To investigate the protein-sparing effect of α-lipoic acid (LA), experimental fish (initial body weight: 18·99 (sd 1·82) g) were fed on a 0, 600 or 1200 mg/kg α-LA diet for 56 d, and hepatocytes were treated with 20 μm compound C, the inhibitor of AMP kinase α (AMPKα), treated for 30 min before α-LA treatment for 24 h. LA significantly decreased lipid content of the whole body and other tissues (P<0·05), and it also promoted protein deposition in vivo (P<0·05). Further, dietary LA significantly decreased the TAG content of serum and increased the NEFA content of serum (P<0·05); however, there were no significant differences among all groups in the hepatopancreas and muscle (P>0·05). Consistent with results from the experiment in vitro, LA activated phosphorylation of AMPKα and notably increased the protein content of adipose TAG lipase in intraperitoneal fat, hepatopancreas and muscle in vivo (P<0·05). Meanwhile, LA significantly up-regulated the mRNA expression of genes involved in fatty acid β-oxidation in the same three areas, and LA also obviously down-regulated the mRNA expression of genes involved in amino acid catabolism in muscle (P<0·05). Besides, it was observed that LA significantly activated the mammalian target of rapamycin (mTOR) pathway in muscle of experimental fish (P<0·05). LA could promote lipolysis and fatty acid β-oxidation via increasing energy supply from lipid catabolism, and then, it could economise on the protein from energy production to increase protein deposition in grass carp. Besides, LA might directly promote protein synthesis through activating the mTOR pathway.

Prevention of the heat-induced aggregation of β-lactoglobulin (β-Lg) would improve the heat stability of whey proteins. The effects of lipoic acid (LA, or thioctic acid), in both its oxidised and reduced form (dihydrolipoic acid, DHLA), on heat-induced unfolding and aggregation of β-Lg were investigated. LA/DHLA was added to native β-Lg and the mixture was heated at 70, 75, 80 or 85 °C for up to 30 min at pH 6·8. The samples were analysed by Polyacrylamide Gel Electrophoresis (PAGE) and Size-exclusion HPLC (SE-HPLC). LA was not as effective as DHLA in reducing the formation of aggregates of heated β-Lg. Heating β-Lg with DHLA resulted in formation of more β-Lg monomers (due to dissociation of native dimers) and significantly less β-Lg aggregates, compared with heating β-Lg alone. The aggregates formed in the presence of DHLA were both covalently linked, via disulphide bonds, and non-covalently (hydrophobically) linked, but the amount of covalently linked aggregates was much less than when β-Lg was heated alone. The results suggest that DHLA was able to partially trap the reactive β-Lg monomer containing a free sulphydryl (−SH) group, by forming a ‘modified monomer’, and to prevent some sulphydryl−sulphydryl and sulphydryl−disulphide interactions that lead to the formation of covalently linked protein aggregates. The effects of DHLA were similar to those of N-ethylmaleimide (NEM) and dithio(bis)-p-nitrobenzoate (DTNB). However, the advantage of using DHLA over NEM and DTNB to lessen aggregation of β-Lg is that it is a food-grade compound which occurs naturally in milk.

Effects of dietary α-lipoic acid on hepatic and serum lipid concentrations and the activity and mRNA levels of lipogenic enzymes were examined in rats. Rats were fed experimental diets containing varying amounts of lipoic acid (0, 1, 2·5, 5 g/kg) for 21 d. Lipoic acid profoundly decreased serum and liver concentrations of TAG, and also lowered serum concentrations of phospholipid and NEFA, and the concentration of cholesterol in the liver. A hypoglycaemic effect of this compound was also observed. Lipoic acid dose-dependently decreased the activity and mRNA levels of fatty acid synthase, ATP-citrate lyase, glucose 6-phosphate dehydrogenase, malic enzyme and pyruvate kinase in the liver despite that reductions were considerably attenuated in the NADPH-producing enzymes. This compound also dose-dependently lowered the mRNA levels of spot 14, adiponutrin, stearoyl-CoA desaturase 1, and Δ5- and Δ6-desaturases. In addition, lipoic acid dose-dependently lowered serum concentrations of insulin and leptin, but increased those of adiponectin. Lipoic acid appeared to reduce hepatic lipogenesis and hence decreases serum and liver lipid levels. Alterations in serum concentrations of insulin and (or) adiponectin may trigger this consequence.

The present study was conducted to determine the effects of α-lipoic acid (ALA) on fatty acid mobilisation and ketone body production in female broiler chickens. In the first experiment, chickens received an intravenous infusion of ALA (0, 25 or 50 mg/kg per h) for 90 min. Blood was drawn at 30 min intervals, and plasma glucose, NEFA, free glycerol and hydroxybutyrate were analysed. In the second experiment, ALA (100 mg/kg per h) was continuously infused to chickens fed or fasted for at least 24 h. Changes in plasma metabolites for 90 min were determined. In the first experiment, as shown by the response area, ALA infusion did not affect plasma glucose but increased (P < 0·05) plasma NEFA, regardless of the dose level. In contrast, plasma hydroxybutyrate was reduced at the lower infusion rate (P < 0·05). No significant changes in plasma free glycerol were observed. In experiment 2, ALA stimulated both plasma glucose (P < 0·01) and NEFA (P < 0·001) and the responses were greater than those of controls, regardless of the feeding state. The interaction between ALA and the feeding condition had a significant effect on plasma hydroxybutyrate (P < 0·01). ALA reduced plasma hydroxybutyrate, and this response was greater in the fasted birds than in those fed. Therefore, the present study found a lowering effect of ALA on plasma hydroxybutyrate level and suggests that the ALA-induced plasma NEFA increment was attributable to decreased hepatic fatty acid oxidation in chickens.

The present study consisted of two experiments. The first experiment was conducted to determine the effects of lipoic acid (ALA; 200mg/kg) on plasma lipids and insulin sensitivity of whole-body tissue in broilers treated with or without corticosterone (5mg/kg). Chickens received these agents from 2 to 5 weeks of age in a 2×2 factorial arrangement. Thereafter, from 39 to 42d of age, insulin sensitivity was estimated using the euglycaemic and hyperinsulinaemic clamp technique. Experiment 2 examined whether ALA supplementation for 5 weeks (400mg/kg) would alter short-chain acyl-CoA concentration in the liver and in vitro lipolysis of an adipose tissue slice, in relation to noradrenaline (10μm) supplementation. In experiment 1, ALA had no effect on the corticosterone-induced negative growth performance. ALA lowered plasma glucose level (P<0·05) and, in contrast, increased triacylglycerol level (P<0·05). These responses to ALA had, however, no interrelationship with corticosterone. The rate of glucose uptake of whole-body P<0·05) but was not affected by noradrenaline supplementation. This study suggests that ALA stimulates the insulin sensitivity of tissues regardless of corticosterone-dependent metabolism and that the ALA-induced fatty acid metabolism of broilers differs between the liver and adipose tissue.

The present study was conducted to determine the role of α-lipoic acid (LA) in plasma metabolites, hepatic O2 consumption, and β-adrenergic response in broilers. In Expt 1, 12-d-old female broiler chicks were divided into three dietary groups and fed on diets with or without LA (5 or 50 mg/kg) until 4 or 6 weeks of age, as a 2 × 3 factorial arrangement. The dietary LA had no effect on growth rates (body weight, abdominal fat, breast muscle, and liver). The higher level of LA increased plasma non-esterified fatty acid and decreased plasma triacylglycerol concentrations only at 6 weeks of age. A 42 % increase in hepatic respiration was observed in the 4-week-old chickens given 50 mg LA/kg diet. In Expt 2, 3-d-old female broiler chicks were treated with or without dietary LA at 50 mg/kg. At 30 and 31 d old, isoproterenol (2 mg/kg body weight per h) was continuously infused into a wing vein for 2 h, and changes in plasma glucose, triacylglycerol, and non-esterified fatty acid concentrations were analysed. Isoproterenol increased plasma glucose over basal levels maximally at 60 min. Furthermore, the glucose increase in the LA-treated chickens was 35% greater than that of the controls at this time. Plasma non-esterified fatty acid and triacylglycerol concentrations were decreased by the isoproterenol infusion, regardless of LA administration. Therefore, the present study suggests that dietary LA has repartitioning effects on energy metabolism in chickens (although this depends on age-related metabolic state) and is a possible facilitator in the β-adrenergic response of plasma glucose to a β-agonist.