[The physiological significance of regulation by catecholamines, second messengers and enzyme inducers of glutathione metabolism].
Stress, catecholamines (CA), cAMP and protein-kinase A do not affect superoxide dismutase, catalase, thioredoxin reductase, thiol transferase and glutathione reductase (GR). However, they activate glutathione peroxidase and glutathione transferase (GT) in a number of organs and inhibit renal gamma-glutamyl transferase. Ca2+ ions activate GT through calmodulin. CA were found to stimulate GSH transport from liver to blood and GT phosphorylation by protein kinase C. This suggests a regulation of the GSH metabolism by hormones and a second messenger. This regulation favours metabolism of active O2 substances (including protection from peroxide stress and leukotriene C4 synthesis), supporting of SH-proteins in reduced state, xenobiotics detoxication. GT and GR induction can play an important role in the mechanism of anti-peroxide action of butylhydroxytoluene.
Kolesnichenko
L S
LS
Kulinskiĭ
V I
VI
D000818:Animals; D002395:Catecholamines / Q000502:physiology*; D000242:Cyclic AMP / Q000502:physiology; D004790:Enzyme Induction; D005978:Glutathione / Q000378:metabolism*; D006801:Humans; D010101:Oxygen Consumption / Q000502:physiology; D011494:Protein Kinases / Q000502:physiology; D015290:Second Messenger Systems / Q000502:physiology*; D013312:Stress, Physiological / Q000503:physiopathology
D002395:Catecholamines; D000242:Cyclic AMP; D011494:Protein Kinases; D005978:Glutathione
Fiziologicheskoe znachenie reguliatsii katekholaminami, vtorymi posrednikami i induktorami fermentov metabolizma glut5ationa.