1. [Functioning of tyrosine protein kinases and phosphatases in gastric mucosa cells under conditions of oxidative and nitrosative stress in gastric lesions].
- Author
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Bohdanova OV, Kot LI, Lavrova KV, and Ostapchenko LI
- Subjects
- Animals, Cell Membrane enzymology, Cell Membrane metabolism, Gastric Mucosa cytology, Gastric Mucosa enzymology, Hypothermia complications, Hypothermia enzymology, Hypothermia metabolism, Male, Rats, Reactive Oxygen Species metabolism, Restraint, Physical, Stomach Ulcer enzymology, Stomach Ulcer etiology, Stress, Psychological complications, Stress, Psychological enzymology, Stress, Psychological metabolism, Gastric Mucosa metabolism, Nitric Oxide metabolism, Oxidative Stress, Phosphoric Monoester Hydrolases metabolism, Protein-Tyrosine Kinases metabolism, Stomach Ulcer metabolism
- Abstract
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.
- Published
- 2008