Dehydroabietic acid activates peroxisome proliferator-activated receptor-γ and stimulates insulin-dependent glucose uptake into 3T3-L1 adipocytes

BioFactors ◽  
2011 ◽  
Vol 37 (4) ◽  
pp. 309-314 ◽  
Author(s):  
Nobuyuki Takahashi ◽  
Ran Yao ◽  
Min-Sook Kang ◽  
Mari Senda ◽  
Chieko Ando ◽  
...  
Keyword(s):  
Glucose Uptake ◽  
Dehydroabietic Acid ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
Insulin Dependent

In vitro Studies on Antidiabetic Potential of New Dosage Forms of AYUSH 82

2017 ◽  
Vol 2 (1) ◽  
pp. 1-9
Author(s):  
M Setia ◽  
K Meena ◽  
A Madaan ◽  
Kartar S Dhiman ◽  
JLN Sastry
Keyword(s):  
Glucose Uptake ◽  
Dosage Forms ◽  
C2c12 Myotubes ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
Test Items ◽  
Ppar Γ ◽  
Central Council ◽  
Insulin Dependent

ABSTRACT AYUSH 82 powder is an Ayurvedic antidiabetic formulation developed by the Central Council for Research in Ayurvedic Sciences (CCRAS), Ministry of AYUSH, Government of India. It comprises ingredients traditionally used for their beneficial effect in diabetes (Prameha/Madhumeha). The hypoglycemic effects of AYUSH 82 powder have been reported in diabetic subjects. In the current study, the antidiabetic potential of AYUSH 82 powder along with its two new dosage forms – AYUSH 82 mixture extract and AYUSH 82 compound extract- was investigated in vitro for elucidating mechanism of their action by possible α-amylase inhibitory property, insulin-dependent glucose uptake in skeletal muscle cell line (C2C12 myotubes), and effect on peroxisome proliferator-activated receptor gamma (PPAR-γ) activity. All the three dosage forms of AYUSH 82 – powder, mixture extract, and compound extract – exhibited inhibition of α-amylase activity. AYUSH 82 mixture extract, however, demonstrated highest extent of inhibition in both methanolic (87.4%) and aqueous (48.2%) format. All the three dosage forms of AYUSH 82 also demonstrated an increase in insulin-dependent glucose uptake in C2C12 myotubes as compared with control. However, none of the test items (TIs) exhibited activation of PPAR-γ expression in tested ranges, indicating that antidiabetic potential of TIs may not be mediated via PPAR-γ activation. Results indicated that the new dosage forms of AYUSH 82 (mixture extract and compound extract) may be useful for making new dosage forms of AYUSH 82 as tablets/capsule, etc. How to cite this article Setia M, Meena K, Madaan A, Srikanth N, Dhiman KS, Sastry JLN. In vitro Studies on Antidiabetic Potential of New Dosage Forms of AYUSH 82. J Drug Res Ayurvedic Sci 2017;2(1):1-9.

scholarly journals Exercise Training-Induced PPARβ Increases PGC-1α Protein Stability and Improves Insulin-Induced Glucose Uptake in Rodent Muscles

Nutrients ◽  
2020 ◽  
Vol 12 (3) ◽  
pp. 652 ◽  
Author(s):  
Ju-Sik Park ◽  
John O. Holloszy ◽  
Kijin Kim ◽  
Jin-Ho Koh
Keyword(s):  
Cytochrome C ◽  
Exercise Training ◽  
Protein Stability ◽  
Glucose Uptake ◽  
Citrate Synthase ◽  
Peroxisome Proliferator ◽  
Mitochondrial Enzymes ◽  
Mrna Levels ◽  
Dependent Manner ◽  
Peroxisome Proliferator Activated Receptor

This study aimed to investigate the long-term effects of training intervention and resting on protein expression and stability of peroxisome proliferator-activated receptor β/δ (PPARβ), peroxisome proliferator-activated receptor gamma coactivator 1-α (PGC1α), glucose transporter type 4 (GLUT4), and mitochondrial proteins, and determine whether glucose homeostasis can be regulated through stable expression of these proteins after training. Rats swam daily for 3, 6, 9, 14, or 28 days, and then allowed to rest for 5 days post-training. Protein and mRNA levels were measured in the skeletal muscles of these rats. PPARβ was overexpressed and knocked down in myotubes in the skeletal muscle to investigate the effects of swimming training on various signaling cascades of PGC-1α transcription, insulin signaling, and glucose uptake. Exercise training (Ext) upregulated PPARβ, PGC-1α, GLUT4, and mitochondrial enzymes, including NADH-ubiquinone oxidoreductase (NUO), cytochrome c oxidase subunit I (COX1), citrate synthase (CS), and cytochrome c (Cyto C) in a time-dependent manner and promoted the protein stability of PPARβ, PGC-1α, GLUT4, NUO, CS, and Cyto C, such that they were significantly upregulated 5 days after training cessation. PPARβ overexpression increased the PGC-1α protein levels post-translation and improved insulin-induced signaling responsiveness and glucose uptake. The present results indicate that Ext promotes the protein stability of key mitochondria enzymes GLUT4, PGC-1α, and PPARβ even after Ext cessation.

PGC-1α coactivates estrogen-related receptor-α to induce the expression of glucokinase

2010 ◽  
Vol 298 (6) ◽  
pp. E1210-E1218 ◽  
Author(s):  
Liu-Luan Zhu ◽  
Yang Liu ◽  
An-Fang Cui ◽  
Di Shao ◽  
Ji-Chao Liang ◽  
...  
Keyword(s):  
Enzyme Regulation ◽  
Regulatory Function ◽  
Acid Oxidation ◽  
Regulatory Sequence ◽  
Peroxisome Proliferator ◽  
Mobility Shift ◽  
Glucokinase Gene ◽  
Peroxisome Proliferator Activated Receptor ◽  
Insulin Dependent ◽  
Novel Target

Peroxisome proliferator-activated receptor-γ coactivator-1α (PGC-1α) is a key regulator of cellular energy metabolism and regulates processes such as adaptive thermogenesis, hepatic gluconeogenesis, fatty acid oxidation, and mitochondrial biogenesis by coactivating numerous nuclear receptors and transcription factors. Here, we demonstrate the presence of the ERRα binding site in the regulatory sequence of the glucokinase gene and that PGC-1α coactivates ERRα to stimulate the transcription of glucokinase. Simultaneous overexpression of PGC-1α and ERRα potently induced the glucokinase gene expression and its enzymatic activity in primary hepatocytes; however, expression of either PGC-1α or ERRα alone had no significant effect. Electrophoretic mobility shift and chromatin immunoprecipitation assays revealed the interaction of ERRα with the glucokinase promoter. Finally, the knockdown of endogenous ERRα with specific siRNA (siERRα) or pharmacological inhibition of ERRα with XCT790 attenuated insulin-induced glucokinase expression. Taken together, this research identifies glucokinase as a novel target of PGC-1α/ERRα and underscores the regulatory function of ERRα in insulin-dependent enzyme regulation.

scholarly journals Effects of Sulfonylureas on Peroxisome Proliferator-Activated Receptor γ Activity and on Glucose Uptake by Thiazolidinediones

2011 ◽  
Vol 35 (4) ◽  
pp. 340 ◽  
Author(s):  
Kyeong Won Lee ◽  
Yun Hyi Ku ◽  
Min Kim ◽  
Byung Yong Ahn ◽  
Sung Soo Chung ◽  
...  
Keyword(s):  
Glucose Uptake ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor

scholarly journals Effect of a novel non-thiazolidinedione peroxisome proliferator-activated receptor α/γ agonist on glucose uptake

Diabetologia ◽  
2007 ◽  
Vol 50 (5) ◽  
pp. 1048-1057 ◽  
Author(s):  
X. Hu ◽  
Y. Feng ◽  
X. Liu ◽  
X.-F. Zhao ◽  
J.-H. Yu ◽  
...  
Keyword(s):  
Glucose Uptake ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor

scholarly journals Deficiency of FcϵR1 Increases Body Weight Gain but Improves Glucose Tolerance in Diet-Induced Obese Mice

Endocrinology ◽  
2015 ◽  
Vol 156 (11) ◽  
pp. 4047-4058 ◽  
Author(s):  
Yun-Jung Lee ◽  
Conglin Liu ◽  
Mengyang Liao ◽  
Galina K. Sukhova ◽  
Jun Shirakawa ◽  
...  
Keyword(s):  
Body Weight ◽  
Adipose Tissue ◽  
Insulin Secretion ◽  
Weight Gain ◽  
Glucose Tolerance ◽  
Glucose Uptake ◽  
Body Weight Gain ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
Enhancer Binding Protein

Prior studies demonstrated increased plasma IgE in diabetic patients, but the direct participation of IgE in diabetes or obesity remains unknown. This study found that plasma IgE levels correlated inversely with body weight, body mass index, and body fat mass among a population of randomly selected obese women. IgE receptor FcϵR1-deficient (Fcer1a−/−) mice and diet-induced obesity (DIO) mice demonstrated that FcϵR1 deficiency in DIO mice increased food intake, reduced energy expenditure, and increased body weight gain but improved glucose tolerance and glucose-induced insulin secretion. White adipose tissue from Fcer1a−/− mice showed an increased expression of phospho-AKT, CCAAT/enhancer binding protein-α, peroxisome proliferator-activated receptor-γ, glucose transporter-4 (Glut4), and B-cell lymphoma 2 (Bcl2) but reduced uncoupling protein 1 (UCP1) and phosphorylated c-Jun N-terminal kinase (JNK) expression, tissue macrophage accumulation, and apoptosis, suggesting that IgE reduces adipogenesis and glucose uptake but induces energy expenditure, adipocyte apoptosis, and white adipose tissue inflammation. In 3T3-L1 cells, IgE inhibited the expression of CCAAT/enhancer binding protein-α and peroxisome proliferator-activated receptor-γ, and preadipocyte adipogenesis and induced adipocyte apoptosis. IgE reduced the 3T3-L1 cell expression of Glut4, phospho-AKT, and glucose uptake, which concurred with improved glucose tolerance in Fcer1a−/− mice. This study established two novel pathways of IgE in reducing body weight gain in DIO mice by suppressing adipogenesis and inducing adipocyte apoptosis while worsening glucose tolerance by reducing Glut4 expression, glucose uptake, and insulin secretion.

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