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1.
FEBS Open Bio ; 12(3): 627-637, 2022 03.
Article in English | MEDLINE | ID: mdl-35038382

ABSTRACT

ß2 -Adrenoceptor (ß2 -AR) signaling decreases the transcriptional activity of forkhead box O (FoxO), but the underlying mechanisms remain incompletely understood. Here, we investigated how ß2 -AR signaling regulates the protein abundance of FoxO and its transcriptional activity in skeletal muscle. We observed that stimulation of ß2 -AR with its selective agonist, clenbuterol, rapidly decreased FoxO1 mRNA expression, and this was accompanied by a decrease in either FoxO1 protein level or FoxO transcriptional activity. We subsequently observed that miR-374b-5p and miR-7a-1-3p were rapidly upregulated in response to ß2 -AR stimulation. Transfection with mimics of either miRNA successfully decreased FoxO1 mRNA. Moreover, because ß2 -AR stimulation increased cAMP concentration, pretreatment with an adenylyl cyclase inhibitor canceled out these effects of ß2 -AR stimulation. These results suggest that ß2 -AR stimulation results in rapid upregulation of miR-374b-5p and miR-7a-1-3p in myotubes, which in turn results in a decrease in FoxO1 mRNA expression via the ß2 -AR-cAMP signaling pathway.


Subject(s)
MicroRNAs , Signal Transduction , Animals , Forkhead Box Protein O1/genetics , Forkhead Box Protein O1/metabolism , Mice , MicroRNAs/genetics , MicroRNAs/metabolism , Muscle Fibers, Skeletal/metabolism , RNA, Messenger/genetics , RNA, Messenger/metabolism , Signal Transduction/genetics
2.
Anim Sci J ; 91(1): e13327, 2020.
Article in English | MEDLINE | ID: mdl-32219959

ABSTRACT

Excessive lipid peroxidation negatively affects the physiological response and meat quality of chickens. Delaying post-hatch feeding was previously found to increase lipid peroxidation in the skeletal muscle of finishing broiler chickens. The aims of this study were to investigate the effects of delayed post-hatch feeding on lipid peroxidation and the mRNA expressions of antioxidant enzymes in the pectoralis major muscle of broiler chicks during the post-hatching period. Newly hatched chicks either had immediate free access to feed (freely-fed chicks) or had no access to feed from 0 to 2 days old (delayed-fed chicks), after which both groups were fed ad libitum until 4 or 13 days old. The lipid peroxidation level was higher in the delayed-fed than freely-fed chicks at 2, 4, and 13 days old. At 2 days old, the mRNA expressions of Cu/Zn-SOD, Mn-SOD, and GPX7 were lower in the delayed-fed than freely-fed chicks, while catalase mRNA levels did not differ. Furthermore, at 4 and 13 days old, lower mRNA expressions of Cu/Zn-SOD and Mn-SOD were observed in the delayed-fed than freely-fed chicks. These results suggest that delaying post-hatch feeding reduces the mRNA levels of Cu/Zn-SOD and Mn-SOD, consequently affecting muscle lipid peroxidation in chicks during subsequent growth.


Subject(s)
Animal Feed , Chickens/metabolism , Feeding Methods/veterinary , Lipid Peroxidation/physiology , Muscle, Skeletal/metabolism , Peroxidases/metabolism , RNA, Messenger/metabolism , Superoxide Dismutase-1/metabolism , Superoxide Dismutase/metabolism , Animal Nutritional Physiological Phenomena , Animals , Gene Expression , Glutathione Peroxidase , Peroxidases/genetics , RNA, Messenger/genetics , Superoxide Dismutase/genetics , Superoxide Dismutase-1/genetics , Time Factors
3.
Nutrients ; 12(2)2020 Feb 07.
Article in English | MEDLINE | ID: mdl-32046170

ABSTRACT

Dietary intake of fiber-rich food has been reported to contribute to multiple health benefits. The aim of the current study is to investigate the effects of a diet containing the outer bran fraction of rice (OBFR), which is rich in insoluble fiber, on the intestinal environment and metabolite profiles of rats. Fourteen 8-week-old male Sprague-Dawley rats were divided into a control group and an OBFR group. For a period of 21 days, the control group was fed a control diet, while the OBFR group was fed a diet containing 5% OBFR. Metabolomics analysis revealed drastic changes in the cecal metabolites of the rats fed the OBFR diet. Furthermore, in the plasma and liver tissue, the concentrations of metabolites involved in pyruvate metabolism, the pentose phosphate pathway, gluconeogenesis, or valine, leucine, isoleucine degradation were changed. Concordantly, the OBFR diet increased the expression of genes encoding enzymes involved in these metabolic pathways in the livers of the rats. Collectively, these results suggest that the OBFR diet altered the concentrations of metabolites in the cecal contents, plasma, and liver, and the hepatic gene expressions of rats, and that this may have mainly contributed to carbohydrate metabolism in the liver.


Subject(s)
Carbohydrate Metabolism , Dietary Fiber/administration & dosage , Dietary Supplements , Liver/metabolism , Oryza , Animals , Carbohydrate Metabolism/genetics , Dietary Fiber/pharmacology , Fatty Acids, Volatile/metabolism , Gene Expression , Gluconeogenesis/drug effects , Leucine/metabolism , Male , Pentose Phosphate Pathway/genetics , Pyruvic Acid/metabolism , Rats, Sprague-Dawley , Valine/metabolism
4.
Gen Comp Endocrinol ; 283: 113232, 2019 11 01.
Article in English | MEDLINE | ID: mdl-31356813

ABSTRACT

Avian glucose transporters (GLUT) responsible for insulin-responsive glucose uptake into adipocytes remain poorly characterized. We aimed to identify the insulin-responsive GLUT using primary culture of chicken adipocytes. Acute stimulation with 1 µM insulin for 20 min increased 2-deoxyglucose uptake, AKT protein phosphorylation, and GLUT1 protein levels on the plasma membrane of the chicken adipocytes, whereas pretreatment with 10 µM triciribine, an AKT inhibitor, canceled these effects. Furthermore, the insulin stimulation did not affect GLUT12 protein levels on the plasma membrane of the chicken adipocytes. Our results suggest that GLUT1 is an insulin-responsive GLUT in chicken adipocytes.


Subject(s)
Adipocytes/metabolism , Cell Membrane/metabolism , Chickens/metabolism , Glucose Transporter Type 1/metabolism , Glucose/metabolism , Insulin/pharmacology , Proto-Oncogene Proteins c-akt/metabolism , Adipocytes/drug effects , Animals , Biological Transport/drug effects , Cell Membrane/drug effects , Deoxyglucose/metabolism , Male , Phosphorylation/drug effects
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