Please use this identifier to cite or link to this item: https://biore.bio.bg.ac.rs/handle/123456789/4083
Title: Modifications of rat liver glucocorticoid receptor by insulin-induced hypoglycemia
Authors: Matić, Gordana 
Trajković, D.
Damjanović, S.
Petrović, J.
Issue Date: 1990
Journal: Biochim. Biophys. Acta
Series/Report no.: 1051;192-198
Abstract: 
Stability-, equilibrium- and kinetic binding parameters, transformation rate and sedimentation properties of liver cytosoi
glucocorticoid receptor from insulin-treated rats were studied. 40% elevation of cytosolic glucocorticoid binding and a
lower affinity of the receptor for ligand were observed in hypoglycemic rats as compared to the controls. A small but
significant decrease of [3H]triamcinolone acetonide-receptor complexes association rate and an increase of dissociation
rate were also found. The rate and the extent of activation of the complexes from insulin-treated rats were somewhat
higher compared to the controls, and the complexes from both groups showed higher affinity for the nuclei isolated from
insulin-treated animals. Mixing experiments suggested that insulin treatment lead to alterations at the level of both the
receptor protein and the nuclear binding sites. Sedimentation properties of transformed and untransformed receptor
remained unchanged upon insulin treatment. The physiological relevance of the data was confirmed by hypoglycemia-related
stimulation of tyrosine aminotransferase induction by dexamethasone.
URI: https://biore.bio.bg.ac.rs/handle/123456789/4083
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