ABSTRACT
The content of reduced glutathione (GSH) and activity of glutathione-dependent enzymes: glutathione peroxidase (GP) and glutathione-S-transferase (GT) in blood serum of rats in the diet supplemented of fine powder seeds Trigonella foenum graecum L. on the background of experimental obesity. It was established that the development of obesity in rats was accompanied by violation of homeostasis in the glutathione-dependent system of blood serum. It has been shown that animals on high-calorie diet-along 14 weeks had a decrease (1,2) in GSH concentration, a decline (1,7) in GP activity and the increase (1,7) of GT activity compared with control values. Addition to high-calorie diet 2% fine powder seeds Trigonella foenum graccum L. reduced the body weight gain by 21%, carried positive modulating effect on the content of GSH and GP, GT activity in animals with experimental obesity.
Subject(s)
Antioxidants/metabolism , Glutathione Peroxidase/blood , Glutathione Transferase/blood , Glutathione/blood , Obesity/drug therapy , Plant Extracts/therapeutic use , Animal Feed , Animals , Body Weight/drug effects , Disease Models, Animal , Male , Obesity/blood , Plant Extracts/administration & dosage , Rats , TrigonellaABSTRACT
The goal of the presented work was the research of signal transduction mechanism in the rat gastric parietal cells under stomach ulcer conditions. In these cells activation of adenylate cyclase (increase of cAMP level and proteinkinase A activity) and phosphoinositide (increases [Ca2+]i; cGMP and phoshatidylinocitole levels; proteinkinase C, proteinkinase G, and calmodulin-dependent-proteinkinase activity) of signals pathway was shown. An increase of plasma membrane phospholipids (PC, PS, PE, PI, LPC) level was shown. Under conditions of influence of the stress factor the membran enzymes activity (H+, K+ -ATPase, 5'-AMPase, Na+, K+ -ATPase, Ca2+, Mg2+ -ATPase and H+, K+ -ATPase) was considerably increased. The intensification of lipid peroxidation processes in rats was demonstrated.
Subject(s)
Gastric Mucosa/metabolism , Signal Transduction , Stomach Ulcer/metabolism , Adenosine Triphosphatases/metabolism , Animals , Cyclic AMP/metabolism , Cyclic GMP/metabolism , Disease Models, Animal , Gastric Mucosa/pathology , Lipid Peroxidation , Male , Membrane Proteins/metabolism , Parietal Cells, Gastric/metabolism , Parietal Cells, Gastric/pathology , Rats , Rats, Wistar , Reactive Oxygen Species/metabolism , Restraint, Physical , Stomach Ulcer/enzymology , Stomach Ulcer/etiology , Stomach Ulcer/pathology , Stress, Psychological/complications , Stress, Psychological/metabolismABSTRACT
Acute cold stress caused lesions of gastric mucosa as a result of its attack by active oxygen and nitrogen compounds. The tissue regeneration is regulated by a cascade of tyrosine protein kinases. Gastric ulceration leads to a decrease in activity of tyrosine protein kinases and phosphatases, following by fall in phosphotyrosine content in proteins of plasma membranes of gastric mucosa cells. No changes in superoxide dismutase activity, slight increase in catalase activity, inhibition of glutathione peroxydase, significant increase in OH* content and decrease in zinc level were observed in the gastric mucosa cells of stressed rats. That increased oxidative damage can lead to inactivation of protein tyrosine phosphatases. Nitric oxide synthase activity was three times higher in gastric mucosa cells after the cold stress. That can promote nitrosylation of tyrosine residues. During following days nitric oxide synthase activity remains high. Superoxide dismutase is activated on the 4 and 5th day after the stress. Catalase activity normalizes after second day. Tyrosine protein kinase activity increases in membranes with maximum on the 4th day, and remains inhibited in cytosole. Tyrosine protein phosphatases keep inhibited as well. Gluthatione peroxydase activity and zinc level decreased on the 5th day. Obtained results can be the evidence of violations in signal transduction through protein tyrosine kinase cascades, due to the reduction in tyrosine phosphorylation, as a result of increase in the content of active oxygen and nitrogen species.
