Distribution of six transplasma membrane NADH-dehydrogenases in rat brain tissue

Yue, Yong; Dreyer, Jean-Luc

doi:10.1016/0165-3806(95)00124-v

Cited by 8 publications

(2 citation statements)

References 22 publications

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“…Noteworthy, rat brain regionalization found in our work for Cb 5 R3 and Cb 5 resembles the reported distribution of NADH-dependent dehydrogenases with transplasma membrane oxidoreductase activity 42 . Consistently, using fluorescence resonance energy transfer imaging we have found that a large part of Cb 5 R3 in the cerebellum cortex was regionalized in close proximity to the neuronal plasma membrane lipid rafts labeled with cholera toxin B 38 .…”

Section: Regionalization Of Cb 5 R3 and Cb 5 In The Brainsupporting

confidence: 55%

Biochemical and anatomical basis of brain dysfunctions caused by cytochrome b5 reductase deficiency or dysregulation

Samhan-Arias¹,

López‐Sánchez²,

Marques‐da‐Silva³

et al. 2016

J Neurol Neuromedicine

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Cytochrome b 5 reductase (Cb 5 R) and cytochrome b 5 (Cb 5 ) are coupled redox systems with a high potential as biomarkers of health and disease in the brain because they regulate metabolic pathways that are essential to maintain normal neuronal function, like lipid biosynthesis, steroid and xenobiotics metabolism, neuronal bioenergetics and production of reactive oxygen species. Mutations of the Cb 5 R reported in humans produce recessive congenital methemoglobinemia of type II, a disease with severe clinical neurological dysfunctions. The isoform 3 of Cb 5 R (Cb 5 R3) and Cb 5 are highly expressed in pyramidal neurons of the primary and secondary motor areas of frontoparietal cerebral cortex, hippocampus, vestibular, reticular and motor nuclei of the cerebellum and brain stem, and also in Purkinje and granule neurons of the cerebellum cortex. These brain areas are highly prone to undergo oxidative stress-induced neurodegeneration and their functional impairment can account for neurological deficits reported in type II congenital methemoglobinemia. R).The redox system Cb 5 /Cb 5 R acts as an electron carrier coupled to cytosolic NADH consumption in endoplasmic reticulum, mitochondria and plasma membrane of mammalian cells. Cb 5 is a pleiotropic co-factor of multiple enzymes and redox chains that play critical roles for normal function of healthy mammalian organisms, and it is largely reduced by the NADH-dependent Cb 5 R activity (reviewed in Samhan-Arias and Gutierrez-Merino 1 ).Neurons have an extremely high dependence on lipid metabolism to make new synaptic connections and also for synaptic plasticity and activity. In mammalian cells Cb 5 and Cb 5 R modulate palmitoilCoA elongation and desaturation and cholesterol synthesis 1 , and also the dihydroceramide:sphinganine C-4 hydroxylase 2 . Moreover, reduced Cb 5 has been shown to activate sialic acid metabolism 3 , a metabolite required for the synthesis of gangliosides, a major family of brain lipids. In addition, Cb 5 is also a cofactor of NADPHdependent cytochrome P450 monooxygenation reactions involved in steroid and xenobiotics metabolism 4,5 . Owing to the relevance of oxidative stress in neurodegenerative processes, it is to be noted that the potentiation by Cb 5 of the metabolism through cytochrome P450s decreases the rate of collateral reactions releasing non-

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Section: Regionalization Of Cb 5 R3 and Cb 5 In The Brainsupporting

confidence: 55%

Biochemical and anatomical basis of brain dysfunctions caused by cytochrome b5 reductase deficiency or dysregulation

Samhan-Arias¹,

López‐Sánchez²,

Marques‐da‐Silva³

et al. 2016

J Neurol Neuromedicine

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“…Whether this is also the case in other dehydrogenases has not been studied (Medina et al 1994). NADH-OR in synaptic membranes has been studied for malay years by Dreyer and coworkers (Yong and Dreyer 1995). A purification protocol corresponding to this enzyme activity was recently presented.…”

Section: Nadh:acceptor Oxidoreductasementioning

confidence: 99%

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

Goldenberg

1998

Protoplasma

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Summary.Despite a large bodyof 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 and bs~a,

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Regionalization of Plasma Membrane-Bound Flavoproteins of Cerebellar Granule Neurons in Culture by Fluorescence Energy Transfer Imaging

et al. 2006

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Flavoproteins are components of plasma membrane redox chains, which have been suggested to play major roles in neuronal activity and survival. We found that the red/orange autofluorescence of mature primary cultures of cerebellar granule neurons (8-9 days in vitro) was largely quenched by millimolar concentrations of dithionite added to the extracellular medium, and pointed out that nearly 50% of this autofluorescence was due to plasma membrane-bound flavoproteins. We report in this work that the lipophilic neuronal plasma membrane markers N-(3-triethylammoniumpropyl)-4-(4-(4-(diethylamino)phenyl)butadienyl)-pyridinium dibromide (RH-414) and N-(3-triethylammoniumpropyl)-4-(6-(4-(diethylamino)phenyl)hexatrienyl)pyridinium dibromide (FM4-64) can form fluorescence energy transfer donor-acceptor pairs with flavoproteins with calculated R (0) values between 3.7 and 4.2 nm. The quantification of the efficiency of fluorescence energy transfer with different concentrations of acceptor dyes has been worked out with re-suspended neurons. Using quantitative images of the neurons in culture, acquired with a CCD camera attached to an epifluorescence microscope, regionalization of the plasma membrane-bound flavoproteins of cerebellar granule neurons has been achieved from the quenching by dithionite of the fluorescence of the acceptor dye. The results unraveled that plasma membrane-bound flavoproteins are largely enriched in interneuronal contact sites forming clusters of 0.5-1 microm diameter size, which appears largely regionalized in the neuron's cell body.

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Distribution of six transplasma membrane NADH-dehydrogenases in rat brain tissue

Cited by 8 publications

References 22 publications

Biochemical and anatomical basis of brain dysfunctions caused by cytochrome b5 reductase deficiency or dysregulation

Biochemical and anatomical basis of brain dysfunctions caused by cytochrome b5 reductase deficiency or dysregulation

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

Regionalization of Plasma Membrane-Bound Flavoproteins of Cerebellar Granule Neurons in Culture by Fluorescence Energy Transfer Imaging

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