest evidence for the separateness of the added system is the failure of model substrates for System A (e.g. N-methylalanine) to inhibit glutamine uptake significantly, and the failure of glutamine to inhibit the uptake of L-cysteine, model substrate for System ASC, at least in this cell. As is the case for cysteine, glutamine inhibits transport by System A (although not competitively), even though showing no transport by that system. Our finding confirms an earlier inference that glutamine uptake by this cell may follow a route not taken by alanine or serine, and explains the apparently erroneous companion inference that glutamine also shares a route with these two amino acids. Its uptake has now been characterized to show a series of differences from Systems A and ASC. Especially significant in view of the importance of glutamine metabolism are an insensitivity of the new system to stimulation by either insulin or glucagon, and its distinct enhancement (not as large as that for System A) on starvation of the cells with respect to amino acids. Hence, a second system has been found to show adaptive regulation.
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PMID:Characteristics of an amino acid transport system in rat liver for glutamine, asparagine, histidine, and closely related analogs. 737 63


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