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Trans-plasma membrane electron transport: A cellular assay for NADH- and NADPH-oxidase based on extracellular, superoxide-mediated reduction of the sulfonated tetrazolium salt WST-1

The cantharidin-induced oxidative burst in tobacco BY-2 cell suspension cultures

Oxidative burst and electrolyte leakage induced by sulfhydryl blockers and by membrane permeabilizing reagents in different organs ofEgeria densa

Contribution of a plasma membrane redox system to the superoxide production by wheat root cells

Ubiquinol regeneration by plasma membrane ubiquinone reductase

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Electron spin resonance study on the formation of ascorbate free radical from ascorbate: The effect of dehydroascorbic acid and ferricyanide

Antioxidant defences of the apoplast

Effect of some electron donors and acceptors on redox capacity and simultaneous net H+/K+ fluxes by aeroponic sunflower seedling roots: Evidence for a CN−-resistant redox chain accessible to nonpermeative redox compounds

The induction of the “turbo reductase” is inhibited by cycloheximide, cordycepin and ethylene inhibitors in Fe-deficient cucumber (Cucumis sativus L.) plants

Changes in sugar beet leaf plasma membrane Fe(III)-chelate reductase activities mediated by Fe-deficiency, assay buffer composition, anaerobiosis and the presence of flavins

Plasma membrane redox system activity in tumour cell lines of mammary origins with different proliferation rates

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Molecular biology of plasma membrane redox enzymes: A survey of current knowledge

Content Provider	Springer Nature Link
Author	Goldenberg, H.
Copyright Year	1998
Abstract	Despite a large body of evidence for enzymatic activities and physiological functions of plasma membrane redox function, few of these enzymes have been characterized in terms of molecular biology. Examples for these with at least some molecular data up to complete sequences, membrane topology and binding sites for substrates and coenzymes or prosthetic groups are NADH-ferricyanide reductase of Ehrlich ascites membranes, NADH-coenzyme Q reductase of liver, NADH oxidase ectoenzyme of liver and HeLa (and possibly other) cells, protein disulfide isomerase which is widespread, and relatives thereof, as well as cytochromes P-450 andb 558, NADPH oxidase of fat and thyroid cells and fat cell amine oxidase. Ferricyanide reductase and coenzyme O reductase may be identical, but NADH oxidase ectoenzyme is distinct and possibly functions also as a disulfide and a copper reductase. On the other hand, the plasma-membrane-located protein disulfide isomerase (PDI), despite its similar enzymatic activity, is completely different from the ectooxidase. The latter is shed from the membrane into the surrounding medium by proteolysis, whereas PDI is not an integral membrane protein and is secreted intact. Another disulfide reductase has been demonstrated in THP-1 cells, which again is totally different from the former two. It turns out that enzymatic activities are insufficient to describe redox enzymes. Special forms of cytochrome P-450 can be induced to expression at the cell membrane of liver, where they are transported by the cytoskeleton-associated secretory pathway. Why some isoforms are expressed at the surface and some are not is not yet clear. Cytochromeb 558, the flavocytochrome of neutrophils, is described in other cells too, but there are different isoforms, which are genetically distinct. A relative has also been identified in duodenal cells, where it functions as a ferric reductase involved in iron absorption. NADPH oxidase of fat cells has very similar properties, but the identity is unproved, whereas thyroid oxidase is a non-heme protein which is calcium-sensitive and does not need assembly of subunits for activation. Finally, fat cell membranes also possess a quinone-containing amine-oxidase which may be involved in signaling of glucose-transport regulation, as it is also found in GLUT4-containing vesicles. However, the physiological connection has yet to be demonstrated.
Starting Page	3
Ending Page	9
Page Count	7
File Format	PDF
ISSN	0033183X
Journal	Protoplasma
Volume Number	205
Issue Number	1-4
e-ISSN	16156102
Language	English
Publisher	Springer-Verlag
Publisher Date	1998-01-01
Publisher Place	Vienna
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Amine oxidase Cytochrome P-450 NADH:acceptor oxidoreductase NADH oxidase NADPH oxidase Protein disulfide isomerase Cell Biology Plant Sciences Zoology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Plant Science Medicine

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Trans-plasma membrane electron transport: A cellular assay for NADH- and NADPH-oxidase based on extracellular, superoxide-mediated reduction of the sulfonated tetrazolium salt WST-1

Comparison of the redox activities in plasma membranes from roots and shoots of etiolated bean seedlings

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Superoxide generation of phagocytes and nonphagocytic cells

Transcriptional regulation of rat liver epoxide hydratase, NADPH-Cytochrome P-450 oxidoreductase, and cytochrome P-450b genes by phenobarbital.

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Molecular biology of plasma membrane redox enzymes: A survey of current knowledge