Amino-Acid Metabolism in Locust Tissues

1957 ◽  
Vol 34 (2) ◽  
pp. 276-289
Author(s):  
B. A. KILBY ◽  
ELISABETH NEVILLE
Keyword(s):  
Amino Acid ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
Schistocerca Gregaria ◽  
Fat Body ◽  
Malpighian Tubule ◽  
Malpighian Tubules ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Mitochondrial Fractions

1. Homogenates of fat-body of Schistocerca gregaria Forsk. were shown to catalyse transamination reactions between α-ketoglutarate and numerous α-amino acids. The aspartate/glutamate and alanine/glutamate transaminases were the most active. They were present in both the ‘soluble’ and the mitochondrial fractions of fat-body cells and also in Malpighian tubules and mid-gut wall. The other transaminases in the fat-body were confined to the mitochondrial fraction. 2. Fat-body, Malpighian tubule and mid-gut wall homogenates were able to convert glutamic acid into glutamine, a compound which could also act as an amino-group donor in some transamination reactions. 3. A glutamate-cytochrome c reductase system which involved diphosphopyridine nucleotide was present in fat-body. 4. Fat-body contained an active arginase, but urease could not be detected. A D-amino-acid oxidase was present, together with a less active L-amino-acid oxidase. 5. In general, it appears that amino-acid metabolism in the locust resembles that in higher animals.

scholarly journals The molecular correlates of organ loss: the case of insect Malpighian tubules

2015 ◽  
Vol 11 (5) ◽  
pp. 20150154 ◽  
Author(s):  
Xiangfeng Jing ◽  
Thomas A. White ◽  
Xiaowei Yang ◽  
Angela E. Douglas
Keyword(s):  
Amino Acid ◽  
Amino Acid Metabolism ◽  
Essential Role ◽  
Acyrthosiphon Pisum ◽  
Acid Metabolism ◽  
Malpighian Tubule ◽  
Malpighian Tubules ◽  
Pea Aphid ◽  
Whole Genome ◽  
Central Importance

Malpighian tubules play an essential role in excretion, osmoregulation and immunity of most insects. Exceptionally, aphids lack Malpighian tubules, providing the opportunity to investigate the fate of genes expressed in an organ that has undergone evolutionary reduction and loss. Making use of the sequenced genomes of Drosophila melanogaster and the pea aphid Acyrthosiphon pisum , we demonstrated that more than 50% of Drosophila genes expressed specifically in the Malpighian tubules had orthologues in the pea aphid genome and that most of the pea aphid orthologues with detectable expression were identified in the gut transcriptome. Relative to the whole genome, genes functioning in amino acid metabolism are significantly over-represented among the pea aphid orthologues of Malpighian tubule genes, likely reflecting the central importance of amino acid acquisition and metabolism in aphids. This study demonstrates that the evolutionary loss of a key insect organ, the Malpighian tubules, has not been associated with the coupled loss of molecular functions.

scholarly journals Anti-ferroptotic mechanism of IL4i1-mediated amino acid metabolism

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Leonie Zeitler ◽  
Alessandra Fiore ◽  
Claudia Meyer ◽  
Marion Russier ◽  
Gaia Zanella ◽  
...  
Keyword(s):  
Gene Expression ◽  
Amino Acid ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
Radical Scavenging ◽  
Gene Expression Program ◽  
Acid Oxidase ◽  
Tumor Cell Death ◽  
Amino Acid Oxidase ◽  
Expression Program

Interleukin-4-induced-1 (IL4i1) is an amino acid oxidase secreted from immune cells. Recent observations have suggested that IL4i1 is pro-tumorigenic via unknown mechanisms. As IL4i1 has homologues in snake venoms (LAAO, L-amino acid oxidases), we used comparative approaches to gain insight into the mechanistic basis of how conserved amino acid oxidases regulate cell fate and function. Using mammalian expressed recombinant proteins, we found venom LAAO kills cells via hydrogen peroxide generation. By contrast, mammalian IL4i1 is non-cytotoxic and instead elicits a cell productive gene expression program inhibiting ferroptotic redox death by generating indole-3-pyruvate (I3P) from tryptophan. I3P suppresses ferroptosis by direct free radical scavenging and through the activation of an anti-oxidative gene expression program. Thus, the pro-tumor effects of IL4i1 are likely mediated by local anti-ferroptotic pathways via aromatic amino acid metabolism, arguing that an IL4i1 inhibitor may modulate tumor cell death pathways.

Amino Acid Metabolism

1979 ◽  
Vol 7 (1) ◽  
pp. 261-262
Author(s):  
E. V. ROWSELL
Keyword(s):  
Amino Acid ◽  
Amino Acid Metabolism ◽  
Acid Metabolism

Effect of intravenous bicarbonate administration on postoperative amino acid metabolism

1985 ◽  
Vol 4 ◽  
pp. 141-146 ◽  
Author(s):  
K VESTERBERG ◽  
J BERGSTROM ◽  
P FURST ◽  
U LEANDER ◽  
E VINNARS
Keyword(s):  
Amino Acid ◽  
Amino Acid Metabolism ◽  
Acid Metabolism

Purification and Characterization of Lupus Anticoagulant Like Protein from Agkistrodon Halys Brevicaudus Venom

1996 ◽  
Vol 76 (06) ◽  
pp. 0993-0997
Author(s):  
Zhao-Yan Li ◽  
Xiao-Wei Wu ◽  
Tie-Fu Yu ◽  
Eric C-Y Lian
Keyword(s):  
Amino Acid ◽  
Lupus Anticoagulant ◽  
Inhibitory Effect ◽  
Clotting Factor ◽  
Acid Oxidase ◽  
Crude Venom ◽  
Amino Acid Oxidase ◽  
Sds Page ◽  
The Individual ◽  
Reducing Condition

SummaryBy means of CM-Sephadex C-25, DEAE-Sephadex A-50, Sephadex G-200, and Sephadex G-75 chromatographies, a lupus anticoagulant like protein (LALP) from Agkistrodon halys brevicaudus was purified. On SDS-PAGE, the purified LALP had a molecular weight of 25,500 daltons under non-reducing condition and 15,000 daltons under reducing condition. The isoelectric point was pH 5.6. Its N terminal amino acid sequencing revealed a mixture of 2 sequences: DCP(P/S)(D/G)WSSYEGH(C/R)Q(Q/K). It was devoid of phospho-lipaseA, fibrino(geno)lytic, 5′-nucleotidase, L-amino acid oxidase, phosphomonoesterase, phosphodiesterase and thrombin-like activities, which were found in crude venom. In the presence of LALP, PT, aPTT, and dRVVT of human plasma were markedly prolonged and its effects were concentration-dependent but time-independent. The inhibitory effect of LALP on the plasma clotting time was enhanced by decreasing phospholipid concentration in TTI test. The individual clotting factor activity was not affected by LALP when higher dilutions of LALP-plasma mixture were used for assay. Russell’s viper venom time was shortened when high phospholipid confirmatory reagent was used. Therefore, the protein has lupus anticoagulant property.

Impairment of Platelet Aggregation by Echis colorata Venom Mediated by L-Amino Acid Oxidase or H2O2

1982 ◽  
Vol 48 (03) ◽  
pp. 277-282 ◽  
Author(s):  
I Nathan ◽  
A Dvilansky ◽  
T Yirmiyahu ◽  
M Aharon ◽  
A Livne
Keyword(s):  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Platelet Aggregation ◽  
Snake Venom ◽  
Oxidase Activity ◽  
Enzyme Preparation ◽  
Acid Oxidase ◽  
Crude Venom ◽  
Amino Acid Oxidase ◽  
Hemostatic Disorders

SummaryEchis colorata bites cause impairment of platelet aggregation and hemostatic disorders. The mechanism by which the snake venom inhibits platelet aggregation was studied. Upon fractionation, aggregation impairment activity and L-amino acid oxidase activity were similarly separated from the crude venom, unlike other venom enzymes. Preparations of L-amino acid oxidase from E.colorata and from Crotalus adamanteus replaced effectively the crude E.colorata venom in impairment of platelet aggregation. Furthermore, different treatments known to inhibit L-amino acid oxidase reduced in parallel the oxidase activity and the impairment potency of both the venom and the enzyme preparation. H2O2 mimicked characteristically the impairment effects of L-amino acid oxidase and the venom. Catalase completely abolished the impairment effects of the enzyme and the venom. It is concluded that hydrogen peroxide formed by the venom L-amino acid oxidase plays a role in affecting platelet aggregation and thus could contribute to the extended bleeding typical to persons bitten by E.colorata.

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