Objective: This study was conducted to investigate the effects of dietary multi-strain probiotic (MSP) (Bacillus coagulans Unique IS2 + Bacillus subtillis UBBS14 + Saccharomyces boulardii Unique 28) on performance, gut morphology and expression of nutrient transporter related genes in broiler chickens. Methods: A total of 256 (4×8×8) day-old CARIBRO Vishal commercial broiler chicks of uniform body weight were randomly distributed into four treatments with 8 replicates each and having eight chicks in each replicate. Four dietary treatments were T1 (negative control-basal diet), T2 (positive control-antibiotic bacitracin methylene disalicylate at 20 mg/kg diet), T3 (MSP at 107 colony-forming unit [CFU]/g feed), and T4 (MSP at 108 CFU/g feed). Results: During 3 to 6 weeks and 0 to 6 weeks, the body weight gain increased significantly (p<0.05) in T3 and T4 groups. The feed intake significantly (p<0.05) reduced from T1 to T3 during 0 to 3 weeks and the feed conversion ratio also significantly (p<0.05) improved in T3 and T4 during 0 to 6 weeks. The humoral and cell mediated immune response and the weight of immune organs were also significantly (p<0.05) improved in T3 and T4. However, significant (p<0.05) dietary effects were observed on intestinal histo-morphometry of ileum in T3 followed by T4 and T2. At 14 d post hatch, the relative gene expression of glucose transporter (GLUT5), sodium-dependent glucose transporter (SGLT1) and peptide transporter (PepT1) showed a significant (p<0.05) up-regulating pattern in T2, T3, and T4. Whereas, at 21 d post hatch, the gene expression of SGLT1 and PepT1 was significantly (p<0.05) downregulated in MSP supplemented treatments T3 and T4. Conclusion: The supplementation of MSP at 107 CFU/g diet showed significant effects with improved performance, immune response, gut morphology and expression of nutrient transporter genes. Thus, the MSP could be a suitable alternative to antibiotic growth promoters in chicken diets.
Objectives: This study aimed to observe the anti-diabetic effect and underlying mechanisms of Galgunhwanggumhwangryun-tang (GHH; Gegen-Qinlian-decoction) in the C2C12 myotubes. Methods: GHH (1.0 mg/ml) or metformin (0.75 mM) or insulin (100 nM) were treated in C2C12 myotubes after 4 days differentiation. The glucose uptake was assessed by 2-[N-(7-160 nitrobenz-2-oxa-1,3-diazol-4-yl)amino]-2-deoxy-d-glucose uptake by C2C12 cells. The expression of adenosine monophosphate-activated protein kinase (AMPK) and phosphorylation AMPK (pAMPK) were measured by western blot. We also evaluated gene expression of glucose transporter type 4 (Slc2a4, formerly known as GLUT4), glucokinase (Gk), carnitine palmitoyltransferase IA (Cpt1a), nuclear respiratory factors 1 (Nrf1), mitochondrial transcription factor A (Tfam), and peroxisome proliferator-activated receptor γ coactivator 1α (Ppargc1a) by quantitative real-time polymerase chain reaction. Results: GHH promoted glucose uptake in C2C12 myotubes. The expression of AMPK protein, which plays an essential role in glucose metabolism, was increased by treatment with GHH. GHH treatment tended to increase gene expression of Slc2a4, Gk, and Nrf1 but was not statistically significant. However, GHH significantly improved Tfam and Ppargc1a gene expression in C2C12 myotubes. Conclusions: In summary, GHH treatment promoted glucose uptake in C2C12 myotubes. We suggest that these effects are associated with increased gene expression involved in mitochondrial biosynthesis and oxidative phosphorylation, such as Tfam and Ppargc1a, and increased expression of AMPK protein.
The aim of this study was to investigate the expression patterns of key genes involved in lipid metabolism in response to dietary Coenzyme Q10 (CoQ10) in hens. A total of 36 forty week-old Lohmann Brown were randomly allocated into 3 groups consisting of 4 replicates of 3 birds. Laying hens were subjected to one of following treatments: Control (BD, basal diet), T1 (BD+ CoQ10 100 mg/kg diet) and T2 (BD+ micellar of CoQ10 100 mg/kg diet). Birds were fed ad libitum a basal diet or the basal diet supplemented with CoQ10 for 5 weeks. Total RNA was extracted from the liver for quantitative RT-PCR. The mRNA levels of HMG-CoA reductase(HMGCR) and sterol regulatory element-binding proteins(SREBP)2 were decreased more than 30~50% in the liver of birds fed a basal diet supplemented with CoQ10 (p<0.05). These findings suggest that dietary CoQ10 can reduce cholesterol levels by the suppression of the hepatic HMGCR and SREBP2 genes. The gene expressions of liver X receptor (LXR) and SREBP1 were down regulated due to the addition of CoQ10 to the feed (p<0.05). The homeostasis of cholesterol can be regulated by LXR and SREBP1 in cholesterol-low-conditions. The supplement of CoQ10 caused a decreased expression of lipid metabolism-related genes including $PPAR{\gamma}$, XBP1, FASN, and GLUTs in the liver of birds (p<0.05). These data suggest that CoQ10 might be used as a dietary supplement to reduce cholesterol levels and to regulate lipid homeostasis in laying hens.
Kwon, Eung Gi;Park, Byung Ki;Kim, Hyeong Cheol;Cho, Young Moo;Kim, Tae Il;Chang, Sun Sik;Oh, Young Kyoon;Kim, Nam Kuk;Kim, Jun Ho;Kim, Young Jun;Kim, Eun-Jib;Im, Seok Ki;Choi, Nag-Jin
Asian-Australasian Journal of Animal Sciences
/
v.22
no.12
/
pp.1654-1660
/
2009
This study was conducted to investigate the effects of different fattening periods i.e. 25, 27 and 29 months of age (25 mo, 27 mo and 29 mo), on feed consumption, body weight gain, carcass parameters, and lipogenic gene expression in 45 Korean native steers (Hanwoo). Daily DM intake was higher in steers on 29 mo compared with those on 25 mo or 27 mo. Daily body weight gain was higher in steers on 25 mo compared with those on 27 mo or 29 mo during fattening and overall experimental periods. Therefore, feed conversion ratio was lower in 25 mo compared with 27 mo or 29 mo during the fattening and whole experimental periods. As expected, slaughter and carcass weights were higher in the order of 29 mo>27 mo>25 mo. Carcass yield grade was relatively lower in 29 mo reflecting higher back fat thickness compared with other treatments, while carcass quality grade was not largely influenced by the treatments. By investigation with an ultra-sound scanning technique, the marbling score was significantly and numerically higher in 25 mo compared with 27 mo or 29 mo. The mRNA levels of stearoyl-CoA desaturase (SCD) gene were gradually increased in the late fattening stages (p<0.01) and mRNA of acetyl-CoA carboxylase (ACC), ATP citrate lyase (ACL) and glucose transporter 4 (GLUT4) gene were highly expressed in 29 mo compared with 25 mo and 27 mo (p<0.05). However, gene expressions of adipocyte fatty acid binding protein 4 (FABP4) and lipoprotein lipase (LPL) were not significantly different among the treatments. Thus the present results indicated that different fattening period has no major effect on carcass characteristics, although 25 mo had a lower carcass weight compared with 27 mo or 29 mo.
Bisphenol A (BPA), an environmental endocrine disrupter, enters the human body continuously in food and drink. Young children are likely to be more vulnerable than adults to chemical exposure due to the immaturities of their organ systems, rapid physical development, and higher ventilation, metabolic rates, and activity levels. The direct effect of BPA on peripheral tissue might also be of importance to the development of insulin resistance. However, the influence that BPA has on insulin signaling molecules in skeletal muscle has not been previously investigated. In this study, we examined the effect of BPA on fasting blood glucose (FBG) in post-weaned Wistar rats and on insulin signaling proteins in C2C12 skeletal muscle cells. Subsequently, we investigated the effects of BPA on insulin-mediated Akt phosphorylation in C2C12 myotubes. In rats, BPA treatment (0.1-1,000 ng/mL for 24 hours) resulted in the increase of FBG and plasma insulin levels, and reduced insulin-mediated Akt phosphorylation. Furthermore, the mRNA expression of insulin receptor (IR) was decreased after 24 hours of BPA treatment in C2C12 cells in a dose-dependent manner, whereas the mRNA levels of other insulin signaling proteins, including insulin receptor substrate-1 (IRS-1) and 5'-AMP-dependent protein kinase (AMPK), were unaffected. Treatment with BPA increased GLUT4 expression and protein tyrosine phosphatase 1B (PTP1B) activity in C2C12 myotubes, but not in protein levels. We conclude that exposure to BPA can induce insulin resistance by decreasing IR gene expression, which is followed by a decrease in insulin- mediated Akt activation and increased PTP1B activity.
Huang, Bo;Wang, Zhiqiang;Park, Jong Hyuk;Ryu, Ok Hyun;Choi, Moon Ki;Lee, Jae-Yong;Kang, Young-Hee;Lim, Soon Sung
Nutrition Research and Practice
/
v.9
no.1
/
pp.22-29
/
2015
BACKGROUND/OBJECTIVES: Recently, anthocyanins have been reported to have various biological activities. Furthermore, anthocyanin-rich purple corn extract (PCE) ameliorated insulin resistance and reduced diabetes-associated mesanginal fibrosis and inflammation, suggesting that it may have benefits for the prevention of diabetes and diabetes complications. In this study, we determined the anthocyanins and non-anthocyanin component of PCE by HPLC-ESI-MS and investigated its anti-diabetic activity and mechanisms using C57BL/KsJ db/db mice. MATERIALS/METHODS: The db/db mice were divided into four groups: diabetic control group (DC), 10 or 50 mg/kg PCE (PCE 10 or PCE 50), or 10 mg/kg pinitol (pinitol 10) and treated with drugs once per day for 8 weeks. During the experiment, body weight and blood glucose levels were measured every week. At the end of treatment, we measured several diabetic parameters. RESULTS: Compared to the DC group, Fasting blood glucose levels were 68% lower in PCE 50 group and 51% lower in the pinitol 10 group. Furthermore, the PCE 50 group showed 2-fold increased C-peptide and adiponectin levels and 20% decreased HbA1c levels, than in the DC group. In pancreatic islets morphology, the PCE- or pinitol-treated mice showed significant prevention of pancreatic ${\beta}$-cell damage and higher insulin content. Microarray analyses results indicating that gene and protein expressions associated with glycolysis and fatty acid metabolism in liver and fat tissues. In addition, purple corn extract increased the phosphorylation of AMP-activated protein kinase (AMPK) and decreased phosphoenolpyruvate carboxykinase (PEPCK), glucose 6-phosphatase (G6pase) genes in liver, and also increased glucose transporter 4 (GLUT4) expressions in skeletal muscle. CONCLUSIONS: Our results suggested that PCE exerted anti-diabetic effects through protection of pancreatic ${\beta}$-cells, increase of insulin secretion and AMPK activation in the liver of C57BL/KsJ db/db mice.
Purpose: The zinc transporter ZIP7 is known to regulate glucose metabolism in skeletal muscles, and skeletal muscles are known to play a critical role in glycemic control. The present study examines the effects of dietary zinc supplementation on the blood glucose concentration and expression of ZIP7 in skeletal muscle obtained from obese mice fed a high-fat diet (HF). Methods: C57BL/6J male mice were divided into three groups and were administered either a HF (60% of total calories from fat), HF supplemented with zinc (HF+Zn, 60% calories from fat + 300 mg zinc/kg diet), or low-fat diet (CON, 10% calories from fat), for 15 weeks. Results: Compared to CON group mice, the final body weights and adipose tissue weights were significantly increased, while the skeletal muscle weights were significantly decreased in mice belonging to the HF and HF+Zn groups. The HF+Zn group had significantly lower levels of fasting blood glucose concentrations than the HF group. Similarly, zinc supplementation significantly decreased the HF-elevated area under the curve values obtained from the oral glucose tolerance test. Skeletal muscle protein levels of ZIP7 in samples obtained from the HF group were significantly decreased as compared to the CON group. Conversely, the skeletal ZIP7 protein levels in the HF+Zn group were significantly increased as compared to the HF group. Moreover, the protein levels of phosphorylated-AKT and glucose transporter 4 in the skeletal muscle were significantly increased subsequent to zinc supplementation. Conclusion: Our data demonstrates that zinc supplementation up-regulates the skeletal muscle ZIP7 expression, which is associated with improved glucose tolerance in the obesity.
Oxygen is the final acceptor of electron transport from fat and carbohydrate oxidation, which is the rate-limiting factor for cellular ATP production. Under altitude hypoxia condition, energy reliance on anaerobic glycolysis increases to compensate for the shortfall caused by reduced fatty acid oxidation [1]. Therefore, training at altitude is expected to strongly influence the human metabolic system, and has the potential to be designed as a non-pharmacological or recreational intervention regimen for correcting diabetes or related metabolic problems. However, most people cannot accommodate high altitude exposure above 4500 M due to acute mountain sickness (AMS) and insulin resistance corresponding to a increased levels of the stress hormones cortisol and catecholamine [2]. Thus, less stringent conditions were evaluated to determine whether glucose tolerance and insulin sensitivity could be improved by moderate altitude exposure (below 4000 M). In 2003, we and another group in Austria reported that short-term moderate altitude exposure plus endurance-related physical activity significantly improves glucose tolerance (not fasting glucose) in humans [3,4], which is associated with the improvement in the whole-body insulin sensitivity [5]. With daily hiking at an altitude of approximately 4000 M, glucose tolerance can still be improved but fasting glucose was slightly elevated. Individuals vary widely in their response to altitude challenge. In particular, the improvement in glucose tolerance and insulin sensitivity by prolonged altitude hiking activity is not apparent in those individuals with low baseline DHEA-S concentration [6]. In addition, hematopoietic adaptation against altitude hypoxia can also be impaired in individuals with low DHEA-S. In short-lived mammals like rodents, the DHEA-S level is barely detectable since their adrenal cortex does not appear to produce this steroid [7]. In this model, exercise training recovery under prolonged hypoxia exposure (14-15% oxygen, 8 h per day for 6 weeks) can still improve insulin sensitivity, secondary to an effective suppression of adiposity [8]. Genetically obese rats exhibit hyperinsulinemia (sign of insulin resistance) with up-regulated baseline levels of AMP-activated protein kinase and AS160 phosphorylation in skeletal muscle compared to lean rats. After prolonged hypoxia training, this abnormality can be reversed concomitant with an approximately 50% increase in GLUT4 protein expression. Additionally, prolonged moderate hypoxia training results in decreased diffusion distance of muscle fiber (reduced cross-sectional area) without affecting muscle weight. In humans, moderate hypoxia increases postprandial blood distribution towards skeletal muscle during a training recovery. This physiological response plays a role in the redistribution of fuel storage among important energy storage sites and may explain its potent effect on changing body composition. Conclusion: Prolonged moderate altitude hypoxia (rangingfrom 1700 to 2400 M), but not acute high attitude hypoxia (above 4000 M), can effectively improve insulin sensitivity and glucose tolerance for humans and antagonizes the obese phenotype in animals with a genetic defect. In humans, the magnitude of the improvementvaries widely and correlates with baseline plasma DHEA-S levels. Compared to training at sea-level, training at altitude effectively decreases fat mass in parallel with increased muscle mass. This change may be associated with increased perfusion of insulin and fuel towards skeletal muscle that favors muscle competing postprandial fuel in circulation against adipose tissues.
Proceedings of the Korean Society of Applied Pharmacology
/
2002.07a
/
pp.113-113
/
2002
Phylogenetically conserved Bcl-2 family proteins play a pivotal role in the regulation of apoptosis from virus to human. Members of the Bcl-2 family consist of antiapoptotic proteins such as Bcl-2, Bcl-xL, and Bcl-w, and proapoptotic proteins such as BAD, Bax, BOD, and Bok. It has been proposed that anti- and proapoptotic Bcl-2 proteins regulate cell death by binding to each other and forming heterodimers. A delicate balance between anti- and proapoptotic Bcl-2 family members exists in each cell and the relative concentration of these two groups of proteins determines whether the cell survives or undergoes apoptosis. Mcl-1 (Myeloid cell :leukemia-1) is a member of the Bcl-2 family proteins and was originally cloned as a differentiation-induced early gene that was activated in the human myeloblastic leukemia cell line, ML-1 . Mcl-1 is expressed in a wide variety of tissues and cells including neoplastic ones. We recently identified a short splicing variant of Mcl-1 short (Mcl-IS) and designated the known Mcl-1 as Mcl-1 long (Mcl-lL). Mcl-lL protein exhibits antiapoptotic activity and possesses the BH (Bcl-2 homology) 1, BH2, BH3, and transmembrane (TM) domains found in related Bcl-2 proteins. In contrast, Mcl-1 S is a BH3 domain-only proapoptotic protein that heterodimerizes with Mcl-lL. Although both Mc1-lL and Mcl-lS proteins contain BH domains fecund in other Bcl-2 family proteins, they are distinguished by their unusually long N-terminal sequences containing PEST (proline, glutamic acid, serine, and threonine) motifs, four pairs of arginine residues, and alanine- and glycine-rich regions. In addition, the expression pattern of Mcl-1 protein is different from that of Bcl-2 suggesting a unique role (or Mcl-1 in apoptosis regulation. Tankyrasel (TRF1-interacting, ankyrin-related ADP-related polymerasel) was originally isolated based on its binding to TRF 1 (telomeric repeat binding factor-1) and contains the sterile alpha motif (SAM) module, 24 ankyrin (ANK) repeats, and the catalytic domain of poly(adenosine diphosphate-ribose) polymerase (PARP). Previous studies showed that tankyrasel promotes telomere elongation in human cells presumably by inhibiting TRFI though its poly(ADP-ribosyl)action by tankyrasel . In addition, tankyrasel poly(ADP-ribosyl)ates Insulin-responsive amino peptidase (IRAP), a resident protein of GLUT4 vesicles, and insulin stimulates the PARP activity of tankyrase1 through its phosphorylation by mitogen-activated protein kinase (MAPK). ADP-ribosylation is a posttranslational modification that usually results in a loss of protein activity presumably by enhancing protein turnover. However, little information is available regarding the physiological function(s) of tankyrase1 other than as a PARP enzyme. In the present study, we found tankyrasel as a specific-binding protein of Mcl-1 Overexpression of tankyrasel led to the inhibition of both the apoptotic activity of Mel-lS and the survival action of Mcl-lL in mammalian cells. Unlike other known tankyrasel-interacting proteins, tankyrasel did not poly(ADP-ribosyl)ate either of the Mcl-1 proteins despite its ability to decrease Mcl-1 proteins expression following coexpression. Therefore, this study provides a novel mechanism to regulate Mcl-1-modulated apoptosis in which tankyrasel downregulates the expression of Mcl-1 proteins without the involvement of its ADP-ribosylation activity.
This experiment was to know properties of Sericin Jam that development, growth of silkgland, content of sericin and composition of amino acid in hemolymph. The characters of Sericin Jam can he seen form this experiment. Hatching ratio was 85% in Sericin Jam and 95% in Jam 120. Especially hatching period of Sericin Jam was longer than Jam 120 and also hatching of Sericin Jam was ununiform. The larval duration of Sericin Jam was 20 days and 23 hours, and Jaw 120 was 21 days and 22 hours. In Sericin Jam, middle silkgland contain a great p arts in silkgalod and posterior silkgand is short and no curves. The period of mounting to emergence was 12 days in Sericin Jam. The period of pupa was 7day. It is property of Sericin Jam that the period is short. Cocoon was very thin and light in Sericin Jam. Weight of cocoon shell of Sericin Jam is 2.7cg. The sericin protein quantity was 100% in cocoon shell of Sericin Jam, about 28% in cocoon shell of Jam 120, however the sericin ratio per Sericin Jam cocoon was 34.6% compare to cocoon shell of Jaw 120 in sericin protein quantity. The amino acids in hemolymph of Sericin Jaw was much hidtidine, lysine, glut amic acid. And the amount of almost amino acids were increased depends upon development at t he 5th instar.
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