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PubMed1977

[Quantitative histoenzymologic characteristics of the human submandibular salivary glands].

Quantitative activity of oxidative-reductive and hydrolytic enzymes obtained during operation was investigated in different parts of the human submandibular salivary glands. Quantitative estimation of enzymic activity was done by photometry of the negatives prepared on MY-phi-6. Comparative examination of enzymatic activity made it possible to state that according to the peculiarities of metabolic processes, the cells of striated and intralobular secreting ducts are similar to the cells of the secreting terminal parts. A high activity of NADP-diaphorase, G-6-PhDG and acid phosphatase in the epithelium of the secreting ducts, and parallelism, stated between histoenzymatic and morphologic criteria of functional activity proved the participation of these structural-functional units in secret-producing processes. A high activity of NAK-diaphorase, LDG and acid phosphatase in all the parts and in the secreting ducts system, in particular, ensures, besides the processes of protein secret formation, an active transport of natrium and potassium, formation of final saliva and its discharge.

Acid Phosphatase↗
PubMed1990

[Disorders of myocardial metabolism in sudden coronary death in the presence of coronary atherosclerosis: findings of quantitative histoenzymologic studies].

The activity of human myocardial enzymes in sudden coronary death (SCD) was quantitatively histochemically examined. The activity of succinate dehydrogenase (SDH), lactate dehydrogenase (LDH), beta-oxybutyrate dehydrogenase (beta-OBDH), alpha-glycerolphosphate dehydrogenase (alpha-GPDH), NAD-diaphorase (NAD-ase), and glucose-6-phosphate dehydrogenase (G-6-PDH) was measured on prompt autopsies (up to 3 hours of death onset). beta-OBDH and LDH showed an increase in activity in the myocardium from the subjects who had suddenly died from coronary heart disease without evident changes in the heart. In SCD in the presence of small cardiosclerosis, the activity of the enzymes characterizing the major processes of energy generation was also enhanced, which was caused by moderately severe myocardial hypertrophy. In the myocardium from the subjects who had died from coronary heart disease in the presence of large postinfarction cardiosclerosis, the activity of the enzymes was directly related to the degree of myocardial hypertrophy and the signs of chronic heart failure. As myocardial hypertrophy progressed, the enzymatic activity rose, but there were signs of chronic heart failure, it fell. The findings suggest that the changes in myocardial enzymatic activity in SCD are heterogeneous and associated with the type of prior abnormalities in the cardiovascular system.

Autopsy↗
PubMed1989

Quantitative histoenzymological characteristics of the myocardium in sudden cardiac death.

Enzymes in the human myocardium following sudden death were examined for activity in a quantitative histoenzymological study, these were NAD-dependent dehadrogenases of succinate (SDG), lactate (LDG), beta-hydroxybutyrate (beta-HOBDG), alpha-glycerophosphate (alpha-GPDG), alcohol (ADG), glucoso-6-phosphate (G-6-PDG), and NAD-diaphorase (NADse), and catalase. Autopsies were performed within 3 h after death. beta-HOBDG and LDG were found to show an increase in activity in the cardiomyocytes of sudden death subjects with coronary heart disease without apparent changes. In the myocardium from death subjects with coronary heart disease and large postinfarct cardiosclerosis, the activity of the enzymes was directly related to the severity of myocardial hypertrophy and signs of chronic heart failure. As myocardial hypertrophy developed, the enzyme activity increased; when there appeared signs of chronic heart failure it decreased. The myocardium from sudden death subjects with alcoholic cardiomyopathy showed diminished redox enzyme activity and higher activity of the enzyme utilizing alcohol (ADG and catalase). The findings suggest that changes in the enzyme activity in the myocardium are of various type and depend on previous cardiac abnormalities.

Adult↗
PubMed1989

[The role of gonadotropins, cyclic AMP, 22-R-hydroxycholesterol and cofactors in regulating endocrine functions of the Leydig cells in rats. II. Effects of LH, hCG, dbcAMP, 22-R-OH-cholesterol and cofactors on the synthesis of pregnenolone and testosterone in the interstitial gland of rats].

The authors examined in vitro the influence of gonadotrophins, cAMP, 22-R-OH-cholesterol and cofactors on the synthesis of pregnenolon and testosterone in the interstitial gland of the rat. Sections of the nucleus were incubated with LH (100 ng/ml), hCG (1.0 j.m./ml), dbcAMP (1 mM), 22-R-OH-cholesterol (30 microM) and cofactors (NAD + NADP + G-6-P + G-6-PDH). It was found that an increase in concentrations of hCG above physiological values was not accompanied by an increase in secreting steroid hormones. LH, hCG and dbcAMP increased the synthesis of pregnenolon twice, and testosterone--three times. 22-R-OH-cholesterol as a substrate increased the synthesis three and four times respectively, and added cofactors five times and four and a half times respectively. Joining 22-R-OH-cholesterol or a cofactor with LH does not intensify a stimulating effect.

Animals↗
PubMed1989

[The role of gonadotropins, cyclic AMP, 22-R-OH-cholesterol and cofactors in regulating endocrine functions of the Leydig cells in rats. III. Mechanisms responsible for "desensitization" of the Leydig cells of rats caused by high doses of hCG].

Two groups of rats (a control group and the group examined) were administered intraperitoneally supraphysiological doses of hCG in order to induce a "down regulation" effect on the level of receptors LH and to achieve the desensibilization of Leydig cells. The authors tried to find out at which stage of sequence of changes from receptor stimulation to hormone production there appears a state of cellular resistance to further stimulation. Sections of the nucleus were incubated with various substances influencing steridogenesis (LH, hCG, dbcAMP, 22-R-OH-cholesterol, NAD + NADP + G-6-P + G-6-PDH). An index of the influence of the above substances on the synthesis of androgens were amounts of pregnenolon as the first and testosterone as the final stage of hormonal changes marked radioimmunologically in nucleus homogenates and incubating media. It was shown that the resistance of Leydig cells to further stimulation in the group of animals that were given high doses of hCG is the result of enzymatic blocks in testosterone synthesis. The first block is "late" block of 17 alpha-hydroxylase and 17-20 desmolase, disturbing transforming of 21-carbon steriods into 19-carbon androgens. When the dose of hCG increases, there appears the second block, the so called "early" block, disturbing mitochondrial synthesis of pregnenolon. It was found that exogenic cofactors are in a position, at least partially, to restore the activity of blocked enzymes.(ABSTRACT TRUNCATED AT 250 WORDS)

Aldehyde-Lyases↗
PubMed1989

[A histochemical study of enzyme activity in the myocardium of victims of sudden death with small-focal cardiosclerosis].

On the material of early autopsies of the above patients the activity of the following myocardial enzymes was undergone the quantitative histochemical study: succinate, lactate, (beta-oxybutyrate, d-glycerophosphate, glucose 6-phosphate and alcohol dehydrogenase, NAD-diaphorase, catalase, phosphorylase. The increase of the activity of practically all enzymes studied was observed in the myocardial areas with no circulation disturbances. This increase was due to the moderate myocardial hypertrophy. On the contrary, in the areas with a non-even blood supply (ischemia) the decrease of the activity of all oxidative-reductive enzymes was observed. The presence of such foci in the myocardium which occur in 70% cases studied facilitates the development of the ventricular fibrillation with a fatal outcome. The enzyme depression is particularly pronounced against the background of a high alcoholic content.

Alcohol Dehydrogenase↗
PubMed1989

[The role of gonadotropins, cyclic AMP, 22-R-hydroxycholesterol and cofactors in regulating endocrine functions of the Leydig cells in rats. I. Effect of cofactors on the synthesis of steroid hormones in the interstitial gland of rats].

The authors evaluated the influence of NAD, NADP, G-6-P and G-6-PDH on the synthesis of steroid hormones in the interstitial gland of the rat. The animals were killed by decapitation, and sections of the nucleus weighing altogether 20 mg were incubated with NAD (0.4 mM), NADP (0.4 mM), G-6-P (3.5 mM) and G-6-PDH (2 j.m./ml) for 4 hours in CO2 incubator. Then the tissue was homogenized, removed by centrifugation and then from the homogenous supernatant the authors extracted steroids which were in the incubating medium and in the tissue. Steroid hormones examined were marked radioimmunologically, they were: pregnenolon as the first and testosterone as the second stage of synthesis of nucleus androgens. The search carried out shows that the strongest stimulator in biosynthesis of pregnenolon was NADP together with the reducing system (G-6-P and G-6-PDH). On the other hand, in case of testosterone the highest effectiveness was achieved by simultaneous use of the cofactors examined. Applying cofactors separately the authors were able to find that both NAD and NADP together with the reducing system were responsible for testosterone synthesis and their simultaneous applying in the incubating medium leads to a synergistic effect.

Animals↗
PubMedDate not supplied

Detoxifying activities in alveolar macrophages of rats treated with acetylcysteine, diethyl maleate and/or aroclor.

Single or sequential treatment of rats with the thiol N-acetyl-L-cysteine (NAC), the glutathione depletor diethyl maleate (DEM) and the enzyme inducer Aroclor 1254 (AR) produced several significant variations on metabolic activities of pulmonary alveolar macrophages (PAM). Specifically, all three compounds elicited an increase in some oxidoreductase activities, including the two dehydrogenases involved in the hexose monophosphate shunt (G6PD and 6PGD) and NADH- or NADPH-dependent diaphorases. Diaphorase activities were especially increased by sequential treatments with AR and DEM or with DEM and NAC. Both NAC and AR also stimulated other detoxifying mechanisms, such as those related to GSH S-transferase activity and to the NADPH-dependent reduction of hexavalent chromium. Therefore, all the monitored parameters were significantly enhanced not only by the enzyme inducer, but also by the thiol, demonstrating its protective role in the biotransformation of mutagenic/carcinogenic compounds.

Acetylcysteine↗
PubMed1986

[The role of N-quinones in the regulation of glucose-6-phosphate metabolism].

In experimental (white rats, rabbits) and clinical (erythrocytes, blood plasma) studies on 29 healthy subjects and patients it has been demonstrated that primary or secondary n-quinone deficiency is accompanied by increased tissue activity of glycolysis enzymes (aldolase, PGmutase) and aerobic pentose phosphate shunt (6 GPDH). Parallel rise in the amount of glycolysis metabolites (pyruvate and lactate) in the blood and the decline in blood plasma glucose level were observed. The changes in glucose-6-phosphate metabolism are, probably, secondary and reflect tissue structure alterations in the development of K and E avitaminosis.

Animals↗
PubMedDate not supplied

[Disordered glucose-6-phosphate transport as a possible cause of glycogenosis type Ib].

More than ten patients with glycogen-storage disease, which were classified as patients with glycogenosis of the I type--deficiency in glucose-6-phosphatase) on the basis of clinical data and biochemical analyses in vivo, were detected within the last few years. But activity of glucose-6-phosphatase was found to be normal in biopsy of samples of the liver tissue obtained from these patients. This disease was termed as glycogenosis of the Ib type. A hypothesis is advanced, according to which the discrepancy in data on biochemical study of the patients in vivo and in vitro is due to absence of a specific permease in liver tissue, which transfers glucose-6-phosphate from cytosol onto the innesurface of membranes of cytoplasmic network, where glucose-6-phosphatase is located.

Adolescent↗
PubMed1973

Simplified spectrophotometric assay for microsomal 3-hydroxy-3-methylglutaryl CoA reductase by measurement of coenzyme A.

A new assay for 3-hydroxy-3-methylglutaryl CoA reductase (mevalonate:NADP oxidoreductase [acylating CoA], EC 1.1.1.34) is based upon the measurement of released coenzyme A (SH) during the reduction of 3-hydroxy-3-methylglutaryl CoA to mevalonate. Coenzyme A was measured in the presence of dithiothreitol, required for activity, by reaction with 5,5'-dithiobis(2-nitrobenzoic acid). Sodium arsenite forms a complex with the dithiol, but not with monothiols. Thus, reduced coenzyme A reacts instantaneously with the reagent and dithiothreitol reacts slowly. The absorbance due to the coenzyme A-5,5'-dithiobis(2-nitrobenzoic acid) reaction is determined by extrapolating the linear (dithiol) absorbance-time curve to the time of addition of the reagent. After subtraction of control absorbance (deletion of NADPH), the concentration of CoA-SH is calculated from epsilon(max) = 1.36 x 10(4) at 412 nm. The method of protein removal and reduction of sulfhydryl groups on the enzyme are critical. This method provides an immediate assay. Recovery of reduced coenzyme A was 98.7%. The assay is applicable for microsomes or purified enzyme and has an effective range of 0.5-50 nmoles of coenzyme A. It was applied to kinetic measurement of the pigeon liver microsomal enzyme reaction. The apparent K(m) value for 3-hydroxy-3-methylglutaryl CoA was 1.75 x 10(-5) M, and for NADPH the value was 6.81 x 10(-4) M. This method was compared with the dual-label method at high and low levels of activity. The data were not statistically different.

Alcohol Oxidoreductases↗