Adrenothyroid System - History of the Question. Structural Organization and Mechanism of Regulatory Functions.

The review considers the fundamental bases of the structural organization and mechanisms of the regulatory functions of the adrenothyroid system. Impairment of adaptation mechanisms caused by activation of uncontrolled processes of a stress reaction or weakening of controlled stress reaction is primarily associated with disorders in the adrenothyroid relationship and the development of adrenothyroid dysfunction syndrome.

Adrenergic Receptors in the Mechanism of Regulation of Mitochondrial and Cytoplasmic Enzymes of Cardiomyocytes by Catecholamines.

We studied the role of adrenoceptors in the regulation of activity of mitochondrial and cytoplasmic enzymes in cardiomyocytes by catecholamines and their metabolites. Different types of adrenergic receptors (AR) agonists acting either on both α- and β-AR or selectively on α- or β-AR, as well as quinoid metabolites of catecholamines were used. It was found that the activating effect of β-AR agonist isadrin (isoproterenol) on succinate dehydrogenase of the mitochondria in the heart is prevented by β-adrenergic blockade.

[Metabolic effects of combined introduction of adrenalin and blocker of methanoprolol beta-adrenophyleters].

The effect of combined administration of adrenaline (0.4 mg/kg, i.p.

[Features of influence adenosine, AMP and hyperadrenalinemiya on the immune status, metabolic enzymes of purine nucleotides and the antioxidant defense system].

Administration of a large dose of adrenaline (4 mg/kg 60 min before analysis) increased blood levels of total leukocytes, lymphocytes, decreased T-cell suppressors, leukocyte migration inhibition reaction (LMIR) and NBT test, but increased the level of conjugated dienes (CD). Administration of AMPand adenosine increased levels of total leukocytes, lymphocytes, T- lymphocytes, T-helpers, decreased the level of malondialdehyde (MDA), LMIR, and T-cell suppressors. Sympathetic hyperactivation induced by administration of a large dose of adrenaline (4 mg/kg 60 min before analysis) was accompanied by an increase in heart and liver activities of glutathione peroxidase (GPx), catalase, AMP deaminase (AMPD), and adenosine deaminase (AD).

[Glutathione redox system, immune status, antioxidant enzymes and metabolism of purine nucleotides in hypothyroidism].

The immune status, components of the glutathione redox system, the activity of antioxidant enzymes and metabolism of purine nucleotides have been investigated in animals with experimental hypothyroidism. On day 8 after an increase in the number of leukocytes, lymphocytes, T-helpers and T-suppressors as well as increased number of B-lymphocytes was found in blood of thyroidectomized rats. This was accompanied by decreased activity of adenosine deaminase (AD), AMP-deaminase (AMPD), and 5'-nucleotidase (5'N) in blood, but the ratio of enzyme activity AD/AMPD increased.

Free radical oxidation in rats in the delayed period after combined exposure to dust and radiation.

We studied the intensity of free radical processes in organs (liver, spleen, thymus, lymph nodes of the small intestine, and adrenal glands) and cells (lymphocytes) in the delayed period after combined exposure to a sublethal dose of γ-radiation (6 Gy) and asbestos dust particles. Combined exposure was followed by accumulation of LPO metabolites (diene conjugates and malonic dialdehyde) in homogenates of the studied organs and resulted in antioxidant defense failure in experimental animals. Ionizing radiation have a pivotal role in these processes.

[Enzymes of purine nucleotide metabolism in assessment of the functional competence of the immune system].

Blood lymphocyte activities of 5'-nucleotidases, adenosine deaminase and AMP deaminase have been investigated for evaluation of immune system state of albino rats under normal conditions, immobilization stress and effect of radiation. Stress-induced reactions were characterized by changes of activities of these enzymes. However the ratios of activities 5'- nucleotidase/AMP-deaminase (coefficient A) and adenosine-deaminase/AMP-deaminase (coefficient B) were even more informative than separate analysis of these enzymes.

[Interrelations and characteristics of adrenergic and thyroid regulation of the enzymes of energy metabolism].

In experiments on albino male rats it was detected that noradrenaline and adrenoxyl intensify the triiodothyronine-125I binding in myocardial and hepatic nucleus mitochondria. Under the action of adrenaline, triiodothyronine the binding is activated in myocardial mitochondria and is diminished in the cardias and hepatic nuclea. Thyroxin and adrenoxyl enhance noradrenaline-3H uptake by the auricular, myocardial and hepatic sections.

[Functional importance of catecholamine metabolism in the regulation of AMP-aminohydrolase activity in mitochondria of the heart and other organs].

The paper deals with main pathways for conversion of catecholamines and their effect on the activity of AMP-aminohydrolase in mitochondria of the heart, liver, brain, kidneys and blood serum. Dopamine-beta hydroxylase is stated to participate in manifestation of dopamine effect on the heart AMP-aminohydrolase, the same may be said with respect to monoaminooxidase in realization of the norepinephrine action on the brain AMP-aminohydrolase. Adrenoxyl (stabilized adrenochrome) duplicates the catecholamine effect with respect to AMP-aminohydrolase in certain organs.

[Triiodothyronine binding and norepinephrine uptake in the heart and liver].

Administration of norepinephrine to thyroidectomized rats activates sharply the [125I]triiodothyronine binding by heart mitochondria and liver nuclei. Epinephrine stimulates the binding by the heart mitochondria and decreases the intensity of this process in the liver and heart nuclei and liver mitochondria As compared to norepinephrine, adrenoxyl is weaker in activation of [125I] triiodothyronine binding by the heart mitochondria and stronger in intensification of binding by the liver nuclei. Physiological concentrations of thyroxine like adrenoxyl administered to intact animals 2h before investigations intensify the uptake of [3H] norepinephrine by sections of the auricles, myocardium and liver.

[Thyroid hormones and mitochondrial cytochrome c oxidoreductase activity].

In the experiments on albino male rats it was shown that thyroid hormones, exerting organospecific effect, control both the activity and the amount of cytochrome-c-oxidoreductase in hepatic, renal, cardiac and cerebral mitochondria. In the mechanism of cytochrome-c-oxidoreductase regulation thyroxin effect is likely to be mediated by cytochrome c amount. Supraphysiological thyroxin concentrations exert a direct action on the enzyme, whereas its physiological levels regulate cytochrome-c-oxidase, acting as an inductor.

[Catecholamine metabolism and mitochondrial enzyme activity].

Specific effects of various catecholamines as well as functional dependence of mitochondrial enzymes activity on catecholamine metabolism were studied. Dopamine activated cytochrome c oxidase in heart mitochondria and decreased this enzymatic activity in liver tissue. Noradrenaline and adrenaline activated cytochrome c oxidase in liver, brain and kidney tissues.

[Adrenoreceptor-independent effect of thyroxine and adrenoxyl on myocardial adenyl cyclase activity and cAMP levels].

A study was made of the effect of different concentrations of noradrenaline, adrenaline, adrenoxyl (stabilized adrenochrome) and thyroxin on the adenylate cyclase activity and cAMP content in the myocardium of intact animals and in neurogenous affections of the myocardium. It was shown that the content of cAMP in the myocardium drops in neurogenous affections and that thyroxin or adrenoxyl in combination with beta-adrenoblockers (propranolol) might be used for the recovery of the cAMP content and adenylate cyclase activity.