The Effect of Urtica dioica Hydro-Alcoholic Extract on Glycemic Index and AMP-Activated Protein Kinase Levels in Diabetic Patients: A Randomized Single-Blind Clinical Trial

2016 ◽  
Vol 19 (3) ◽  
Author(s):  
Bahare Korani ◽  
Ali Mirzapour ◽  
Ali Akbar Moghadamnia ◽  
Soraya Khafri ◽  
Nahid Neamati ◽  
...  
Keyword(s):  
Clinical Trial ◽  
Protein Kinase ◽  
Glycemic Index ◽  
Urtica Dioica ◽  
Diabetic Patients ◽  
Alcoholic Extract ◽  
Amp Activated Protein Kinase ◽  
Single Blind

scholarly journals Coenzyme Q10 Attenuates High Glucose-Induced Endothelial Progenitor Cell Dysfunction through AMP-Activated Protein Kinase Pathways

2016 ◽  
Vol 2016 ◽  
pp. 1-14 ◽  
Author(s):  
Hsiao-Ya Tsai ◽  
Chih-Pei Lin ◽  
Po-Hsun Huang ◽  
Szu-Yuan Li ◽  
Jia-Shiong Chen ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Coenzyme Q10 ◽  
High Glucose ◽  
Endothelial Progenitor Cell ◽  
Progenitor Cell ◽  
Heme Oxygenase 1 ◽  
Diabetic Patients ◽  
No Production ◽  
Endothelial Progenitor ◽  
Amp Activated Protein Kinase

Coenzyme Q10 (CoQ10), an antiapoptosis enzyme, is stored in the mitochondria of cells. We investigated whether CoQ10 can attenuate high glucose-induced endothelial progenitor cell (EPC) apoptosis and clarified its mechanism. EPCs were incubated with normal glucose (5 mM) or high glucose (25 mM) enviroment for 3 days, followed by treatment with CoQ10 (10 μM) for 24 hr. Cell proliferation, nitric oxide (NO) production, and JC-1 assay were examined. The specific signal pathways of AMP-activated protein kinase (AMPK), eNOS/Akt, and heme oxygenase-1 (HO-1) were also assessed. High glucose reduced EPC functional activities, including proliferation and migration. Additionally, Akt/eNOS activity and NO production were downregulated in high glucose-stimulated EPCs. Administration of CoQ10 ameliorated high glucose-induced EPC apoptosis, including downregulation of caspase 3, upregulation of Bcl-2, and increase in mitochondrial membrane potential. Furthermore, treatment with CoQ10 reduced reactive oxygen species, enhanced eNOS/Akt activity, and increased HO-1 expression in high glucose-treated EPCs. These effects were negated by administration of AMPK inhibitor. Transplantation of CoQ10-treated EPCs under high glucose conditions into ischemic hindlimbs improved blood flow recovery. CoQ10 reduced high glucose-induced EPC apoptosis and dysfunction through upregulation of eNOS, HO-1 through the AMPK pathway. Our findings provide a potential treatment strategy targeting dysfunctional EPC in diabetic patients.

scholarly journals Isoginkgetin enhances adiponectin secretion from differentiated adiposarcoma cells via a novel pathway involving AMP-activated protein kinase

2007 ◽  
Vol 194 (3) ◽  
pp. 569-578 ◽  
Author(s):  
Guohong Liu ◽  
Mirta Grifman ◽  
James Macdonald ◽  
Peter Moller ◽  
Flossie Wong-Staal ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Metabolic Diseases ◽  
Diabetic Patients ◽  
Peroxisome Proliferators ◽  
Slight Effect ◽  
Increase Insulin Sensitivity ◽  
Plasma Adiponectin ◽  
Attractive Candidate ◽  
Diabetic Treatment ◽  
Amp Activated Protein Kinase

Adiponectin is an anti-diabetic hormone secreted byadipocytes. Circulating adiponectin levels are lower in obese and type II diabetic patients than in healthy people. Weight loss or thiazolidinedione treatment increases plasma adiponectin levels. Animal models and human studies suggest that elevated adiponectin levels increase insulin sensitivity. We screened a library of drug-like compounds and natural products for novel agents enhancing adiponectin production. We identified isoginkgetin, a compound derived from the leaves of Ginkgo biloba, to up-regulate adiponectin secretion with potency comparable to that of rosiglitazone, a known modulator of adiponectin production. However, unlike rosiglitazone, peroxisome proliferators-activated receptor γ activity seems not required for the action of isoginkgetin, and isoginkgetin has only a slight effect on adipogenesis, which makes it an attractive candidate for anti-diabetic treatment. Further investigation revealed that both isoginkgetin and rosiglitazone activate AMP-activated protein kinase (AMPK) in adipocytes. Our findings suggest a novel mechanism for the elevation of adiponectin by isoginkgetin, which is different from that of rosiglitazone. Furthermore, this novel mechanism for adiponectin regulation involving AMPK can potentially facilitate new understanding of metabolic diseases and identification of new targets, as well as agents that increase plasma adiponectin levels.

Chronic activation of AMP-activated protein kinase increases monocarboxylate transporter 2 and 4 expression in skeletal muscle

2017 ◽  
Vol 95 (8) ◽  
pp. 3552
Author(s):  
E. M. England ◽  
H. Shi ◽  
S. K. Matarneh ◽  
E. M. Oliver ◽  
E. T. Helm ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Monocarboxylate Transporter ◽  
Chronic Activation ◽  
Amp Activated Protein Kinase
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