0000000000123249

AUTHOR

Ira Böckmann

showing 2 related works from this author

Modulation of neuronal phospholipase D activity under depolarizing conditions

1999

Neuronal phospholipase D (PLD) activity was hypothesized to be involved in vesicle trafficking and endocytosis and, possibly, transmitter release. We here report that prolonged depolarization of rat hippocampal slices by potassium chloride (KCl) or 4-aminopyridine inhibited PLD activity. Similarly, PLD activity in rat cortical synaptosomes was significantly inhibited by depolarizing agents including veratridine and ouabain. Inhibition of calcium/calmodulin kinase II (CaMKII) which positively modulates synaptosomal PLD activity [Sarri et al. (1998) FEBS Lett. 440, 287-290] by KN-62 caused a further reduction of PLD activity in depolarized synaptosomes. Depolarization-induced inhibition of PL…

Phosphatidylinositol 45-DiphosphateTime FactorsBiophysicschemistry.chemical_elementCalciumHippocampusBiochemistryOuabainMembrane PotentialsPotassium Chloridechemistry.chemical_compoundStructural BiologyCa2+/calmodulin-dependent protein kinaseSynaptosomeElectrochemistryPhospholipase DGeneticsmedicineAnimalsPhospholipase D activityEnzyme InhibitorsRats WistarMolecular BiologyProtein Kinase CProtein Synthesis InhibitorsSynaptosomePhospholipase DCalcium/calmodulin-dependent protein kinase IINeomycinDepolarizationPhosphatidylinositol-45-bisphosphateCell BiologyRatsCell biologyenzymes and coenzymes (carbohydrates)chemistryCalcium-Calmodulin-Dependent Protein KinasesDepolarizationlipids (amino acids peptides and proteins)VeratridineSynaptosomesmedicine.drugFEBS Letters
researchProduct

Regulation of phospholipase D activity in synaptosomes permeabilized with Staphylococcus aureus alpha-toxin.

1998

In order to investigate the regulation of presynaptic phospholipase D (PLD) activity by calcium and G proteins, we established a permeabilization procedure for rat cortical synaptosomes using Staphylococcus aureus alpha-toxin (30-100 microg/ml). In permeabilized synaptosomes, PLD activity was significantly stimulated when the concentration of free calcium was increased from 0.1 microM to 1 microM. This activation was inhibited in the presence of KN-62 (1 microM), an inhibitor of calcium/calmodulin-dependent kinase II (CaMKII), but not by the protein kinase C inhibitor, Ro 31-8220 (1-10 microM). Synaptosomal PLD activity was also stimulated in the presence of 1 microM GTPgammaS. When Rho pro…

MaleStaphylococcus aureusCell Membrane PermeabilityG proteinBacterial ToxinsBiophysicschemistry.chemical_elementCalciumBiologyIn Vitro TechniquesBiochemistryClostridium difficile toxin Bchemistry.chemical_compoundHemolysin ProteinsStructural BiologyStaphylococcus aureus α-toxinCa2+/calmodulin-dependent protein kinaseSynaptosomeGeneticsPhospholipase DPhospholipase D activityAnimalsRats WistarMolecular BiologyProtein kinase CSynaptosomePhospholipase DRho proteinCalcium/calmodulin-dependent protein kinase IICell BiologyBrefeldin AMolecular biologyRatsEnzyme Activationenzymes and coenzymes (carbohydrates)BiochemistrychemistryGuanosine 5'-O-(3-Thiotriphosphate)lipids (amino acids peptides and proteins)CalciumSynaptosomesFEBS letters
researchProduct