Growth performance, amino acid retention and mRNA levels of mTORC1 signaling pathway genes in Nile tilapia fingerlings fed protein-bound and crystalline amino acids

Aquaculture ◽  
2021 ◽  
pp. 736953
Author(s):  
Thaís Pereira da Cruz ◽  
Mariana Michelato ◽  
Maeli Dal-Pai-Silva ◽  
Tassiana Gutierrez de Paula ◽  
Edson Assunção Macedo ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Growth Performance ◽  
Signaling Pathway ◽  
Nile Tilapia ◽  
Mrna Levels ◽  
Mtorc1 Signaling ◽  
Crystalline Amino Acids

scholarly journals Suppression of the mTORC1/STAT3/Notch1 pathway by activated AMPK prevents hepatic insulin resistance induced by excess amino acids

2014 ◽  
Vol 306 (2) ◽  
pp. E197-E209 ◽  
Author(s):  
Hongliang Li ◽  
Jiyeon Lee ◽  
Chaoyong He ◽  
Ming-Hui Zou ◽  
Zhonglin Xie
Keyword(s):  
Insulin Resistance ◽  
Amino Acids ◽  
Amino Acid ◽  
Signaling Pathway ◽  
High Protein Diet ◽  
Chronic Administration ◽  
Hepatic Insulin Resistance ◽  
Notch1 Signaling ◽  
Mtorc1 Signaling ◽  
Notch1 Signaling Pathway

Nutrient overload is associated with the development of obesity, insulin resistance, and type 2 diabetes. However, the underlying mechanisms for developing insulin resistance in the presence of excess nutrients are incompletely understood. We investigated whether activation of AMP-activated protein kinase (AMPK) prevents the hepatic insulin resistance that is induced by the consumption of a high-protein diet (HPD) and the presence of excess amino acids. Exposure of HepG2 cells to excess amino acids reduced AMPK phosphorylation, upregulated Notch1 expression, and impaired the insulin-stimulated phosphorylation of Akt Ser473 and insulin receptor substrate-1 (IRS-1) Tyr612. Inhibition of Notch1 prevented amino acid-induced insulin resistance, which was accompanied by reduced expression of Rbp-Jk, hairy and enhancer of split-1, and forkhead box O1. Mechanistically, mTORC1 signaling was activated by excess amino acids, which then positively regulated Notch1 expression through the activation of the signal transducer and activator of transcription 3 (STAT3). Activation of AMPK by metformin inhibited mTORC1-STAT3 signaling, thereby preventing excess amino acid-impaired insulin signaling. Finally, HPD feeding suppressed AMPK activity, activated mTORC1/STAT3/Notch1 signaling, and induced insulin resistance. Chronic administration of either metformin or rapamycin inhibited the HPD-activated mTORC1/STAT3/Notch1 signaling pathway and prevented hepatic insulin resistance. We conclude that the upregulation of Notch1 expression by hyperactive mTORC1 signaling is an essential event in the development of hepatic insulin resistance in the presence of excess amino acids. Activation of AMPK prevents amino acid-induced insulin resistance through the suppression of the mTORC1/STAT3/Notch1 signaling pathway.

scholarly journals Glutamine and cystine-enriched diets modulate aquaporins gene expression in the small intestine of piglets

PLoS ONE ◽  
2021 ◽  
Vol 16 (1) ◽  
pp. e0245739
Author(s):  
Inês Vieira da Silva ◽  
Bárbara P. Soares ◽  
Catarina Pimpão ◽  
Rui M. A. Pinto ◽  
Teresa Costa ◽  
...  
Keyword(s):  
Amino Acids ◽  
Small Intestine ◽  
Amino Acid ◽  
Biochemical Parameters ◽  
Dietary Supplementation ◽  
Basal Diet ◽  
Mrna Levels ◽  
Promising Target ◽  
Dietary Treatments ◽  
Glycerol Permeability

The regulation of glycerol permeability in the gastrointestinal tract is crucial to control fat deposition, lipolysis and gluconeogenesis. Knowing that the amino acid glutamine is a physiological regulator of gluconeogenesis, whereas cystine promotes adiposity, herein we investigated the effects of dietary supplementation with glutamine and cystine on the serum biochemical parameters of piglets fed on amino acid-enriched diets, as well as on the transcriptional profile of membrane water and glycerol channels aquaporins (AQPs) in the ileum portion of the small intestine and its impact on intestinal permeability. Twenty male piglets with an initial body weight of 8.8 ± 0.89 kg were allocated to four dietary treatments (n = 5) and received, during a four week-period, a basal diet without supplementation (control) or supplemented with 8 kg/ton of glutamine (Gln), cystine (Cys) or the combination of the two amino acids in equal proportions (Gln + Cys). Most biochemical parameters were found improved in piglets fed Gln and Cys diet. mRNA levels of AQP3 were found predominant over the others. Both amino acids, individually or combined, were responsible for a consistent downregulation of AQP1, AQP7 and AQP10, without impacting on water permeability. Conversely, Cys enriched diet upregulated AQP3 enhancing basolateral membranes glycerol permeability and downregulating glycerol kinase (GK) of intestinal cells. Altogether, our data reveal that amino acids dietary supplementation can modulate intestinal AQPs expression and unveil AQP3 as a promising target for adipogenesis regulation.

Paralogs of Atlantic salmon myoblast determination factor genes are distinctly regulated in proliferating and differentiating myogenic cells

2010 ◽  
Vol 298 (6) ◽  
pp. R1615-R1626 ◽  
Author(s):  
Neil I. Bower ◽  
Ian A. Johnston
Keyword(s):  
Cell Cycle ◽  
Amino Acids ◽  
Amino Acid ◽  
Atlantic Salmon ◽  
Antigen Expression ◽  
Nuclear Antigen ◽  
Quiescent State ◽  
Mrna Levels ◽  
Proliferating Cells

The mRNA expression of myogenic regulatory factors, including myoD1 (myoblast determination factor) gene paralogs, and their regulation by amino acids and insulin-like growth factors were investigated in primary cell cultures isolated from fast myotomal muscle of Atlantic salmon ( Salmo salar). The cell cycle and S phase were determined as 28.1 and 13.3 h, respectively, at 18°C. Expression of myoD1b and myoD1c peaked at 8 days of culture in the initial proliferation phase and then declined more than sixfold as cells differentiated and was correlated with PCNA (proliferating cell nuclear antigen) expression ( R = 0.88, P < 0.0001; R = 0.70, P < 0.0001). In contrast, myoD1a transcripts increased from 2 to 8 days and remained at elevated levels as myotubes were formed. mRNA levels of myoD1c were, on average, 3.1- and 5.7-fold higher than myoD1a and myoD1b, respectively. Depriving cells of amino acids and serum led to a rapid increase in pax7 and a decrease in myoD1c and PCNA expression, indicating a transition to a quiescent state. In contrast, amino acid replacement in starved cells produced significant increases in myoD1c (at 6 h), PCNA (at 12 h), and myoD1b (at 24 h) and decreases in pax7 expression as cells entered the cell cycle. Our results are consistent with temporally distinct patterns of myoD1c and myoD1b expression at the G1 and S/G2 phases of the cell cycle. Treatment of starved cells with insulin-like growth factor I or II did not alter expression of the myoD paralogs. It was concluded that, in vitro, amino acids alone are sufficient to stimulate expression of genes regulating myogenesis in myoblasts involving autocrine/paracrine pathways. The differential responses of myoD paralogs during myotube maturation and amino acid treatments suggest that myoD1b and myoD1c are primarily expressed in proliferating cells and myoD1a in differentiating cells, providing evidence for their subfunctionalization following whole genome and local duplications in the Atlantic salmon lineage.

scholarly journals Effects of amino acid biomass or feed-grade amino acids on growth performance of growing swine and poultry12

2019 ◽  
Vol 4 (1) ◽  
pp. 49-58
Author(s):  
Madie R Wensley ◽  
Jason C Woodworth ◽  
Joel M Derouchey ◽  
Steve S Dritz ◽  
Mike D Tokach ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Growth Performance ◽  
Control Diet ◽  
Positive Control ◽  
Negative Control ◽  
Suitable Alternative ◽  
Poultry Diets ◽  
Dietary Treatments

Abstract Three experiments were conducted to determine the effect of three fermented amino acids (AA) with their respective biomass compared to crystalline AA on the growth performance of swine and poultry. In experiment 1, 315 barrows (DNA 200 × 400, initially 11.3 ± 0.69 kg) were allotted to 1 of 4 dietary treatments with 5 pigs per pen and 15 or 16 pens per treatment. Dietary treatments included a negative control (16% standardized ileal digestible [SID] Tryptophan:lysine [Trp:Lys] ratio), positive control (21% SID Trp:Lys ratio from crystalline Trp), or diets containing Trp with biomass to provide 21 or 23.5% SID Trp:Lys ratios, respectively. Pigs fed the positive control or low Trp with biomass diet had increased (P &lt; 0.05) ADG compared to pigs fed the negative control diet, with pigs fed the high Trp with biomass diet intermediate. Pigs fed the low Trp with biomass diet had increased (P &lt; 0.05) G:F compared to the negative control diet, with others intermediate. In experiment 2, 1,320 1-d-old male broilers (Cobb 500, initially 45.2 g) were allotted to one of four dietary treatments with 33 birds per pen and 10 pens per treatment. Dietary treatments included a negative control (58/58% Threonine:lysine [Thr:Lys] ratio), positive control (65/66% Thr:Lys ratio from crystalline Thr), or diets containing Thr with biomass to provide 65/66 or 69/70% Thr:Lys ratios in starter and grower diets, respectively. Broilers fed the positive control or Thr with biomass diets had increased (P &lt; 0.05) ADG compared to broilers fed the negative control diet. Broilers fed the positive control or the low Thr with biomass diet had increased (P &lt; 0.05) G:F compared to the negative control and high Thr with biomass treatments. In experiment 3, 2,100 one-day-old male broilers (Cobb 500, initially 39.4 g) were allotted to one of four dietary treatments with 35 birds per pen and 15 pens per treatment. Dietary treatments included a negative control (59/63% Valine:lysine [Val:Lys] ratio), positive control (75/76% Val:Lys ratio from crystalline Val), or diets containing Val with biomass to provide 75/76 or 84/83% Val:Lys ratios in starter and grower diets, respectively. Broilers fed the positive control or Val with biomass diets had increased (P &lt; 0.05) ADG, ADFI, and G:F compared to those fed the negative control diet. In conclusion, Trp, Thr, or Val with their respective biomass appear to be equally bioavailable and a suitable alternative to crystalline AA in swine and poultry diets.

scholarly journals Regulation of type I collagen mRNA in lung fibroblasts by cystine availability

1998 ◽  
Vol 331 (2) ◽  
pp. 417-422 ◽  
Author(s):  
David C. RISHIKOF ◽  
Ping-Ping KUANG ◽  
Christine POLIKS ◽  
Ronald H. GOLDSTEIN
Keyword(s):  
Amino Acids ◽  
Steady State ◽  
Amino Acid ◽  
Type I Collagen ◽  
State Level ◽  
Lung Fibroblasts ◽  
Type I ◽  
Mrna Levels ◽  
Collagen Mrna ◽  
Amino Acid Availability

The steady-state level of α1(I) collagen mRNA is regulated by amino acid availability in human lung fibroblasts. Depletion of amino acids decreases α1(I) collagen mRNA levels and repletion of amino acids induces rapid re-expression of α1(I) mRNA. In these studies, we examined the requirements for individual amino acids on the regulation of α1(I) collagen mRNA. We found that re-expression of α1(I) collagen mRNA was critically dependent on cystine but not on other amino acids. However, the addition of cystine alone did not result in re-expression of α1(I) collagen mRNA. Following amino acid depletion, the addition of cystine with selective amino acids increased α1(I) collagen mRNA levels. The combination of glutamine and cystine increased α1(I) collagen mRNA levels 6.3-fold. Methionine or a branch-chain amino acid (leucine, isoleucine or valine) also acted in combination with cystine to increase α1(I) collagen mRNA expression, whereas other amino acids were not effective. The prolonged absence of cystine lowered steady-state levels of α1(I) collagen mRNA through a mechanism involving decreases in both the rate of gene transcription as assessed by nuclear run-on experiments and mRNA stability as assessed by half-life determination in the presence of actinomycin D. The effect of cystine was not mediated via alterations in the level of glutathione, the major redox buffer in cells, as determined by the addition of buthionine sulphoximine, an inhibitor of γ-glutamylcysteine synthetase. These data suggest that cystine directly affects the regulation of α1(I) collagen mRNA.

scholarly journals The Prodomain of Ssy5 Protease Controls Receptor-Activated Proteolysis of Transcription Factor Stp1

2010 ◽  
Vol 30 (13) ◽  
pp. 3299-3309 ◽  
Author(s):  
Thorsten Pfirrmann ◽  
Stijn Heessen ◽  
Deike J. Omnus ◽  
Claes Andréasson ◽  
Per O. Ljungdahl
Keyword(s):  
Amino Acids ◽  
Transcription Factor ◽  
Transcription Factors ◽  
Amino Acid ◽  
Signaling Pathway ◽  
Temperature Control ◽  
Regulatory Mechanism ◽  
Potent Inhibitor ◽  
Large N

ABSTRACT Extracellular amino acids induce the yeast SPS sensor to endoproteolytically cleave transcription factors Stp1 and Stp2 in a process termed receptor-activated proteolysis (RAP). Ssy5, the activating endoprotease, is synthesized with a large N-terminal prodomain and a C-terminal chymotrypsin-like catalytic (Cat) domain. During biogenesis, Ssy5 cleaves itself and the prodomain and Cat domain remain associated, forming an inactive primed protease. Here we show that the prodomain is a potent inhibitor of Cat domain activity and that its inactivation is a requisite for RAP. Accordingly, amino acid-induced signals trigger proteasome-dependent degradation of the prodomain. A mutation that stabilizes the prodomain prevents Stp1 processing, whereas destabilizing mutations lead to constitutive RAP-independent Stp1 processing. We fused a conditional degron to the prodomain to synthetically reprogram the amino acid-responsive SPS signaling pathway, placing it under temperature control. Our results define a regulatory mechanism that is novel for eukaryotic proteases functioning within cells.

Sign in / Sign up

Export Citation Format

Share Document