Kolesnichenko L S, Kulinskiĭ V I
Fiziol Zh SSSR Im I M Sechenova. 1990 Oct;76(10):1418-25.
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.
应激、儿茶酚胺（CA）、环磷酸腺苷（cAMP）和蛋白激酶A对超氧化物歧化酶、过氧化氢酶、硫氧还蛋白还原酶、硫醇转移酶和谷胱甘肽还原酶（GR）没有影响。然而，它们可激活许多器官中的谷胱甘肽过氧化物酶和谷胱甘肽转移酶（GT），并抑制肾γ-谷氨酰转移酶。钙离子通过钙调蛋白激活GT。已发现CA可刺激谷胱甘肽从肝脏向血液的转运以及蛋白激酶C对GT的磷酸化作用。这表明激素和第二信使可调节谷胱甘肽代谢。这种调节有利于活性氧物质的代谢（包括免受过氧化物应激和白三烯C4合成的影响）、维持还原状态的SH蛋白、外源性物质的解毒。GT和GR的诱导在丁基羟基甲苯的抗过氧化物作用机制中可能起重要作用。
