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  • 1
    Electronic Resource
    Electronic Resource
    Phospholipase D Activity of Rat Brain Neuronal Nuclei (1996)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 67 (1996), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Phospholipase D activity of rat brain neuronal nuclei, measured with exogenous phosphatidylcholine as substrate, was characterized. The measured activity of neuronal nuclei was at least 36-fold greater than the activity in glia nuclei. The pH optimum was 6.5, and unsaturated but not saturated fatty acids stimulated the enzyme. The optimal concentration of sodium oleate for stimulation of the enzyme activity was 1.2 mM in the presence of 0.75 mM phosphatidylcholine. This phospholipase D activity was cation independent. In the absence of NaF, used as a phosphatidic acid phosphatase inhibitor, the principal product was diglyceride; whereas in the presence of NaF, the principal product was phosphatidic acid. The phospholipase D, in addition to having hydrolytic activity, was able to catalyze a transphosphatidylation reaction. Maximum phosphatidylethanol formation was seen with 0.2–0.3 M ethanol. GTPγS, ATPγS, BeF2, AIF3, phosphatidic acid, and phosphatidylethanol inhibited the neuronal nuclei phospholipase D activity. The addition of the cytosolic fraction of brain, liver, kidney, spleen, and heart to the incubation mixtures resulted in inhibition of the phospholipase D activity. Phospholipase D activity was detectable in nuclei prepared from rat kidney, spleen, heart, and liver.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1996.67020760.x
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  • 2
    Electronic Resource
    Electronic Resource
    Phosphatidylethanol Formation via Transphosphatidylation by Rat Brain Synaptosomal Phospholipase D (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 48 (1987), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Phosphatidylethanol (Peth) formation catalyzed by the transphosphatidylation activity of phospholipase D was demonstrated to occur in a rat brain synaptosomal enriched preparation. The optimal pH was determined to be 6.5, and the optimal ethanol concentration was determined to be 0.3–0.4 M with an apparent Km of 0.2 M. Peth formation was barely detectable in the absence of an appropriate activator and several unsaturated fatty acids were found to be effective activators. The concentrations of oleic acid required for maximum activation varied with the concentration of exogenous phosphatidylcholine present in the incubation mixtures. All detergents tested were significantly less active than the unsaturated fatty acids and divalent ions were not required for Peth formation. Phosphatidylcholine was the most effective phosphatidyl donor of the phospho-lipids tested. Peth forming activity was greatest in the synap-tic membrane fraction of the various brain subfractions examined. The 12,000 g-100,000 g paniculate fraction of lung, heart, and adipose tissue had activities similar to that of brain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1987.tb05707.x
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  • 3
    Electronic Resource
    Electronic Resource
    Modulation of the Serine Base Exchange Enzyme Activity of Rat Brain Membranes by Amphiphilic Cations and Amphiphilic Anions (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 60 (1993), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The biosynthesis of phosphatidylserine in mammalian tissues is catalyzed by the serine base exchange enzyme. The activity of this membrane-bound enzyme can be manipulated by amphiphiles. Amphiphilic cations, such as oleylamine, W-7, chlorpromazine, and didodecyldimethylamine, stimulate the serine base exchange activity. Amphiphilic anions, such as bis(2-ethylhexyl) hydrogen phosphate and cholesterol sulfate, inhibit the serine base exchange activity. These effects are more pronounced at pH 7.0 than at the pH optimum of 8.5 for this enzyme. Both the stimulators and the inhibitors alter the Vmax values without changing the Km value for serine, suggesting that their mechanism of action is related to interactions of the membrane-bound cosubstrate, phosphatidylethanolamine, with the membrane-bound enzyme. The optimal concentration of stimulator varies with the amount of membrane protein present; however, supraoptimal concentrations cause inhibitions. It is proposed that the amphiphilic cations enhance the interaction of the phosphorylethanolamine moiety of the membrane-bound cosubstrate with the enzyme and the amphiphilic anions interfere with such an interaction. Some of the pharmacological properties of these amphiphilic cations, employed clinically as antidepressants, may be mediated by modulation of the serine base exchange enzyme activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1993.tb03281.x
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  • 4
    Electronic Resource
    Electronic Resource
    Effect of Modification of Membrane Phospholipid Composition on Phospholipid Methylation in Aggregating Cell Culture (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 46 (1986), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The effect of the presence of nitrogenous bases in the growth medium of fetal rat brain aggregating cell cultures was investigated. The presence of either N-dimethylethanolamine (MME) or N,N-dimethylethanolamine (DME) in the growth medium resulted in significant increase of the corresponding phospholipid, phosphatidyl-N-monomethylethanolamine (PMME) or phosphatidyl-N,N-dimethylethanolamine (PDME). They represented 28% and 32% of the total phospholipids, respectively. The presence of the new phospholipids was accompanied by a significant decrease of phosphatidyl ethanolamine (PE) and phosphatidylcholine (PC). Cells grown in the presence of ethanolamine or choline had only barely detectable amounts of PMME and PDME. Intact cells previously grown with the bases were incubated with [methyl-3H]methionine. Incubation of cells previously grown in presence of the bases MME and DME resulted in a marked increase of radioactivity in the corresponding phospholipids possessing one additional methyl group, PDME and PC respectively. The incorporation of S-adenosyl[methyl−3H]methionine (AdoMet) was examined in cell homogenates incubated in presence or absence of either PMME or PDME acceptors. The addition of these exogenous phospholipids caused a three or fourfold stimulation of radioactivity incorporated into the total phospholipids of cells grown in the absence of nitrogen bases. The cells grown in presence of either MME or DME in the culture medium did not show an increased incorporation of methyl groups from AdoMet into the total phospholipids after addition of exogenous acceptors. This work suggests that MME and DME incorporated into the corresponding phospholipids function as effective substrates for phospholipid-N-methylation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1986.tb08505.x
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  • 5
    Electronic Resource
    Electronic Resource
    Synaptosomal Phospholipase D Potential Role in Providing Choline for Acetylcholine Synthesis (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 45 (1985), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The phospholipase D of the rat brain synaptic membrane possesses the highest activity of this enzyme of any mammalian tissue examined. The synaptic phospholipase D activity is latent and barely detectable in the absence of 4 mM sodium oleate. Several other fatty acids were either less effective or ineffective as stimulators of activity compared to this monounsaturated fatty acid. The activity was decreased by hemicholinium-3, an inhibitor of choline uptake and slightly activated by neostigmine, an acetylcholinesterase inhibitor. Incubation of synaptosomes in the presence of sodium oleate and acetyl-coenzyme A resulted in the formation of a product chromatographing with acetylcholine. Acetylcholine formation was nearly undetectable in the absence of sodium oleate or acetyl-coenzyme A. These results implicate synaptosomal phospholipase D in releasing choline from phosphatidylcholine for acetylcholine formation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1985.tb07229.x
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  • 6
    Electronic Resource
    Electronic Resource
    Amyloid β Protein (25–35) Stimulation of Phospholipase C in LA-N-2 Cells (1997)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 69 (1997), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The amyloid β protein (25–35) stimulated appearance of 3H-inositol phosphates from [3H]inositol-prelabeled LA-N-2 cells was investigated. This stimulation was unaltered by extra- and intracellular calcium chelators in a calcium-free medium or by several protein kinase inhibitors. This phospholipase C stimulation by amyloid β protein appeared to be pertussis toxin sensitive. It is possible that this phospholipase C stimulation by amyloid β protein is a receptor-mediated process. This possibility is based on two related observations. The stimulation is ablated by the presence of conventional antagonists for metabotropic, adrenergic, and bombesin agonists. The IC50 values were 12 µM for propranolol, 15 µM for AP-3, and 25 nM for [Tyr4,d-Phe12]bombesin. Additional support comes from results of densensitization and resensitization experiments. Amyloid β protein stimulation of phospholipase C was absent from LA-N-2 cells previously treated with norepinephrine, trans-1-amino-1,3-cyclopentanedicarboxylic acid (t-ACPD), bombesin, or amyloid β peptide. In a similar manner, LA-N-2 cells previously treated with amyloid β protein were no longer responsive to norepinephrine, t-ACPD, or bombesin. The responsiveness to amyloid β protein returned, subsequent to a period of resensitization for the individual agonists. It is suggested that this observed amyloid β protein stimulation of phospholipase C may be responsible for the elevated quantity of inositol seen in the brains of Alzheimer's disease patients.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1997.69010252.x
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  • 7
    Electronic Resource
    Electronic Resource
    Hydrolysis of Endogenous Phospholipids by Rat Brain Microsomes (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 44 (1985), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Phosphatidylcholine of rat brain microsomes was labeled in vivo by intracerebral injection of either [3H]oleic acid or [methyl-3H]choline chloride. These labeled microsomes served both as the enzyme source as well as a source of endogenously labeled substrate. Phospholipase D (PLD) activity was detected with these particles only in the presence of exogenous oleate, its activator. Ca2+ and the ionophore A 23187 inhibit PLD activity of oleate-labeled microsomes. In oleate-labeled particles, besides phosphatidic acid the product of PLD action radioactivity was also detected in diglyceride as a result of resident phosphatidate phosphohydrolase, which hydrolyzed the phosphatidic acid. The phosphatidate phosphohydrolase could not be completely inhibited by KF and propranolol. The release of endogenous fatty acids from labeled phospholipid by a mellitin-stimulated phospholipase A2 also present in these particulates produced minimal stimulation of endogenous PLD. Phosphatidylcholine (PC) and phosphatidylethanolamine (PE) are hydrolyzed by 50% in the presence of mellitin and 90% of the radioactivity was found in the lyso-compounds. Mellitin and oleate together reduced the radioactivity found in lyso-PC and increased that in lyso-PE.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1985.tb07125.x
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  • 8
    Electronic Resource
    Electronic Resource
    Presence of Phospholipid-N-Methyltransferases and Base-Exchange Enzymes in Rat Central Nervous System Axolemma-Enriched Fractions (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 43 (1984), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Rat CNS myelinated axons were fractionated by sucrose density gradient centrifugation with a zonal rotor. Fraction VI, obtained at 28–30% sucrose, appeared, on the basis of the presence of related marker enzymes, to be enriched in axolemma. Phospholipid-N-methyltransferases (PMTs) and base-exchange enzymes were associated with fraction VI. PMT activity was significantly stimulated by the addition of either phosphatidylmonomethylethanolamine or phosphatidyldimethylethanolamine but the PMT activity of the homogenate or the myelinated axons was unresponsive. Recoveries of the ethanolamine, serine, and choline base-exchange activities were 14.4%, 13.8%, and 3.4%, respectively, of that present in the myelinated axons. The myelin-rich fraction obtained simultaneously seems contaminated with other membrane fractions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1984.tb12838.x
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  • 9
    Electronic Resource
    Electronic Resource
    Human Brain Cerebroside β-Galactosidase: Deficiency of Transgalactosidic Activity in Krabbe's Disease (1980)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 34 (1980), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Under experimental conditions optimal for the assay of D-galactosyl-N-acylsphingosine galactohydrolase (EC 3.2.1.46) activity, homog-enates of neurologically normal human brain tissue could transfer galactose from galactosyl ceramide (gal-cer), lactosyl ceramide (lac-cer), 4-methylumbelliferyl- β-galactoside (4-MU-gal), or p-nitrophenyl- β-galactoside (PNP-gal) to [1-14C]oleoyl sphingosine, but homogenates of brain tissue from patients with Krabbe's disease lacked this ability. The rate of hydrolysis of ganglioside GM1 and to a lesser extent, of PNP-gal by homogenates of Krabbe's brain tissue was also decreased. Activity of PNP- β-galactosidase in normal brain tissue, like that of cerebroside β-galactosidase from the same source, was considerably more heat-stable than the activity of either 4-MU- β-galactosidase or the predominant GM1β-D-galactosidase (EC 3.2.1.23). Lac-cer and GM1, as well as 4-MU-gal and PNP-gal, were competitive inhibitors of human-brain cerebroside β-galactosidase. These findings confirm the ability of mammalian cerebroside β-galactosidase to catalyze a transgalactosylation reaction and provide additional information on the substrate specificity of human brain cerebroside β-galactosidase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1980.tb04639.x
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  • 10
    Electronic Resource
    Electronic Resource
    HYDROLYTIC AND TRANSGLUCOLYTIC ACTIVITIES OF A PARTIALLY PURIFIED CALF BRAIN β-GLUCOSIDASE (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 27 (1976), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Properties of both a transglucosylation reaction and the hydrolytic activity of a partially purified calf brain β-glucosidase were investigated. Sodium taurocholate and a ‘Gaucher factor’ stimulated both activities. A purified ‘stimulatory’ factor from human liver did not appear to significantly affect the hydrolytic activity towards either 4-methylumbelliferone-β-d-glucoside or [14C]glucosyl ceramide. Several compounds were found to be competitive inhibitors of the hydrolytic activity, conduritol B epoxide and norjirimycin being the most effective. Glucosyl ceramide hydrolysis was more sensitive to inhibition by p-chloromercuribenzenesulfonate than 4-methylumbelliferone-β-glucoside cleavage. The partially purified enzyme preparation catalyzed the formation of [14C]glucosyl ceramide with N-[14C]oleoyl sphingosine as the acceptor and several β-glucosides as the donor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1976.tb05159.x
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