Hormones, glutathione status and protein S-thiolation.
The formation of mixed disulfides between proteins and glutathione has been discussed as a potentially interesting metabolic signal. The S-thiolation of proteins with glutathione has been observed in several systems in vitro. We have correlated the increase in glutathione disulfide (GSSG) with the amount of protein mixed disulfides. The methodological aspects are briefly presented; normal values for protSSG are about 20-30 nmol per g wet weight of liver. Several processes have been related to changes in the thiol redox state. The stimulation of flux through the pentose phosphate pathway during the metabolism of t-butyl hydroperoxide is presented, and the increase in cellular activity of glucose-6-phosphate dehydrogenase is correlated with the increase in the level of protSSG. Hormonal stimulation of GSH efflux from the liver by vasopressin or by alpha-adrenergic agonists such as phenylephrine or epinephrine is presented and discussed in relation to physiological states of peripheral (non hepatic) GSH utilization. Preliminary work relates the release of GSH to the perturbations in thiol redox state in inflammation and in exercise.
Sies
H
H
Institut für Physiologische Chemie I, Universität Düsseldorf, West Germany.
Brigelius
R
R
Graf
P
P
D000818:Animals; D004220:Disulfides / Q000378:metabolism*; D005978:Glutathione / Q000378:metabolism*; D006728:Hormones / Q000502:physiology*; D007249:Inflammation / Q000378:metabolism; D008099:Liver / Q000378:metabolism; D010084:Oxidation-Reduction; D010545:Peroxides / Q000378:metabolism; D005082:Physical Exertion; D051381:Rats; D013438:Sulfhydryl Compounds / Q000378:metabolism; D020122:tert-Butylhydroperoxide
D004220:Disulfides; D006728:Hormones; D010545:Peroxides; D013438:Sulfhydryl Compounds; D020122:tert-Butylhydroperoxide; D005978:Glutathione