ABSTRACT
BACKGROUND: Chinese herbal extract Number Ten (NT) is a dietary herbal formulation prepared from rhubarb, ginger, astragalus, red sage and tumeric. This study tested the effectiveness of NT in reducing body weight gain in rats. METHODS: Sixty female Wistar rats were fed a high fat diet and acclimated to gavage feeding. The rats were divided into five treatment groups: (1) Control (n = 15); (2) NT-H (n = 15), 1.5 g/day; (3) NT-L (n = 10), 0.75 g/day; (4) Pr-fed (n = 10), pair fed to NT-H; (5) d-FF (n = 10), d-fenfluramine 2 mg/kg. Ten rats per group were sacrificed on day 56. Weight, food intake, clinical chemistry and body composition were evaluated. Five animals in the control and 1.5 g/day NT groups were left untreated during a two week recovery period. RESULTS: The 0.75 g/day NT, 1.5 g/day NT, d-fenfluramine and pair fed groups gained 24.6%, 33.3%, 12.3% and 33.3% less than the control respectively (P < 0.0006). Leptin decreased 27.5% to 46.2% in the treatment groups vs. control (P < 0.009). Parametrial fat decreased 14.1% to 55.5% in the NT and pair fed groups vs. control (P < 0.006). The NT groups had soft stools, loss of hair around the mouth and coloration to the urine and stool without evidence of blood or bilirubin (attributed to chromogens in NT). There were no differences between groups in the clinical chemistry. CONCLUSION: This study demonstrated the efficacy of NT in reducing weight gain in rodents.
ABSTRACT
It has been suggested that the F1-ATPase beta-subunit is the enterostatin receptor. We investigated the binding activity of the purified protein with a labeled antagonist, beta-casomorphin1-7, in the absence and presence of cold enterostatin. 125I-beta-casomorphin1-7 weakly binds to the rat F1-ATPase beta-subunit. Binding was promoted by low concentrations of cold enterostatin but displaced by higher concentrations. To study the relationship between binding activity and feeding behavior, we examined the ability of a number of enterostatin analogs to affect beta-casomorphin1-7 binding to the F1-ATPase beta-subunit. Peptides that suppressed food intake promoted beta-casomorphin1-7 binding whereas peptides that stimulated food intake or did not affect the food intake displaced beta-casomorphin1-7 binding. Surface plasmon resonance measurements show that the beta-subunit of F1-ATPase binds immobilized enterostatin with a dissociation constant of 150 nM, where no binding could be detected for the assembled F1-ATPase complex. Western blot analysis showed the F1-ATPase beta-subunit was present on plasma and mitochondrial membranes of rat liver and amygdala. The data provides evidence that the F1-ATPase beta-subunit is the enterostatin receptor and suggests that enterostatin and beta-casomorphin1-7 bind to distinct sites on the protein.
