1. The effects of peroxovanadate and peroxovanadyl on glucose metabolism in vivo and identification of signal transduction proteins involved in the mechanism of action in isolated soleus muscle.
- Author
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Yamazaki RK, Hirabara SM, Tchaikovski OJ, Lopes MC, Nogata C, Aikawa J, Nunes EA, Tanhoffer RA, Lissa MD, and Fernandes LC
- Subjects
- Animals, Diabetes Mellitus, Experimental etiology, Diabetes Mellitus, Experimental metabolism, Glycogen metabolism, Hyperglycemia etiology, Hyperglycemia physiopathology, Insulin pharmacology, Lactic Acid metabolism, Male, Mitogen-Activated Protein Kinase 1 metabolism, Mitogen-Activated Protein Kinase 3 metabolism, Muscle, Skeletal cytology, Muscle, Skeletal metabolism, Phosphorylation drug effects, Rats, Rats, Wistar, Vanadium Compounds chemistry, Glucose metabolism, Hypoglycemic Agents pharmacology, Muscle, Skeletal drug effects, Signal Transduction drug effects, Vanadates pharmacology, Vanadium Compounds pharmacology
- Abstract
The insulin-like effects of peroxovanate (POV) and peroxovanadyl (PSV) on rates of lactate formation and glycogen synthesis were measured in isolated incubated soleus muscle preparations. In another experiment rats were made insulin deficient by streptozotocin injection and treated with POV and PSV (0.25 mM) administered in the drinking water and in the course of 7 days glycemia were determined. Also, signal transduction proteins ERK 1 and ERK 2 involved in the insulin signaling were measured in soleus muscle of diabetic rats treated with POV and PSV. Peroxides of vanadate and vanadyl significantly stimulated glucose utilization in soleus muscle preparations in vitro. The stimulation of glycogen synthesis and lactate formation by POV and PSV was similar to insulin stimuli. Rats treated with POV or PSV presented reduction of glycemia, food and fluid intake with amelioration of the diabetic state during the short period of treatment (7 days). POV and PSV modulated ERK1/2 phosphorilation and the insulin administration in these rats caused an addictive effect on phosphorilation state of these proteins.
- Published
- 2005
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