Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q8NEX9 (reductase)
 26,410 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

NADPH-cytochrome c reductase (NADPH : ferricytochrome oxido-reductase, EC 1.6.2.4), the flavoprotein which mediates the NADPH-dependent reduction of cytochromes P-450 in adrenocortical microsomes, has been localized immunohistochemically at the light microscopic level in rat adrenal glands. Localization was achieved through the use of sheep antiserum produced against purified, trypsin-solubilized rat hepatic microsomal NADPH-cytochrome c reductase in both an unlabeled antibody peroxidase-antiperoxidase technique and an indirect fluorescent antibody method. The sheep antibody to rat hepatic microsomal NADPH-cytochrome c reductase concomitantly inhibited the NADPH-cytochrome c reductase and progesterone 21-hydroxylase activities catalyzed by isolated rat adrenal microsomes. When sections of rat adrenal glands were exposed to the reductase antiserum in both immunohistochemical procedures, positive staining for NADPH-cytochrome c reductase was observed in parenchymal cells of the three cortical zones but not in medullary chromaffin cells. The intensity of staining, however, was found to differ among the three cortical zones, with the most intense staining being found in the zona fasciculata and the least in the zona glomerulosa. The intensity of staining was also found to differ among cells within the zona fasciculata. These immunohistochemical observations demonstrate that microsomal NADPH-cytochrome c reductase is not distributed uniformly throughout the rat adrenal cortex.
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PMID:Immunohistochemical studies on electron transport proteins associated with cytochromes P-450 in steroidogenic tissues. II. Microsomal NADPH-cytochrome c reductase in the rat adrenal. 10 28

Cytochrome P450 in the mitochondria of the adrenal cortex functions in the monooxygenation reactions for the biosynthesis of various steroid hormones, such as cholesterol side chain cleavage, hydroxylation at 11 beta-position and that at 18-position of the steroid structure. The cytochrome is firmly associated with the mitochondrial membrane and therefore can be isolated only by the aid of ionic or non-ionic detergent. Recently, two cytochromes P450 each catalyzing a specified reaction have been purified to a homogeneous state, that is, P450scc having cholesterol side chain cleavage activity and P45011 beta having 11 beta-hydroxylation activity. The properties of these purified P450's as well as the other components of the monooxygenase system, adrenodoxin and adrenodoxin reductase, are, therefore, summarized and compared to those of P450 in the mitochondrial preparation in situ. Among many findings, both purified cytochromes P450 were revealed to be a low-spin type hemoprotein and their spin states were changed to a high-spin state by being complexed with the corresponding substrate. The binding of a substrate also facilitated the reduction of the cytochrome and appeared to increase the stability of the oxygenated form of cytochrome P450. These effects are important from the point of view that the primary role of the heme of cytochrome P450 is the activation of molecular oxygen. In addition, the results of our detailed kinetic studies on the transfer of electrons from adrenodoxin to cytochrome P450 in the reconstituted system have also been described. Finally, the topology of adrenodoxin and the reductase were shown to be on the inner mitochondrial membrane by a peroxidase-labeled antibody method.
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PMID:Cytochrome P450 in adrenocortical mitochondria. 22 25

The chromogen ABTS is the di-ammonium salt of 2,2'-azino-di[3-ethyl-benzthiazolin-sulfonic acid (6)] routinely used in the "glucose-oxidase assay" with the peroxidase (GOD-Perid method, Boehringer). 1. The specific property of ABTS to give a stable radical cation by oxidation with hydrogen peroxide in the presence of peroxidase was used to design a kinetic method, for enzyme-activity determinations. 2. The assay is suitable for the specific oxido-reductase using oxygen as acceptor, known also as "aerobic transhydrogenases" which are H2O2 formers (EC 1.-.3.-). 3. L-Amino acid: oxygen oxidoreductase (deaminating) (EC 1.4.3.2), was used throughout, being a representative model for such determinations.
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PMID:[A kinetic method for the determination of the activity of "aerobic transhydrogenases" (author's transl)]. 24 20

The zonal distribution of adrenodoxin and adrenodoxin reductase (EC 1.6.7.1) in the bovine adrenal cortex as well as their intracellular localization has been studied by the direct method of peroxidase-labelled antibody (Fab' or F(ab')2 fraction) technique. The results indicated that both proteins localized mainly in zonae fasciculata and reticularis whereas very few were present in the zona glomerulosa. Only parenchymal cells in the adrenal cortex were proved to contain both proteins. The intracellular localization of both adrenodoxin and the reductase was demonstrated to be exclusively on the inner membrane of mitochondria of these parenchymal cells by immunoelectron microscopy. The validity of the immunocytochemical method employed in this study to determine the fine localization of both proteins in the mitochondria as well as the significance of the zonal distribution in relation to the function of each individual zone is discussed.
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PMID:Immunohistochemical localization of adrenodoxin and adrenodoxin reductase in bovine adrenal cortex. 36 62

Lecithin and kephalin content in the microsomes and mitochondria of the rat liver, and also the activity of enzymatic and nonenzymatic systems of the phospholipid peroxidation showed a sharp change following 3,4-benzpyrene injection. Carcinogenesis is accompanied by significant changes in the lipid peroxides content and in the activity of the enzyme utilizing lipoperoxides (glutathion peroxidase, glutathion reductase). Accumulation of lipid peroxides in the rat liver in carcinogenesis was connected with disturbed balance of the generating systems and detoxication of lipid peroxides in the tumour is attributed to the high activity of the protective enzymatic systems and serves as a reflection of the adaptation mechanisms directed to the maintenance of a high pool of proliferating cells in the tumour.
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PMID:[Lipid peroxide metabolism in chemical carcinogenesis]. 42 80

The variation of the activities of glutathion peroxidase, glutathion reductase, glucose-6-phosphate dehydrogenase, as well as of the concentrations of lipid peroxides and -SH groups of nonproteic nature, was followed up in the hepatocyte of normal rats, of those with, streptozotocin-induced-diabetes, and of diabetic rats treated with thiazolidin carboxylic (ThCA) acid. Free peroxides and glutathion peroxidase were increased in the diabetic animals as against the normals, whereas glutathion reductase, glucose-6-phosphate dehydrogenase and the -SH groups of nonproteic nature had lower values. A return to normal of these parameters was noticed in the animals treated with ThCA.
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PMID:The effect of thiazolidin carboxylic acid (ThCA) on the redox equilibrium maintaining in the rat hepatocyte with streptozotocin-induced diabetes. 63 31

This paper reports a study of changes in red blood cell enzymes and some serum parameters during and after treatment of protein-calorie malnutrition. The red cell GSH levels were low during the crisis, together with the levels of GSSG:NADPH reductase, GSH:H2O2 peroxidase, aspartate aminotransferase and alanine aminotransferase. After treatment the levels of all these enzymes increased significantly to normal values. Of the serum parameters investigated, significant reduction in the activity of the enzymes cholinesterase, catecholamine oxidase, total proteins, albumin, urea and electrolytes were obvious, and returned to normal values after treatment. Ceruloplasmin activity remained low even after three weeks' treatment and could not be related to copper levels. The results are discussed in relation to anemia and liver damage that may accompany the syndrome.
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PMID:Protein-calorie malnutrition: a study of red blood cell and serum enzymes during and after crisis. 82 Apr 94

A 37-yr-old woman with nontoxic goiter is presented. The thyroid 131I uptake at 3 and 24 hr were, respectively, 77.1% and 81.4% dose. Thiocyanate discharged 65.5% of the accumulated 131I in 30 min. In vitro organification of iodine in the thyroid homogenate from the patient was impaired and it was restored to normal by the addition of H2O2, glucose, and glucose oxidase system, FAD, or reduced cytochrome b5. Riboflavin, FMN, oxidized cytochrome b5, oxidized or reduced cytochrome c, NAD(H), and NADP(H) were ineffective in the reaction. The microsomal NADH-cytochrome b5 reductase activity was definitely low in the patient's thyroid. It was augmented to a normal level by incubation of the microsomes with FAD for 30 min or more. The activities of thyroid peroxidase, G6-PD, 6-PGD, catalase, protease, and NADPH-cytochrome c reductase were within normal limits. The major thyroid protein was normal thyroglobulin which could be readily iodinated in the presence of H2O2 and horse radish peroxidase. These findings suggest the correlation of an iodide organification defect with a cytochrome b5 reductase deficiency. Administration of high doses of FAD led to the restoration of thyroidal iodide organification mechanism associated with an increased thyroid hormone production and to a marked decrease of the goiter. Riboflavin was given without effect even at a high dosage level. Consequently, it seems likely that the deficient cytochrome b5 reductase activity in this patient is due to a defect in the biosynthesis of FAD, the coenzyme of the reductase, from riboflavin.
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PMID:Deficient cytochrome b5 reductase activity in nontoxic goiter with iodide organification defect. 116 26

Subcellular distribution study of cytoplasmic organelles was performed on human polymorphonuclear leukocytes after homogenization in 0.34 molar sucrose by differential centrifugation and sucrose density gradient centrifugation of the homogenate. The whole homogenate and each fraction was assayed for nitroblue tetrazolium (NBT)-reductase with and without 1 mM potassium cyanide, and the distribution of this enzyme was compared to the distribution of lysozyme, peroxidase, beta-glucuronidase, and acid and alkaline phosphatase. Enzyme recovery was 97 per cent and ranged between 74 and 124 per cent. Latent activity of all enzymes except NBT-reductase, acid, and alkaline phosphatase was demonstrated by observing a four- to sixfold increase in activity after the addition of Triton-X 100. Maximal relative specific activity using either DPNH or without cyanide for NBT-reductase was found in the 100,000 x g differential centrifugation fraction and was concentrated in the less dense top fraction of the sucrose density gradient. The distribution pattern was similar to acid and alkaline phosphatase. In contrast, the maximal concentration of beta-glucuronidase and peroxidase was found in the heavier 7,200 x g granule fraction and in the more dense bottom fractions of the sucrose density gradient. Maximal lysozyme activity was concentrated in the 30,000 x g granule fraction and in the fractions located between the heaviest and lightest fractions of the sucrose density gradient. The lack of latent activity and the similarity of subcellular distribution of NBT-reductase to acid and alkaline phosphatase, two enzymes associated with microsomes and plasmalemal membranes in human polymorphonuclear leukocytes (PMN), indicates that NBT-reductase is also a nonlysosomal enzyme located in microsomes or in plasmalemal membranes. These findings support the previously described histochemical observations that initial reduction of NBT to formazan occurs on the PMN plasmalemal surface membrane at the point of particle attachment. In addition, they suggest that alteration of the surface membrane of the PMN by particle attachment or other surface forces may activate NBT-reductase, leading to an accumulation of formazan in the region of the altered membrane as the phagocytic vacuole is formed.
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PMID:Subcellular distribution of nitroblue tetrazolium reductase (NBT-R) in human polymorphonuclear leukocytes (PMN). 118 38

Activity of redox-enzymes of AA system and of catalase was measured in two near-isogenic tomato lines, respectively resistant and susceptible to Tobacco Mosaic Virus infection. AFR reductase, DHA reductase and catalase showed quite similar activities in both lines, whereas AA peroxidase activity in resistant plants was 75% higher than in susceptible ones, with Km values about 4-fold lower. These data suggest that hydrogen peroxide scavenging operated by AA peroxidase could play an important role in the development of biological defence mechanisms against pathogens.
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PMID:Ascorbate peroxidase activity in resistant and susceptible plants of Lycopersicon esculentum. 129 16


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