scholarly journals Integrated Metabolome and Transcriptome Analyses Reveal Etiolation-Induced Metabolic Changes Leading to High Amino Acid Contents in a Light-Sensitive Japanese Albino Tea Cultivar

2021 ◽  
Vol 11 ◽  
Author(s):  
Hiroto Yamashita ◽  
Yuka Kambe ◽  
Megumi Ohshio ◽  
Aya Kunihiro ◽  
Yasuno Tanaka ◽  
...  
Keyword(s):  
Amino Acid ◽  
Protein Degradation ◽  
Urea Cycle ◽  
Metabolic Changes ◽  
Nitrogen Excretion ◽  
Tea Leaves ◽  
Arginase 1 ◽  
High Amino Acid ◽  
Transcriptome Analyses ◽  
Tea Cultivar

Plant albinism causes the etiolation of leaves because of factors such as deficiency of chloroplasts or chlorophylls. In general, albino tea leaves accumulate higher free amino acid (FAA) contents than do conventional green tea leaves. To explore the metabolic changes of etiolated leaves (EL) in the light-sensitive Japanese albino tea cultivar “Koganemidori,” we performed integrated metabolome and transcriptome analyses by comparing EL with green leaves induced by bud-sport mutation (BM) or shading treatments (S-EL). Comparative omics analyses indicated that etiolation-induced molecular responses were independent of the light environment and were largely influenced by the etiolation itself. Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment and pathway analyses revealed the downregulation of genes involved in chloroplast development and chlorophyll biosynthesis and upregulation of protein degradation-related pathways, such as the ubiquitin-proteasome system and autophagy in EL. Metabolome analysis showed that most quantified FAAs in EL were highly accumulated compared with those in BM and S-EL. Genes involved in the tricarboxylic acid (TCA) cycle, nitrogen assimilation, and the urea cycle, including the drastically downregulated Arginase-1 homolog, which functions in nitrogen excretion for recycling, showed lower expression levels in EL. The high FAA contents in EL might result from the increased FAA pool and nitrogen source contributed by protein degradation, low N consumption, and stagnation of the urea cycle rather than through enhanced amino acid biosynthesis.

scholarly journals Liver intracellular L-cysteine concentration is maintained after inhibition of the trans-sulfuration pathway by propargylglycine in rats

1997 ◽  
Vol 78 (5) ◽  
pp. 823-831 ◽  
Author(s):  
Ana Triguero ◽  
Teresa Barber ◽  
Concha GarcÍa ◽  
Inmaculada R. Puertes ◽  
Juan Sastre ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Degradation ◽  
Histological Examination ◽  
Blood Concentration ◽  
Urea Cycle ◽  
Blood Levels ◽  
Liver And Kidney ◽  
Amino Acid Homeostasis ◽  
Stimulation Of

To study the fate of l-cysteine and amino acid homeostasis in liver after the inhibition of the trans-sulfuration pathway, rats were treated with propargylglycine (PPG). At 4 h after the administration of PPG, liver cystathionase (EC 4.4.1.1) activity was undetectable, l-cystathionine levels were significantly higher, l-cysteine was unchanged and GSH concentration was significantly lower than values found in livers from control rats injected intraperitoneally with 0.15 M-NaCl. The hepatic levels of amino acids that are intermediates of the urea cycle, l-ornithine, l-citrulline and l-arginine and blood urea were significantly greater. Urea excretion was also higher in PPG-treated rats when compared with control rats. These data suggest a stimulation of ureagenesis in PPG-treated rats. The inhibition of γ-cystathionase was reflected in the blood levels of amino acids, because the L-methionine: l-cyst(e)ine ratio was significantly higher in PPG-treated rats than in control rats; blood concentration of cystathionine was also greater. Histological examination of liver and kidney showed no changes in PPG-treated rats when compared with controls. The administration of N-acetylcysteine (NAC) to PPG-treated rats reversed the changes in blood urea and in liver GSH. These data suggest that when liver l-cysteine production was impaired by the blockage of the trans-sulfuration pathway, the concentration of this amino acid was maintained mainly by an increase in protein degradation and by a depletion in GSH concentration that may spare l-cysteine.

scholarly journals Altered Nitrogen Balance and Decreased Urea Excretion in Male Rats Fed Cafeteria Diet Are Related to Arginine Availability

2014 ◽  
Vol 2014 ◽  
pp. 1-9 ◽  
Author(s):  
David Sabater ◽  
Silvia Agnelli ◽  
Sofía Arriarán ◽  
José-Antonio Fernández-López ◽  
María del Mar Romero ◽  
...  
Keyword(s):  
Amino Acid ◽  
Urea Cycle ◽  
Cafeteria Diet ◽  
Nitrogen Excretion ◽  
Male Rats ◽  
Synthetase Activity ◽  
Carbamoyl Phosphate Synthetase ◽  
Carbamoyl Phosphate ◽  
Urea Excretion ◽  
Dietary Nitrogen

Hyperlipidic diets limit glucose oxidation and favor amino acid preservation, hampering the elimination of excess dietary nitrogen and the catabolic utilization of amino acids. We analyzed whether reduced urea excretion was a consequence of higherNOx; (nitrite, nitrate, and other derivatives) availability caused by increased nitric oxide production in metabolic syndrome. Rats fed a cafeteria diet for 30 days had a higher intake and accumulation of amino acid nitrogen and lower urea excretion. There were no differences in plasma nitrate or nitrite.NOxand creatinine excretion accounted for only a small part of total nitrogen excretion. Rats fed a cafeteria diet had higher plasma levels of glutamine, serine, threonine, glycine, and ornithine when compared with controls, whereas arginine was lower. Liver carbamoyl-phosphate synthetase I activity was higher in cafeteria diet-fed rats, but arginase I was lower. The high carbamoyl-phosphate synthetase activity and ornithine levels suggest activation of the urea cycle in cafeteria diet-fed rats, but low arginine levels point to a block in the urea cycle between ornithine and arginine, thereby preventing the elimination of excess nitrogen as urea. The ultimate consequence of this paradoxical block in the urea cycle seems to be the limitation of arginine production and/or availability.

scholarly journals Theanine, Antistress Amino Acid in Tea Leaves, Causes Hippocampal Metabolic Changes and Antidepressant Effects in Stress-Loaded Mice

2020 ◽  
Vol 22 (1) ◽  
pp. 193
Author(s):  
Keiko Unno ◽  
Yoshio Muguruma ◽  
Koichi Inoue ◽  
Tomokazu Konishi ◽  
Kyoko Taguchi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Stress Condition ◽  
Stress Sensitivity ◽  
Metabolic Changes ◽  
Group Housing ◽  
Tea Leaves ◽  
Stress Vulnerability ◽  
Antidepressant Effects ◽  
Senescence Accelerated Mouse ◽  
Abundant Amino Acid

By comprehensively measuring changes in metabolites in the hippocampus of stress-loaded mice, we investigated the reasons for stress vulnerability and the effect of theanine, i.e., an abundant amino acid in tea leaves, on the metabolism. Stress sensitivity was higher in senescence-accelerated mouse prone 10 (SAMP10) mice than in normal ddY mice when these mice were loaded with stress on the basis of territorial consciousness in males. Group housing was used as the low-stress condition reference. Among the statistically altered metabolites, depression-related kynurenine and excitability-related histamine were significantly higher in SAMP10 mice than in ddY mice. In contrast, carnosine, which has antidepressant-like activity, and ornithine, which has antistress effects, were significantly lower in SAMP10 mice than in ddY mice. The ingestion of theanine, an excellent antistress amino acid, modulated the levels of kynurenine, histamine, and carnosine only in the stress-loaded SAMP10 mice and not in the group-housing mice. Depression-like behavior was suppressed in mice that had ingested theanine only under stress loading. Taken together, changes in these metabolites, such as kynurenine, histamine, carnosine, and ornithine, were suggested to be associated with the stress vulnerability and depression-like behavior of stressed SAMP10 mice. It was also shown that theanine action appears in the metabolism of mice only under stress loading.

scholarly journals Effects of insulin and anchorage on hepatocytic protein metabolism and amino acid transport

1981 ◽  
Vol 48 (1) ◽  
pp. 1-18
Author(s):  
A. Poli ◽  
P.B. Gordon ◽  
P.E. Schwarze ◽  
B. Grinde ◽  
P.O. Seglen
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Protein Degradation ◽  
Amino Acid Transport ◽  
Protein Synthesis Inhibitor ◽  
Acid Transport ◽  
Synthesis Inhibitor ◽  
Insulin Effect ◽  
High Amino Acid ◽  
Amino Acid Concentrations

Insulin partially inhibits endogenous protein degradation in isolated hepatocytes. The inhibition seems to specifically affect the lysosomal pathway of degradation, since it is not additive to the effects of lysosome inhibitors such as propylamine and leupeptin. The insulin effect is potentiated by intermediate concentrations of amino acids, but is largely abolished at high amino acid concentrations which suppress degradation maximally, suggesting that the hormone may exert its effect indirectly by acting upon the more basal amino acid control mechanism. Glucagon, which stimulates protein degradation, similarly displays its effect only in the presence of intermediate amino acid concentrations. The insulin inhibition is not affected by the aminotransferase inhibitor, aminooxyacetate, indicating that it is not due to interference with amino acid metabolism. Protein synthesis furthermore does not seem to be required, since a significant insulin effect can be seen in the presence of the protein synthesis inhibitor, cycloheximide. The issue is, however, complicated by the fact that cycloheximide itself inhibits protein degradation to approximately the same extent as does insulin. Insulin stimulates uptake of the amino acid alpha-aminoisobutyrate (AIB), but not the uptake of valine, indicating a specific stimulation of ‘A’-type transport. Cycloheximide similarly stimulates AIB uptake, without completely obfuscating the transport effect of insulin. Neither protein synthesis, protein degradation, amino acid transport, nor the effects of insulin were affected by cell-to-substratum anchorage (attachment and spreading) in any detectable way.

scholarly journals RAPID COMMUNICATION: Residual feed intake in beef cattle is associated with differences in protein turnover and nutrient transporters in ruminal epithelium

2019 ◽  
Vol 97 (5) ◽  
pp. 2181-2187
Author(s):  
Ahmed A Elolimy ◽  
Emad Abdel-Hamied ◽  
Liangyu Hu ◽  
Joshua C McCann ◽  
Daniel W Shike ◽  
...  
Keyword(s):  
Amino Acid ◽  
Beef Cattle ◽  
Protein Degradation ◽  
Insulin Signaling ◽  
Feed Intake ◽  
Feed Efficiency ◽  
Protein Turnover ◽  
Residual Feed Intake ◽  
Ubiquitin Proteasome ◽  
Ruminal Epithelium

Abstract Residual feed intake (RFI) is a widely used measure of feed efficiency in cattle. Although the precise biologic mechanisms associated with improved feed efficiency are not well-known, most-efficient steers (i.e., with low RFI coefficient) downregulate abundance of proteins controlling protein degradation in skeletal muscle. Whether cellular mechanisms controlling protein turnover in ruminal tissue differ by RFI classification is unknown. The aim was to investigate associations between RFI and signaling through the mechanistic target of rapamycin (MTOR) and ubiquitin-proteasome pathways in ruminal epithelium. One hundred and forty-nine Red Angus cattle were allocated to 3 contemporary groups according to sex and herd origin. Animals were offered a finishing diet for 70 d to calculate the RFI coefficient for each. Within each group, the 2 most-efficient (n = 6) and least-efficient animals (n = 6) were selected. Compared with least-efficient animals, the most-efficient animals consumed less feed (P < 0.05; 18.36 vs. 23.39 kg/d DMI). At day 70, plasma samples were collected for insulin concentration analysis. Ruminal epithelium was collected immediately after slaughter to determine abundance and phosphorylation status of 29 proteins associated with MTOR, ubiquitin-proteasome, insulin signaling, and glucose and amino acid transport. Among the proteins involved in cellular protein synthesis, most-efficient animals had lower (P ≤ 0.05) abundance of MTOR, p-MTOR, RPS6KB1, EIF2A, EEF2K, AKT1, and RPS6KB1, whereas MAPK3 tended (P = 0.07) to be lower. In contrast, abundance of p-EEF2K, p-EEF2K:EEF2K, and p-EIF2A:EIF2A in most-efficient animals was greater (P ≤ 0.05). Among proteins catalyzing steps required for protein degradation, the abundance of UBA1, NEDD4, and STUB1 was lower (P ≤ 0.05) and MDM2 tended (P = 0.06) to be lower in most-efficient cattle. Plasma insulin and ruminal epithelium insulin signaling proteins did not differ (P > 0.05) between RFI groups. However, abundance of the insulin-responsive glucose transporter SLC2A4 and the amino acid transporters SLC1A3 and SLC1A5 also was lower (P ≤ 0.05) in most-efficient cattle. Overall, the data indicate that differences in signaling mechanisms controlling protein turnover and nutrient transport in ruminal epithelium are components of feed efficiency in beef cattle.

Biochemical characterization of a glucoamylase from Saccharomycopsis fibuligera R64

Biologia ◽  
2011 ◽  
Vol 66 (1) ◽  
Author(s):  
Dessy Natalia ◽  
Keni Vidilaseris ◽  
Pasjan Satrimafitrah ◽  
Wangsa Ismaya ◽  
Purkan ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Amino Acid Sequence Identity ◽  
Biochemical Characterization ◽  
Saccharomycopsis Fibuligera ◽  
Sequence Identity ◽  
Ic50 Value ◽  
High Amino Acid ◽  
Ph Range

AbstractGlucoamylase from the yeast Saccharomycopsis fibuligera R64 (GLL1) has successfully been purified and characterized. The molecular mass of the enzyme was 56,583 Da as determined by mass spectrometry. The purified enzyme demonstrated optimum activity in the pH range of 5.6–6.4 and at 50°C. The activity of the enzyme was inhibited by acarbose with the IC50 value of 5 μM. GLL1 shares high amino acid sequence identity with GLU1 and GLA1, which are Saccharomycopsis fibuligera glucoamylases from the strains HUT7212 and KZ, respectively. The properties of GLL1, however, resemble that of GLU1. The elucidation of the primary structure of GLL1 contributes to the explanation of this finding.

The Drosophila homeobox gene optix is capable of inducing ectopic eyes by an eyeless-independent mechanism

Development ◽  
2000 ◽  
Vol 127 (9) ◽  
pp. 1879-1886 ◽  
Author(s):  
M. Seimiya ◽  
W.J. Gehring
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Gene Family ◽  
Eye Development ◽  
Ectopic Expression ◽  
Amino Acid Sequence Similarity ◽  
Sine Oculis ◽  
High Amino Acid ◽  
Independent Mechanism ◽  
Ectopic Eyes

optix is a new member of the Six/so gene family from Drosophila that contains both a six domain and a homeodomain. Because of its high amino acid sequence similarity with the mouse Six3 gene, optix is considered to be the orthologous gene from Drosophila rather than sine oculis, as previously believed. optix expression was detected in the eye, wing and haltere imaginal discs. Ectopic expression of optix leads to the formation of ectopic eyes suggesting that optix has important functions in eye development. Although optix and sine oculis belong to the same gene family (Six/so) and share a high degree of amino acid sequence identity, there are a number of factors which suggest that their developmental roles are different: (1) the expression patterns of optix and sine oculis are clearly distinct; (2) sine oculis acts downstream of eyeless, whereas optix is expressed independently of eyeless; (3) sine oculis functions synergistically with eyes absent in eye development whereas optix does not; (4) ectopic expression of optix alone, but not of sine oculis can induce ectopic eyes in the antennal disc. These results suggest that optix is involved in eye morphogenesis by an eyeless-independent mechanism.

Reimbursement for Medical Foods for Inborn Errors of Metabolism

PEDIATRICS ◽  
1994 ◽  
Vol 93 (5) ◽  
pp. 860-860
Author(s):  
Keyword(s):  
Amino Acid ◽  
Metabolic Diseases ◽  
Urea Cycle ◽  
Private Insurance ◽  
Type I ◽  
Urea Cycle Disorders ◽  
Healthy Children ◽  
Inborn Errors ◽  
Medical Foods ◽  
Cycle Disorders

Inborn errors of amino acid metabolism such as phenylketonuria, maternal phenylketonuria, maple syrup urine disease, homocystinuria, methylmalonic acidemia, propionic acidemia, isovaleric acidemia and other disorders of leucine metabolism, glutaric acidemia type I and tyrosinemia types I and II, and urea cycle disorders are rare diseases that are treatable by diet. Treatment might include the restriction of one or more amino acids, the restriction of total nitrogen, or the supplementation of specific substances. Untreated, these diseases culminate in severe mental retardation or death. Once diagnosis is confirmed, treatment of amino acid and urea cycle disorders must be carefully monitored by a physician with expertise in metabolic diseases. Special medical foods, commercially available, are indispensable for the active, ongoing treatment of diagnosed amino acid and urea cycle disorders. Special medical foods would, if used as the sole dietary source, represent a hazard to affected and healthy children. US Public Law (Publ L) 100-290 defines the term medical food as ". . . a food which is formulated to be consumed or administered enterally under the supervision of a physician and which is intended for the specific dietary management of a disease or condition for which distinctive nutritional requirements, based on recognized scientific principles, are established by medical evaluation."1 After passage of Publ L 100-290, many states provided funding for these products through Medicaid, and most states offered assistance through Crippled Children's and Women, Infant, and Children's programs. Some states now have laws mandating private insurance coverage for special medical foods. It is the position of the American Academy of Pediatrics that special medical foods that are used in the treatment of amino acid and urea cycle disorders are medical expenses that should be reimbursed.

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