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Biomedical subjects

L S Kolesnichenko

Publications and source records attributed to L S Kolesnichenko.

At least 19 recordsLinked to original sources
PubMed2005

Molecular mechanisms of hormonal activity. II. Kinase systems. Systems with intracellular receptors. Transactivation of STS.

Hormone receptors and other components, functional mechanisms, and biological role of analyzed signal transduction systems (STS) are described. The recently revealed module principle of the structure and STS transactivation providing diversity and plasticity of regulation are highlighted. STS activities are significantly changed in many diseases. Novel promising pharmaceuticals targeted to certain components of STS increase in number from year to year. The data published by the beginning of January 2004 are summarized in this review.

Animals↗
PubMed2005

Molecular mechanisms of hormonal activity. I. Receptors. Neuromediators. Systems with second messengers.

Hormone signal transfer along all of the cell compartments including nucleus is powered by signal transduction systems. Characteristics and importance of hormone receptors, principal components, functional mechanisms, and biological role of different systems with second messengers are described. Considerable examples of the importance of these systems for medicine are adduced. The drugs modifying these systems comprise more than 65% of contemporary medicines.

Animals↗
PubMed2003

Influence of changes in glutathione concentration on body temperature and tolerance to cerebral ischemia.

Two compounds that deplete glutathione (buthionine sulfoximine and diethyl maleate) with different mechanisms of action decrease body temperature and increase tolerance to complete global cerebral ischemia, both correlating closely with the glutathione concentration decrease. Glutathione apparently participates in the regulations of these functional parameters. GSH diethyl ester does not influence the latter, though it increases moderately the GSH concentration. Injection of GSH ester into the cerebral ventricles or subcutaneously selectively increases the GSH level in the brain and liver. An influence of the brain on the glutathione system in the liver was revealed. Diethyl maleate and GSH ester increase the activity of glutathione metabolizing enzymes under certain conditions.

Animals↗
PubMed1997

Current aspects of hormonology.

On the occasion of the 95th anniversary of the discovery of the first hormone, the definition and use of terms "hormone" and "second messenger" are discussed. The term "hormonology" is proposed to denote the fundamental science of hormones. The combined session in 1950 of the Academy of Sciences and the Academy of Medical Sciences of the USSR is thought to have had a negative effect on the development of hormonology in our country. Hormonology is one of the most rapidly developing branches of contemporary biology. New concepts on the generation of hormones in the majority if not all cells of an organism, on the obligatory regulation of all biologically essential processes, and on the importance and multiplicity of signal transduction systems are of general significance for biology. The development of fundamental hormonology is very important for contemporary medicine.

Hormones↗
PubMed1990

[The physiological significance of regulation by catecholamines, second messengers and enzyme inducers of glutathione metabolism].

Stress, catecholamines (CA), cAMP and protein-kinase A do not affect superoxide dismutase, catalase, thioredoxin reductase, thiol transferase and glutathione reductase (GR). However, they activate glutathione peroxidase and glutathione transferase (GT) in a number of organs and inhibit renal gamma-glutamyl transferase. Ca2+ ions activate GT through calmodulin. CA were found to stimulate GSH transport from liver to blood and GT phosphorylation by protein kinase C. This suggests a regulation of the GSH metabolism by hormones and a second messenger. This regulation favours metabolism of active O2 substances (including protection from peroxide stress and leukotriene C4 synthesis), supporting of SH-proteins in reduced state, xenobiotics detoxication. GT and GR induction can play an important role in the mechanism of anti-peroxide action of butylhydroxytoluene.

Animals↗
PubMed1987

[Activity of enzymes of glutathione metabolism and regulation by cAMP in human tumors].

Tumors were studied in 38 patients, tissues located far away from tumor being used as control. Breast and stomach tumors revealed relatively high levels of glutathione reductase, glutathione-S-transferase (I) and, particularly, gamma-glutamyl transferase (II). The said changes were not observed in colorectal tumors. Gamma-glutamyl transferase (II) may be used as a marker for breast and stomach malignancies in man but it is not a universal and absolutely specific marker for all tumors. The activity of glutathione peroxidase (III) either did not change or decreased. The activating effect of cAMP on III and I remained generally unchanged in all tumors studied.

Adult↗
PubMed1987

[Regulation by catecholamines and cAMP of enzymes of thiol and disulfide metabolism].

In vivo exo- and endogenous catecholamines have no influence on the activities of thioredoxin reductase, glutathione reductase, thiol transferase and nonselenium-dependent glutathione peroxidase. At the same time catecholamines activate via beta-adrenoceptors glutathione S-transferase and selenium-dependent glutathione peroxidase from many tissues and inhibit gamma-glutamyl transferase from kidney. In vitro cAMP has identical effects on the activities of the above enzymes. The possible significance of regulation of glutathione metabolism enzymes is discussed.

Adrenergic alpha-Agonists↗
PubMed1986

[Phosphorylation and inhibition of gamma-glutamyl transferase activity by cAMP-dependent protein kinase].

It was shown that preparations of bovine kidney gamma-glutamyl transferase with different degree of purity are phosphorylated by cAMP-dependent protein kinase. Phosphorylation is accompanied by a simultaneous decrease of both transferase and hydrolase activities of the enzyme. Hence, gamma-glutamyltransferase may serve as a substrate and target of regulation by cAMP-dependent protein kinase.

Animals↗
PubMed1983

[Disulfide reductase activity in mouse regenerating liver].

Fourteen hours after partial hepatectomy there was a decrease in basal disulfide reductase and glutathione reductase activity in cytosole fraction of proliferating hepatocytes. In nuclear fraction, the activation effect of cAMP and cGMP on the disulfide recovery was replaced by inhibition. Meanwhile the activity of glutathione reductase noticeably increased. Forty-five hours after operation disulfide reductase activity of cytosole appreciably rose during maximal mitotic activity of the regenerating liver. The data obtained provide evidence in favor of the involvement of disulfide reductase enzymes into reparative regeneration of the liver.

Animals↗
PubMed1977

[Different cooperativity of some oxidoreductases to specialized and nonspecialized regulators].

The activation of 2 different mouse liver enzymes: cytozolic disulfide reductase (DSR) and mitochondrial NAD-isocitrate dehydrogenase (ICDH), by catecholamines and especially by 3',5'-AMP is characterized by negative cooperativity; substrate (both enzymes), protamine and EDTA (DSR) produce the positive cooperativity type of activation; DSR activation by isopropyl noradrenaline and serotonine is characterized by hyperbolic kinetics. Consequently, one and the same enzyme can combine positive cooperativity to non-specialized regulators (substrate, protamine, EDTA) with negative cooperativity to specialized regulators (3',5'-AMP, catecholamines). The systems, switching on by catecholamines and 3',5'-AMP, are oligomeric, and the degree and even the type of cooperativity can modify depending on the kind of catecholamine. The negative cooperativity is revealed in literature for many effects of catecholamines and 3',5'-AMP. Probably, it guarantees the broad range of regulations. Dose effect curves for 3',5'-AMP, catecholamines and other hormones should be analyzed on the basis of allosteric protein kinetics. A simple nomogram is given to estimate nH less than 1.

Allosteric Regulation↗
PubMed1976

[Kinetics and regulatory properties of the disulfide reductase enzyme from mouse liver].

Disulfide reductase (DSR) of mice liver supernatant is kinetically demonstrated as associating-dissociating oligomeric protein with positive homotropic cooperativity for the substrate. Cyclic 3',5'-AMP (10(-11)--10(-5) M) activates DSR and increases V, but does not change either [S]0,5, nor nH and does not shift the plot of specific activity versus the enzyme concentration. ATP, GTP, UTP, CTP, protamine, histone, Mg2+, Ca2+, EDTA (but not adenosine, 5'-AMP, 2'3'-AMP, ADP beef serum albumin) activated DSR. The effects of different modifiers are not summed up. Preincubation is essential for the action of the majority of the activators. Heating for 8 minutes at 55 degrees C desensitized completely DSR to all the modifiers without changing its catalytic activity, [S]0,5 and nH values. Possible mechanisms of activation of DSR, especially the involvement of protein kinase, are discussed.

Animals↗
PubMed1976

[Detection and study of a protein factor mediating stimulation of disulfide reductase activity by cyclic 3', 5'-AMP and other effectors].

DSR stimulation in the supernatant fraction under the effect of 3', 5'-AMP 10(-7) M, ATP 5.10(-5) M, Mg2+5.10(-5) M, EDTA 5.10(-4) M and protamine 5 mg/ml was mediated through a factor which was readily sorbed by BaSO4, Al (OH)3 and activated carbon, and was easily eluated with a 10-fold increase of the buffer molarity. Barium eluates of the liver and of the brain restored the effect of 3', 5'-AMP eliminated by BaSO4, crosswise and equally. Apparently, the sorbed factor was a protein since it was not dialyzed, very thermolabile and readily inactivated by a low trypsin concentrations. The factor restored the DSR activation eliminated or decreased by the protein proteinkinase inhibitor (PPKI). A linear relationship between active quantities of the PPKI and the protein factor were in favour of the fact that the protein factor was affiliated or identical to proteinkinase. A possible biological significance of the DSR activation and the hypothesis on the existence of a special protamine-sensitive proteinkinase is discussed.

Animals↗