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The experiment was conducted to estimate the ideal dietary sodium (Na) and chloride (Cl) level for broilers during day 1 to 21 using a corn-soybean meal diet under a dietary Na:Cl ratio of 1:1. A total of 490 1-d-old Arbor Acres male broilers were randomly allotted by body weight to one of seven treatments in a completely randomized design. Each treatment consisted of seven replicate cages with 10 chicks per cage. Broilers were fed a Na and Cl-unsupplemented corn-soybean meal basal diet (control, containing 0.02% Na and 0.08% Cl) and the Na and Cl-supplemented basal diets containing 0.14%, 0.20%, 0.26%, 0.32%, 0.38%, and 0.44% Na and Cl levels, respectively for 21 d. The results indicated that average daily gain, average daily feed intake, blood partial pressure of CO2 and concentrations of HCO3−, total CO2, Na+, Cl−, base excess and anion gap, tibial ash, and ash Na contents of broilers were affected (P  < 0.001) by dietary Na and Cl level, and increased linearly (P  < 0.001) and quadratically (P  < 0.001) with increasing Na and Cl levels. Feed/gain ratio, mortality, blood K+ concentration, serum osmotic pressure and K+, glucose and uric acid concentrations as well as heart, liver, and kidney indices of broilers were affected (P  < 0.01) by dietary Na and Cl level, and decreased linearly (P  < 0.001) and quadratically (P  < 0.001) with increasing Na and Cl levels. The estimates of dietary optimal Na and Cl levels were 0.07% to 0.16% according to the best-fitted broken-line or asymptotic models (P  < 0.001) of the above sensitive indicators. Therefore, the optimal dietary Na and Cl level was suggested to be 0.16% to support all of the above Na and Cl metabolic requirements of broilers fed the corn-soybean meal diet during day 1 to 21, which is lower than the 0.20% recommendation by the Chinese Feeding Standard of Chicken (2004). [ABSTRACT FROM AUTHOR]

This study aimed to characterize the effects of different dietary forms of supplemental manganese (Mn) on hepatic lipid deposition, gene expression, and enzyme activity in liver fat metabolism in 42-d-old broiler chickens. In total 420 one-day-old Arbor Acres (AA) broilers (rooster:hen = 1:1) were assigned randomly based on body weight and sex to 1 of 6 treatments (10 replicate cages per treatment and 7 broilers per replicate cage) in a completely randomized design using a 2 (sex) × 3 (diet) factorial arrangement. The 3 diets were basal control diets without Mn supplementation and basal diets supplemented with either Mn sulfate or Mn proteinate. No sex × diet interactions were observed in any of the measured indexes; thus, the effect of diet alone was presented in this study. Dietary Mn supplementation increased Mn content in the plasma and liver, adipose triglyceride lipase (ATGL) activity, and ATGL mRNA and its protein expression in the liver by 5.3% to 24.0% (P  < 0.05), but reduced plasma triglyceride (TG), total cholesterol, and low-density lipoprotein (LDL-C) levels, liver TG content, fatty acid synthase (FAS) and malic enzyme (ME) activities, mRNA expression of sterol-regulatory element-binding protein 1 (SREBP1), FAS , stearoyl-coA desaturase (SCD), and ME , as well as the protein expression of SREBP1 and SCD in the liver by 5.5% to 22.8% (P  < 0.05). No differences were observed between the 2 Mn sources in all of the determined parameters. Therefore, it was concluded that dietary Mn supplementation, regardless of Mn source, decreased hepatic lipid accumulation in broilers by inhibiting SREBP1 and SCD expression, FAS and ME activities, and enhancing ATGL expression and activity. [ABSTRACT FROM AUTHOR]

Recent study showed that zinc (Zn) and amino acid transporters may be involved in enhancing Zn absorption from Zn proteinate with moderate chelation strength (Zn-Prot M) in the duodenum of broilers. However, the specific mechanisms by which Zn-Prot M promotes the above Zn absorption are unknown. Therefore, in this study, 3 experiments were conducted to investigate specific and direct effects of Zn-Prot M and Zn sulfate (ZnS) on Zn absorption and expression of related transporters in primary duodenal epithelial cells of broiler embryos so as to preliminarily address possible mechanisms. In experiment 1, cells were treated with 100 μmol Zn/L as ZnS or Zn-Prot M for 20, 40, 60, 80, 100, or 120 min. Experiment 2 consisted of 3 sub-experiments. In experiment 2A, cells were treated with a Zn-unsupplemented basal medium (Control) or the basal medium supplemented with 100 or 200 μmol Zn/L as ZnS or Zn-Prot M for 60 min; in experiment 2B, cells were treated with a Zn-unsupplemented basal medium (Control) or the basal medium supplemented with 200 μmol Zn/L of as the ZnS or Zn-Prot M for 120 min; in experiment 2C, cells were treated with a Zn-unsupplemented basal medium (Control) or the basal medium supplemented with 400 or 800 μmol Zn/L as ZnS or Zn-Prot M for 120 min. In experiment 3, cells were treated with a Zn-unsupplemented basal medium (Control) or the basal medium supplemented with 400 μmol Zn/L as ZnS or Zn-Prot M for 120 min. The results of experiment 1 indicated that the minimum incubation time for saturable Zn absorption was determined to be 50.83 min using the best fit line. The results in experiment 2 demonstrated that a Zn concentration of 400 μmol/L and an incubation time of 120 min were suitable to increase the absorption of Zn from Zn-Prot M compared to ZnS. In experiment 3, Zn absorption across cell monolayers was significantly increased by Zn addition (P  < 0.05), and was significantly greater with Zn-Prot M than with ZnS (P  < 0.05). Compared to the control, Zn addition significantly decreased Zn transporter 10 and peptide-transporter 1 mRNA expression levels and increased y + L-type amino transporter 2 (y + LAT2) protein abundance (P  < 0.05). Moreover, protein expression levels of zrt/irt-like protein 3 (ZIP3), zrt–irt-like protein 5 (ZIP5), and y + LAT2 were significantly greater for Zn-Prot M than for ZnS (P  < 0.05). These findings suggest that Zn-Prot M promote Zn absorption by increasing ZIP3, ZIP5 and y + LAT2 protein expression levels in primary duodenal epithelial cells. [ABSTRACT FROM AUTHOR]