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PubMed1993

Involvement of neuropeptides in the regulation of growth, structure and function of the adrenal cortex.

Current data on the influence of neuropeptides on the growth, structure and function of cells comprising the hypothalamo-pituitary-adrenal axis were presented and discussed. The action of vasopressin, oxytocin, neurotensin, bombesin, neuropeptide Y, substance P and VIP have been evaluated. The hypothesis has been introduced that in vivo effect of some neuropeptides on the structure and function of the adrenal cortex is mediated by vasopressin.

Adrenal Cortex↗
PubMedDate not supplied

[Effect of thymectomy on the endocrine function of the adrenal cortex and testes in rats].

The paper is concerned with a study of endocrine function of the adrenal cortex and testes of rats after thymectomy using a radioimmunoassay. Postnatal thymectomy resulted after 3 months in a decrease in the level of corticosterone in the blood, the level of testosterone did not change as compared to that in animals after false operation. Thymectomized rats were characterized by a stronger sensitivity of the adrenals and gonads to physical exercise of moderate intensity which was expressed in a more significant elevation of the corticosterone level in the blood and a decrease in the testosterone level. A decrease in the Na+ concentration and an increase in the K+ content in erythrocytes and blood plasma were revealed in the thymectomized rats 3 and 6 mos after operation. A deficit of the thymus hormone influenced endocrine function of the adrenals and testes.

Adrenal Cortex↗
PubMed1975

[Relationship between the quality of dietary proteins and the functional status of the adrenal cortex. 5. Content of corticosterone and cortisol in the liver and in the mucosa of the small intestine of rats fed with proteins of various quality (estimation of binding capacity for corticosteroids)].

Relationships between the Quality of Dietary Proteins and the Functional State of the Adrenal Cortex. (5) Content of Corticosterone and Cortisol in the Liver and in the Mucosa of the Small Intestine of Rats Fed Proteins of Varying Quality (Estimation of the Binding Capacity for Corticosteroids). Growing male Wistar rats were used to investigate in which way the quality of dietary proteins (maize gluten and maize gluten supplemented with amino acids) influenced the content of corticosteroids in the liver and in the mucosa of the small intestine of untreated rats (N), adrenalectomized animals (AE) and animals treated with corticosteroids (N + S). In AE animals the content of corticosteroids in the tissues was very low. In N + S animals of both dietary groups the mucosa of the small intestine contained more corticosteroids than the liver; the content of corticosteroids in the mucosa, however, was also found to vary in dependence upon the diet fed. The mucosa of N + S animals receiving dietary proteins of high quality contained more corticosteroids; this indicates a higher binding capacity of the mucosa for corticosteroids.

Adrenal Cortex↗
PubMedDate not supplied

[Morphologic and biochemical study of the functional state of the adrenal cortex in the rat during prolonged hypokinesia].

Female rats exposed to 3-month hypokinesia were used to study adrenal morphology and plasma corticosterone. Prolonged hypokinesia (60-90 days) led to a dissociation between adrenal hypertrophy and lower corticosterone content in plasma. During hypokinesia rats were also exposed to an additional stress-effect, i.e. 5-hour immobilization. This approach showed that in the course of 90-day hypokinesia the adrenal cortex retained its ability to react to an acute stress by an enhanced corticosteroid secretion. Moreover, in response to stress-effects of identical strength and duration the experimental adrenals produced more corticosterone than the controls with no structural rearrangement or de-lipoidization.

Adaptation, Physiological↗
PubMed1977

Purification of bovine adrenal-cortex plasma-membrane vesicles containing a highly corticotropin-sensitive adenylate-cyclase system and angiotensin-II-binding sites.

The purpose of this experimental investigation was to provide a purified plasma membrane fraction containing a highly hormone-responsive adenylate cyclase system. Bovine adrenal cortex was homogenised and a washed pellet (450 000 X g - min) was fractionated by zonal centrifugation in a sucrose and dextran gradient. Adenylate cyclase activity was purified up to 60-fold to a specific activity of 55, 340 and 210 pmol of adenosine 3':5'-monophosphate (cyclic AMP) produced/minute per mg of protein at 38 degrees C for the basal, adrenocorticotrophin and fluoride-activated states, respectively. The time course of the adenylate cyclase activity is linear. The concentration necessary for half-maximal stimulation by adrenocorticotrophin-(1-24)-tetracosipeptide is 0.5 muM. The high hormone-responsiveness of the membrane preparation allows one to demonstrate activation of adenylate cyclase by very weakly agonistic adrenocorticotrophin fragments. The F- activated state can be detergent-dispersed by Lubrol and shows a Km (ATP) different from that of either the basal or adrenocorticotrophin-stimulated state. Other marked enzymes such as 5'-nucleotidase, glucose-6-phosphatase and cytochrome oxidase were followed during purification. The plasma membrane fraction shows rather homogeneous, relatively large vesicles (mean diameter 0.5 mum). It contains high-affinity binding sites for angiotensin II (about 2 pmol per mg protein) with an apparent association constant of 2 X 10(7) (1/mol) at 12 degrees C. The yield, 20 mg of membrane protein per preparation, may make it a tool in either affinity-labelling studies with the peptide hormones mentioned or the starting point for solubilisation and purification of adenylate cyclase.

Adenylyl Cyclases↗