[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.