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Effects of chronic intermittent cold stress on pituitary adrenocortical and sympathetic adrenomedullary functioning.

Basal and stress-induced pituitary-adrenocortical (PA) and sympathetic adrenomedullary (SAM) function was investigated in rats exposed to chronic intermittent cold stress (4 degrees C for 4 h a day for 21 days; CHR). We found that basal plasma levels of corticosterone (B), corticosteroid-binding-globulin, ACTH, epinephrine (E) and norepinephrine (NE) were similar in CHR and control (CTL) animals. In contrast, activity of the adrenal catecholamine-synthesizing enzyme tyrosine hydroxylase, but not phenylethanolamine-N-methyl transferase, was significantly elevated in CHR compared to CTL. Following exposure to a heterotypic stressor (20 min restraint), plasma levels of B were significantly higher in CHR than CTL, but the stress-induced levels of E and NE were not different between groups. These data suggest that, although basal PA function is not altered by exposure to chronic intermittent cold stress, components of the SAM system are affected by this paradigm, and that co-ordinate facilitation of both PA and SAM responses to a novel stressor is not a necessary consequence of exposure to chronic intermittent stress.

Adrenal Medulla↗

Cortisol binding capacity of corticosteroid binding globulin in hyperadrenocorticoid and healthy dogs.

Corticosteroid binding globulin (CBG) binding capacity and plasma cortisol concentration were determined in 27 dogs with hyperadrenocorticism and in 17 healthy control dogs. Cortisol concentrations were significantly higher in hyperadrenocorticoid dogs than in controls. CBG binding capacity did not differ between the two groups. It is concluded that excessive endogenous cortisol secretion does not induce an increase in CBG binding capacity. Consequently, the determination of CBG binding capacity provides no additional information for the diagnosis of canine Cushing's syndrome.

Animals↗

Characterization of [3H] corticosterone binding activity in adrenal incubation media.

Glucocorticoid-binding activity in adrenal incubation media was investigated with regard to characterization of a protein-like ligand. Scatchard analysis of corticosterone binding activity indicated the presence of a single non-interacting protein with a dissociation constant (Kd) of 8.81 X 10(-10) M (0 degrees C), a value which is different from that of plasma and cytoplasmic glucocorticoid binding proteins. In addition, an observed lack of affinity of the protein for dexamethasone distinguishes the protein from Type II cytoplasmic receptor proteins. Thus our data suggest a glucocorticoid-binding protein which is distinct from the two known groups of glucocorticoid-binding proteins, corticosteroid-binding globulin (CBG) and cytoplasmic receptors.

Adrenal Glands↗

Synthesis of some steroid spin labels.

An improved synthesis of spin-labeled cortisol, cortisone, and testosterone using N,N'-cyclohexylcarbodiimide (DCC) is reported. The spin labeled steroids are shown to result from the esterification at the most reactive C(21) and C(17) hydroxyl groups. A mild and high yield oxidation of cortisol spin label to cortisone spin label by chromium trioxide-pyridine is also discussed.

Cortisone↗

Preparation of electrophoretic variants of corticosteroid-binding globulin (CBG) using liquid liquid partition chromatography.

Human corticosteroid-binding globulin (CBG) was purified to homogeneity by application of three different chromatographic methods. After fractionation of pregnancy serum with ammonium sulfate the 80%-pellet was used for affinity chromatography based on tresyl activated Sepharose (Pharmacia, Uppsala, Sweden). The affinity eluate was injected into a Mono Q anion exchange column (Pharmacia). Fractions containing CBG were finally purified by liquid liquid chromatography on LiParGel 750 (Merck, Darmstadt, F.R.G.). The purified protein was characterized by IEF and PAGE. This paper describes a method for the chromatographic separation of the two variants of CBG without a loss of binding activity towards steroids for each of the two characteristic bands of this protein.

Chromatography, Affinity↗