Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.6.99.1 (NADPH-diaphorase)
3,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Quantitative histochemical assays of several enzymes (succinic, lactic, beta-hydroxybutyrate, alpha-glycerophosphate, and glucose-6-phosphate dehydrogenases, NAD diaphorase, and phosphorylase) in the myocardium of persons who had died suddenly with postinfarctional cardiosclerosis have failed to reveal any changes specific for this patient group. Direct correlations were established between the enzyme activities assayed, on the one hand, and the extent of myocardial hypertrophy and the signs of chronic heart failure, on the other. The activities of beta-hydroxybutyrate dehydrogenase and glucose-6-phosphate dehydrogenase, which are involved in fatty acid utilization and in the pentose phosphate pathway, were elevated in cases of moderate hypertrophy, as were those of all redox enzymes in cases of strongly marked hypertrophy, although they were reduced in cases with signs of chronic cardiac failure despite the presence of considerable myocardial hypertrophy. Areas of acute myocardial ischemia were discovered in 45% of the cases.
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PMID:[Histochemical study of the enzyme activity of the myocardium of sudden death victims with postinfarct cardiosclerosis]. 296 Feb 98

The purpose of this study was to evaluate the effect of endurance exercise on the histochemistry and wet weight of the reinnervating rat plantaris muscle. Two groups of young female Wistar rats (6 weeks old), 1 sedentary denervated control (n = 13) and 1 exercised denervated experimental (n = 17), were denervated unilaterally by cutting and resecting the sciatic nerve. To effect reinnervation a skin grafting operation was carried out on the nerve so that the gap caused by resection was bridged. The third group was the sedentary non-denervated normal control (n = 10). A progressive training program of 18 weeks of treadmill running was carried out by the experimental group. Approximately 5 months after denervation, the plantaris muscles were studied histochemically for reduced nicotinamide adenine dinucleotide diaphorase (NADH-D) and mitochondrial alpha-glycerophosphate dehydrogenase (alpha-GPD) activities. Fibres were classified as "red", "white", or "intermediate" with NADH-D. Alpha-GPD differentiates "intermediate" from "red" fibre types in case of difficulty in differentiating these fibre types from each other with NADH-D. The weight of the reinnervated plantaris muscle increased significantly after exercise. The exercise did not change the fibre type proportions--including "red" fibre type--in the deep region of the reinnervating plantaris. There were significant differences between normal control and denervated control or experimental groups in histochemical fibre populations in the deep region of the plantaris. The findings of this study suggest that: treadmill running did not increase the oxidative capacity of the deep region of the reinnervating rat plantaris muscle; treadmill training did not damage the reinnervating plantaris.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effect of endurance exercise on fibre type composition and muscle weight of reinnervating rat plantaris muscle. 358 51

Thirty-six wild-caught woodchucks (Marmota monax) were characterized according to sex, weight, trapping locality, liver pathology, and serum or hepatic markers of woodchuck hepatitis virus. Liver subcellular fractions were assayed for microsomal cytochromes P-450, aryl hydrocarbon hydroxylase, glutathione, cytosolic enzymes involved in its metabolism (glutathione S-transferase, glutathione peroxidase, and glutathione reductase), in the hexose monophosphate shunt (glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase), NADH- and NADPH-dependent diaphorases, and DT diaphorase. Moreover, liver postmitochondrial fractions were assayed for their ability to activate procarcinogens [i.e., a tryptophan pyrolysate product, aflatoxin B1, 2-aminofluorene, and trans-7,8-dihydrobenzo(a)pyrene] to mutagenic metabolites in the Ames reversion test and to decrease the activity of direct-acting mutagens [i.e., 4-nitroquinoline N-oxide, 2-methoxy-6-chloro-9-[3-(2-chloroethyl)aminopropylamino]acridine X 2HCl, and sodium dichromate]. A considerable interindividual variability in metabolism was observed among the examined woodchucks. Some of the investigated parameters were more elevated in virus carriers, especially in those suffering from chronic active hepatitis, but only a few of the recorded differences (i.e., oxidized glutathione reductase and NADPH-dependent diaphorase) were statistically significant. The comparison of the monitored activities in woodchucks and in other rodent species (rat and mouse) led to the conclusion that the liver metabolism of mutagens and carcinogens in woodchucks is more oriented in the sense of activation, while detoxification mechanisms are more efficient in rats and mice.
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PMID:Metabolism of mutagens and carcinogens in woodchuck liver and its relationship with hepatitis virus infection. 360 50

The individual effects of two putative metabolites of primaquine (5,6-dihydroxyprimaquine and 5,6-dihydroxy-8-aminoquinoline) on the hexose monophosphate shunt (HMS) and on the ATP-dependent proteolytic system which rapidly degrades oxidized erythrocyte protein were measured in intact red blood cells in vitro from two blood donors. In red cells treated with nitrite (1-40 mM) or phenylhydrazine (0.01-10 mM), proteolytic activity was detected only with concentrations (7.5 mM NaNO2 and 0.25 mM phenylhydrazine) causing greater than 15-fold elevation of HMS activity, and glucose-6-phosphate dehydrogenase (G6PD)-deficient (25% of normal activity) red cell suspensions thus treated showed approximately 30% greater proteolysis. G6PD-normal and deficient red cells treated with the primaquine analogs, however, did not experience proteolysis with concentrations (0.25 mM) in excess of those causing 17-fold elevation of HMS activity. Stimulation of the HMS by the primaquine analogs thus appears unrelated to an erythrotoxic oxidative stress. Methylene blue is known to cause an elevation of HMS activity through direct and diaphorase II-dependent oxidation of reduced nicotinamide adenine dinucleotide phosphate (NADPH) which is independent of injurious oxidative stress. It was found that the putative primaquine metabolites also caused direct and diaphorase II-dependent oxidation of NADPH in dilute hemolysate, thus suggesting that the putative primaquine metabolites have a methylene blue-like redox disposition in red blood cells. Results obtained in this study suggest that the hemolytic toxicity of primaquine may be unrelated to processes which lead to oxidative deterioration of red cell protein.
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PMID:Oxidative activity of hydroxylated primaquine analogs. Non-toxicity to glucose-6-phosphate dehydrogenase-deficient human red blood cells in vitro. 375 45

Study of the activity of some myocardial enzymes in sudden death cases with alcoholic cardiomyopathy (ACMP) was made by quantitative histochemical methods. The decrease of dehydrogenase activity of succinate, lactate, beta-hydroxybutyrate, alpha-glycerophosphate and NAD-diaphorase was found in line with the increase of the activity of glucose-6-phosphate dehydrogenase, alcohol dehydrogenase and catalase versus control (myocardium of those who died of trauma). Disorders of major metabolic processes in the myocardium may occasionally lead to electrical instability resulting in ventricular fibrillation and sudden cardiac death. In almost 80% of sudden cardiac deaths in ACMP foci of acute myocardial ischemia are found, that can lead to ventricular fibrillation with lethal outcome.
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PMID:[Histoenzymologic characteristics of the myocardium in sudden death in patients with alcoholic cardiomyopathy]. 380 Jun 78

The biochemical basis for paraquat tolerance was investigated using one of the paraquat-resistant Escherichia coli mutants previously isolated. When grown in the absence of paraquat (PQ2+), the specific activities of glucose-6-phosphate dehydrogenase and NADPH:PQ2+-diaphorase, both required for the expression of PQ2+ toxicity, were comparable in the wild type and the mutant. However, growth in the presence of 1 mM PQ2+ resulted in greater induction of these two enzymes in the wild type than in the mutant. Nevertheless, when the mutant was grown in 50 mM PQ2+, the activities of these two enzymes were comparable to those of the wild type grown in the presence of 1 mM PQ2+. Measurement of cyanide-resistant respiration, an indication of intracellular superoxide generation, showed that the intracellular flux of superoxide mediated by subsaturating concentrations of paraquat was significantly lower in the mutant than in the wild type. Extracellular superoxide formation, as measured by superoxide dismutase-inhibitable cytochrome c reduction, was higher in the wild type than in the mutant whether grown in the absence or the presence of PQ2+. The mutant did not show cross-resistance toward juglone or plumbagin, compounds known to exacerbate superoxide generation. The kinetics of [14C]PQ2+ uptake showed that the wild type accumulated PQ2+ against a concentration gradient, whereas the mutant seemed to do so only by facilitated diffusion. The results indicate that the impaired paraquat uptake system in the mutant results in the physiological and biochemical differences observed between the wild type and mutant.
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PMID:Biochemical characterization of a paraquat-tolerant mutant of Escherichia coli. 389 18

The Fab fragment of rabbit IgG antibody to bacterial glucose 6-phosphate dehydrogenase covalently linked to the cortisol retained the capacity to inhibit the enzyme completely. In optimal conditions the antibody to cortisol effectively bound the cortisol residues of the cortisol-Fab conjugate, making it incapable of inhibiting the enzyme. The enzyme modulatory properties of the cortisol-Fab conjugate were exploited to set up a direct competitive homogeneous enzyme immunoassay for cortisol in human serum. The procedure involved the use of the auxiliary enzyme diaphorase, specific for NADH, which converts the nitro blue tetrazolium salt to a colored formazan. The procedure detects modulated glucose 6-phosphate dehydrogenase activity by a single-point measurement without serum interference. The assay working range was between 20 and 640 micrograms/1 of cortisol and used 50 microliters of sample.
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PMID:Homogeneous colorimetric enzyme inhibition immunoassay for cortisol in human serum with Fab anti-glucose 6-phosphate dehydrogenase as a label modulator. 389 82

Biochemical, cytochemical and immunological methods were used to compare the metabolic and neuroendocrine properties of the subfornical organ (SFO) with the hypothalamo-neurohypophysial system (HNS) in the rat. The SFO resembles the HNS in that both have (a) increased label incorporation into RNA during dehydration; (b) an intense reaction for glucose-6-phosphate dehydrogenase; (c) NADPH-diaphorase and the Type I pathway for hydrogen utilization from NADPH, presumably as part of the mixed-function oxidase system for the metabolism of endogenous substrates and xenobiotics; (d) immunoreactive vasopressin and oxytocin. Gel filtration of extracts of the SFO area using Sephadex G-25 chromatography resulted in immunoreactive peaks for both AVP and OT which were similar to synthetic hormones. One other fraction in the SFO extract, containing a substance(s) of higher molecular weight than AVP, was detected using the antiserum for AVP. The concentration of immunoreactive AVP in the SFO area was increased after colchicine, decreased by hypophysectomy, and unaltered by: (a) infusion (4.6 pg/min for 3 hr) or injection (1 or 6 ng) of AVP into the lateral cerebroventricle; (b) dehydration; (c) renin administered intracerebroventricularly; (d) pinealectomy; or (e) hypertension in the spontaneously hypertensive rat. In conclusion, cells in the SFO have specialized metabolic and neuroendocrine properties similar to the HNS. It can be inferred from these biochemical specializations that the SFO has metabolic and secretory activities.
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PMID:The subfornical organ: biochemical and neuroendocrine comparisons with the hypothalamo-neurohypophysial system. 402 8

Histochemical study of enzymatic activity in the myocardium was performed in sudden cardiac death. Human hearts in which there were no macroscopic and histological focal or diffuse changes served as material. The following enzymes were studied in the anterior or posterior walls of the left ventricle or in the interventricular septum: succinate dehydrogenase, lactate dehydrogenase (LDH), beta-hydroxybutyrate dehydrogenase (OHBDH), alpha-glycerophosphate- and glucose-6-phosphate dehydrogenase, NAD-diaphorase and phosphorylase. Increased activity of OHBDH and LDH was found: 36,0 and 22,6% higher than in trauma and brain hemorrhage that served as control. These alterations seem to be connected with the increase of blood content of fatty acids, and lactate as a response to the catecholamine excess. Foci of an acute ischemia were found in the interventricular septum in 80% of cases in which phosphorylase was revealed. The appearance of the ischemic foci was obviously due to the coronary arteries contraction.
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PMID:[Histoenzymological characteristics of the myocardium in sudden cardiac death]. 405 12

The enzyme pattern of 13 cases of malignant fibrous histiocytoma (MFH) and 11 cases of myxofibrosarcoma (MFS), a malignant myxomatous soft tissue tumor of fibroblastic histiocytic origin, has been studied. 6 of the 13 MFHs were analyzed enzyme histochemically at the light microscopic level and 7 on the ultrastructural level; of the 11 MFSs 9 were analyzed enzyme histochemically at the light microscopic level and 2 on the ultrastructural level. Differences were observed in the subjectively estimated enzyme activity between low grade MFS and high grade MFS and MFH, and also between histiocyte-like and fibroblast-like tumor cells. Generally a strong reaction of oxidoreductase enzymes (NADH2-diaphorase, NADPH2-diaphorase, glucose-6-phosphate dehydrogenase) and hydrolytic enzymes (acid phosphatase and leucine aminopeptidase) was found in the high grade tumors and was usually higher in the histiocyte-like than in the fibroblast-like cells. Ultrastructurally acid phosphatase occurred predominantly in primary and secondary lysosomes and Golgi zones of the histiocyte-like cells. A strong reaction of alkaline phosphatase was found light microscopically in 2 of 5 MFHs and 5 of 9 MFSs. Ultrastructurally alkaline phosphatase was located along the cytoplasmic membrane of predominantly fibroblast-like cells in 3 of 7 MFHs and 1 of 2 MFSs. The results agree with the concept of two main cell types in MFH and MFS, fibroblasts and histiocytes.
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PMID:Enzyme histochemistry of malignant fibroblastic histiocytic tumors. A light and electron microscopic analysis. 608 56


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