Bioactive Components from Flowers ofSambucus nigraL. Increase Glucose Uptake in Primary Porcine Myotube Cultures and Reduce Fat Accumulation inCaenorhabditis elegans

2013 ◽  
Vol 61 (46) ◽  
pp. 11033-11040 ◽  
Author(s):  
Sumangala Bhattacharya ◽  
Kathrine B. Christensen ◽  
Louise C. B. Olsen ◽  
Lars P. Christensen ◽  
Kai Grevsen ◽  
...  
2018 ◽  
Vol 4 ◽  
Author(s):  
Hui-Chi Chen ◽  
Yu-Tang Tung ◽  
Sheng-Yi Chen ◽  
Jer-An Lin ◽  
Gow-Chin Yen

The increasing methylglyoxal (MG) level of body has been found in people with obesity and insulin resistance, resulting from their dietary style and abnormal metabolic functions. MG promotes inflammation, oxidative stress, glycation, and all of which are closely related to insulin resistance and chronic diseases. Phyllanthus emblica L. fruit has various bioactivities such as anti-inflammation, anti-diabetes, anti-nonalcoholic fatty liver, and anti-dyslipidemia. Therefore, this study was aimed to investigate the effects of water extract of P. emblica (WEPE) and its enriched compound, ellagic acid, on MG-induced inflammation, insulin resistance, and lipogenesis in 3T3-L1 cells. The results showed that MG activated the peroxisome proliferator activated receptor-gamma (PPARγ) and CCAAT/ enhancer-binding protein alpha (C/EBPα), which can increase adipogenesis in adipocytes. In addition, MG enhanced pro-inflammatory cytokine IL-6 protein expression and release through the activation of MAPK and NF-κB signaling pathway, as well as increasing the monocyte chemoattractant protein-1 expression to cause macrophage infiltration. MG also significantly reduced glucose uptake, indicating that insulin resistance in obese patients may be related to MG generation. WEPE and ellagic acid effectively decreased IL-6 protein expression and cytokine release through inactivation of JNK and p65 pathways. WEPE and ellagic acid significantly increased glucose uptake and reduced insulin resistance by MG treatment. WEPE also decreased the protein-tyrosine phosphatase 1B to reduce insulin resistance and inhibited MG-induced fat accumulation related proteins such as PPARγ, C/EBPα, FAS, and p-ACC. Therefore, WEPE may have the potential to ameliorate MG-induced inflammation, increase glucose uptake, and decrease fat accumulation.


Planta Medica ◽  
2010 ◽  
Vol 76 (12) ◽  
Author(s):  
K Christensen ◽  
D Kotowska ◽  
L Olsen ◽  
S Bhattacharya ◽  
X Fretté ◽  
...  

Planta Medica ◽  
2016 ◽  
Vol 81 (S 01) ◽  
pp. S1-S381
Author(s):  
HC Huang ◽  
CL Chao ◽  
SY Hwang ◽  
TC Chang ◽  
CH Chao ◽  
...  

Author(s):  
Siti N.H. Muhammad ◽  
Nik S. Yaacob ◽  
Nur A.M. Safuwan ◽  
Agustine N. Fauzi

Background: Survival and progression of cancer cells are highly dependent on aerobic glycolysis. Strobilanthes crispus has been shown to have promising anticancer effects on breast cancer cells. The involvement of the glycolysis pathway in producing these effects is unconfirmed, thus further investigation is required to elucidate this phenomenon. Objective: This study aims to determine the effect of S. crispus active fraction (F3) and its bioactive components on glycolysis in triple-negative breast cancer cells (MDA-MB-231). Methods: This study utilizes F3, lutein, β-sitosterol, and stigmasterol to be administered in MDA-MB-231 cells for measurement of antiglycolytic activities through cell poliferation, glucose uptake, and lactate concentration assays. Cell proliferation was assessed by MTT assay of MDA-MB-231 cells after treatment with F3 and its bioactive components lutein, β-sitosterol, and stigmasterol. The IC50 value in each compound was determined by MTT assay to be used in subsequent assays. The determination of glucose uptake activity and lactate concentration were quantified using fluorescence spectrophotometry. Results: Antiproliferative activities were observed for F3 and its bioactive components, with IC50 values of 100 µg/mL (F3), 20 µM (lutein), 25 µM (β-sitosterol), and 90 μM (stigmasterol) in MDA-MB-231 cells at 48 h. The percentage of glucose uptake and lactate concentration in MDA-MB-231 cells treated with F3, lutein, or β sitosterol were significantly lower than those observed in the untreated cells in a time-dependent manner. However, treatment with stigmasterol decreased the concentration of lactate without affecting the glucose uptake in MDA-MB-231 cells. Conclusion: The antiglycolytic activities of F3 on MDA-MB-231 cells are attributed to its bioactive components.


1983 ◽  
Vol 244 (6) ◽  
pp. E632-E635 ◽  
Author(s):  
I. Gottesman ◽  
L. Mandarino ◽  
J. Gerich

Using the glucose clamp technique, glucose uptake was determined isotopically in normal human volunteers at plasma glucose concentrations of congruent to 60, 95, and 160 mg/dl during insulin infusions that increased plasma insulin to congruent to 20, 80, and 160 microU/ml. Because glucose uptake was found to be a linear function of plasma insulin at each plasma glucose concentration (r greater than 0.92, P less than 0.01), glucose uptake at 0 plasma insulin was estimated by linear regression analysis. The values thus derived (1.30, 1.62, and 2.59 mg . kg-1 . min-1 for plasma glucose concentrations of 60, 95, and 160 mg/dl, respectively) produced a linear Eadie-Hofstee plot, suggesting that insulin-independent glucose uptake followed Michaelis-Menten kinetics. The Km for glucose uptake at 0 plasma insulin (congruent to 10 mM) was similar to those observed for glucose uptake at the other plasma insulin concentrations studied (congruent to 9-12 mM), but its Vmax was less (5.2 vs. 6.4, 18.5, and 26.8 mg . kg-1 . min-1 for congruent to 20, 80, and 160 U/ml, respectively). These results indicate that in postabsorptive human subjects 75-85% of glucose uptake is noninsulin-mediated and provide additional support for the concept that insulin may increase glucose uptake merely by providing additional transport sites. The method described herein provides an assessment of insulin-independent glucose uptake in vivo that may prove useful in distinguishing between intrinsic defects of the glucose transport system and those due to defects in insulin action.


1961 ◽  
Vol 201 (6) ◽  
pp. 1041-1043 ◽  
Author(s):  
J. M. Khanade ◽  
M. C. Nath

Lipogenesis and glucose uptake by epididymal fat pads of rats fed different diets have been investigated. Lipogenesis was found to be depressed in rats fed high fat, high fat and high protein, thyroid, thiouracil, and thiamine-deficient diets. The same dose of insulin causes varying degrees of lipogenesis in the tissues, depending on the type of diet fed previously. Lipogenesis is above normal in hydrolyzed glucose-cycloacetoacetate-fed rats but glucose uptake is not appreciably affected. The glucose uptake of adipose tissue is significantly depressed in rats fed high fat, high fat with high protein, and vitamin B1 deficient diets, and in rats with hypothyroidism. Both hyperthyroidism and hydrolyzed glucose-cycloacetoacetate feeding increase glucose uptake by the tissue. Alloxan diabetes reduces lipogenesis as well as glucose uptake.


2011 ◽  
Vol 77 (6) ◽  
pp. 2058-2070 ◽  
Author(s):  
Matthias Raberg ◽  
Katja Peplinski ◽  
Silvia Heiss ◽  
Armin Ehrenreich ◽  
Birgit Voigt ◽  
...  

ABSTRACTBy taking advantage of the available genome sequence ofRalstonia eutrophaH16, glucose uptake in the UV-generated glucose-utilizing mutantR. eutrophaG+1 was investigated by transcriptomic and proteomic analyses. Data revealed clear evidence that glucose is transported by a usuallyN-acetylglucosamine-specific phosphotransferase system (PTS)-type transport system, which in this mutant is probably overexpressed due to a derepression of the encodingnagoperon by an identified insertion mutation in gene H16_A0310 (nagR). Furthermore, a missense mutation innagE(membrane component EIICB), which yields a substitution of an alanine by threonine in NagE and may additionally increase glucose uptake, was identified. Phosphorylation of glucose is subsequently mediated by NagF (cytosolic PTS component EIIA-HPr-EI) or glucokinase (GlK), respectively. The inability of the defined deletion mutantR. eutrophaG+1 ΔnagFECto utilize glucose strongly confirms this finding. In addition, secondary effects of glucose, which is now intracellularly available as a carbon source, on the metabolism of the mutant cells in the stationary growth phase occurred: intracellular glucose degradation is stimulated by the stronger expression of enzymes involved in the 2-keto-3-deoxygluconate 6-phosphate (KDPG) pathway and in subsequent reactions yielding pyruvate. The intermediate phosphoenolpyruvate (PEP) in turn supports further glucose uptake by the Nag PTS. Pyruvate is then decarboxylated by the pyruvate dehydrogenase multienzyme complex to acetyl coenzyme A (acetyl-CoA), which is directed to poly(3-hydroxybutyrate). The polyester is then synthesized to a greater extent, as also indicated by the upregulation of various enzymes of poly-β-hydroxybutyrate (PHB) metabolism. The larger amounts of NADPH required for PHB synthesis are delivered by significantly increased quantities of proton-translocating NAD(P) transhydrogenases. The current study successfully combined transcriptomic and proteomic investigations to unravel the phenotype of this hitherto-undefined glucose-utilizing mutant.


2013 ◽  
Vol 455 (2) ◽  
pp. e1-e3
Author(s):  
James S. V. Lally ◽  
Gregory R. Steinberg

Skeletal muscle is critical for whole-body glucose homoeostasis. Insulin and muscle contractions induced by exercise can increase glucose uptake through distinct intracellular signalling pathways involving PKB (protein kinase B)/Akt and AMPK (AMP-activated protein kinase) respectively. Whereas the proximal events governing these processes are becoming well understood, less is known about the regulation of the complex events necessary for the control of glucose uptake at the plasma membrane. In recent years, a number of common targets of AMPK and PKB/Akt have emerged as important components controlling glucose uptake, but the necessary phosphorylation events required for the control of glucose uptake have remained more elusive. In the current issue of the Biochemical Journal, Liu et al. identify that PIKfyve, a phosphoinositide phosphate kinase, is required for contraction-stimulated glucose uptake. They demonstrate that AMPK directly phosphorylates PIKfyve at Ser307, the same site as PKB/Akt, and that phosphorylation is increased in response to muscle contractions. These data provide compelling evidence for a new AMPK substrate that converges with PKB/Akt signalling and may be critical for the control of glucose uptake in skeletal muscle.


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