Increasing reports suggest that cheese intake lowers the risk of developing metabolic syndrome (MS). However, the mechanism by which cheese prevents MS is poorly understood. In this study, we investigated the effect of cheese on improvement of lipid metabolism in liver using a fatty liver model induced by high fat plus cholesterol diet. Rats were fed for 28 days as followed; high fat diet (Hfat), high fat plus cholesterol diet (Control), or cheese plus cholesterol diet (Cheese). Then hepatic and fecal lipid were analyzed. The results showed that, in the cheese fed group, liver triglyceride and cholesterol as well as liver weight were significantly lower than those of control group. In addition, the fecal lipid level in cheese fed group was significantly higher than that of control group. These results suggest that the beneficial effects of cheese on metabolic syndrome may be due to lowering the fat deposition in liver and increasing fat excretion from feces.
Alamin 996 is a mixture of mineral contained in the milk whey and has been reported to be effective against dysmenorrhea This study aimed to investigate the effect of Alamin 996 on the prostaglandin F2α (PGF2α)-induced contraction in the isolated rat uterus. PGF2α induced the rhythmic contraction. The frequency of this contraction was concentration-dependently inhibited by Alamin 996, but the contractile force was not significantly affected. To clarify this inhibitory mechanism by Alamin996, the effects of BAY K 8644, Ca2+ channel agonist, and dantrolene, inhibitor of the calcium-induced calcium release from the endoplasmic reticulum, were tested. The inhibitory effect on the rhythmic contractile frequency by Alamin 996 was significantly and concentration-dependently attenuated by the addition of BAY K 8644, suggesting Alamin 996 did not affect on the smooth muscle contractile function. Even under the pretreatment with dantrolene, Alamin 996 concentration-dependently inhibited the rhythmic contractile frequency, suggesting no involvement of ryanodine receptor on the effect of Alamin 996. Alamin 996 was found to inhibit phospholipase C activity by in vitro study. The effect of Mg2+ containing Alamin 996 was tested. Mg2+ significantly and concentration-dependently inhibited the frequency of PGF2α-induced rhythmic contraction. Moreover, contractile force was also markedly inhibited, suggesting the difference of the inhibitory mechanism between Alamin 996 and Mg2+ sulfate. These results show that Alamin 996 inhibits the PGF2α-induced rhythmic contractile frequency without affecting the contractile force and that this inhibitory action mediated by inhibiting calcium release from the endoplasmic reticulum through phospholipase C may explain the utility of Alamin 996 against dysmenorrhea.
Lactoferrin (Lf) is an iron-binding glycoprotein found in many body fluids including bovine milk. Among its many biological functions, Lf can solubilize more than a 70 fold molar equivalent of iron in the presence of bicarbonate anions. Iron fortification of foods and nutraceuticals with the iron-Lf complex (FeLf) is attractive because of the high bioavailability of iron without adverse effects, such as metallic taste, irritation of gastric mucosa, and iron-catalyzed lipid oxidation. Thus, FeLf is a useful ingredient for the iron fortification of food for the prevention of anaemia. Additionally, FeLf is more stable against heat treatment and hydrolyzing enzymes than Lf, and possesses the palliative effects against dysmenorrhoea and mental stress. In the present review, we look back on 20 years of research and development on FeLf, and introduce key features of FeLf on application to food products.
Bifidobacteria rapidly colonize in the intestines of breast-fed infants after their births. Though human milk oligosaccharides (HMOs) were identified as the factor promoting intestinal growths of bifidobacteria 60 years ago, the molecular mechanism how bifidobacteria metabolize HMOs has not been clarified for long time. Discovery of the metabolic pathway specific to galacto-N-biose (GNB) and lacto-N-biose I (LNB) of bifidobacteria has led to reveal the mechanism, since components of HMOs often include the structure of LNB. Infant-type bifidobacterial species possess the GNB/LNB pathway. Extracellular enzymatic system liberating LNB from HMOs was identified from Bifidobacterium bifidum. On the other hand, Bifidobacterium longum subsp. infantis imports intact HMO to be hydrolyzed by intracellular enzymes, even though it possesses the GNB/LNB pathway. LNB is expected as potent bifidus factor for infant-type species. LNB was produced practically from sucrose and GlcNAc by using four bifidobacterial enzymes including enzymes constituting the GNB/LNB pathway.