Modulation of phospholipases A₂ and C activities against dilauroylphosphorylcholine in mixed monolayers with semisynthetic derivatives of ganglioside and sphingosine

References

• Hannun Y. A., Bell R. M. Functions of sphingolipids and sphingolipid breakdown products in cellular regulation. Science 1989; 243: 500–507
   PubMed Web of Science ®Google Scholar
• Nishizuka Y. Intracellular signalling by hydrolysis of phospholipids and activation of protein kinase C. Science 1992; 258: 607–613
   PubMed Web of Science ®Google Scholar
• Kolesnick R. N. Sphingomyelin and derivatives as cellular signals. Progress in Lipid Research 1991; 30: 1–38
   PubMed Web of Science ®Google Scholar
• Vaccarino F., Guidotti A., Costa E. Ganglioside inhibition of glutamate-mediated protein kinase C translocation in primary cultures of cerebellar neurons. Proceedings of the National Academy of Sciences, USA 1987; 84: 8707–8711
   PubMed Web of Science ®Google Scholar
• Hakomori S. bifunctional role of glycosphingolipids. Modulators for transmembrane signalling anbd mediators for cellular interactions. Journal of Biological Chemistry 1990; 265: 18713–18716
   PubMed Web of Science ®Google Scholar
• Manev H, Favaron M., Vicini S., Guidotti A., Costa E. Glutamate-induced neuronal death in primary cultures of cerebellar granule cells: protection by synthetic derivatives of endogenous sphingolipids. Journal of Pharmacology and Experimental Therapeutics 1990; 252: 419–427
   PubMed Web of Science ®Google Scholar
• Kreuter D., Kim J. Y. H., Goldenring J. R., Rasmussen H., Ukomadu C., DeLorenzo R. J., Yu R. K. Regulation of protein kinase C activity by gangliosides. Journal of Biological Chemistry 1987; 262: 1633–1637
   Google Scholar
• Yates A. J., Walters J. C., Wood C. L., Johnson J. D. Ganglioside modulation of cyclic AMP-dependent protein kinase and cyclic nucleotide phosphodiesterase in vitro. Journal of Neurochemistry 1989; 53: 162–167
   PubMed Web of Science ®Google Scholar
• Farooqui A. A., Hirashima Y., Horrocks L. A. Brain phospholipases and their role in signal transduction. Advances in Experimental Medicine and Biology, N. G. Bazan, M. G. Murphy, G. Toffano. Plenum, New York 1992; Vol. 318: 11–25
   Google Scholar
• van den Bosch H. Intracellular phospholipases A. Biochimica et Biophysica Acta 1980; 604: 191–246
   PubMed Web of Science ®Google Scholar
• van den Bosch H., de Jong J. G. N., Aarman A. J. Phospholipase A2 from rat liver mitochondria. Methods in Enzymology, E. A. Dennis. Academic, San Diego 1991; Vol. 197: 365–373
   Google Scholar
• Tojo H., Ono T., Okamoto M. Spleen phospholipases A2. Methods in Enzymology, E. A. Dennis. Academic, San Diego 1991; Vol. 197: 390–399
   Google Scholar
• Dennis E. A., Rhe S. G., Billah M. B., Hannun Y. A. Role of phospholipases in generating lipid second messengers in signal transduction. FASEB Journal 1991; 5: 2068–2077
   PubMed Web of Science ®Google Scholar
• Berridge M. J. Inositol triphosphate and diacylglycerol: two interacting second messengers. Annual Review of Biochemistry 1987; 56: 159–193
   PubMed Web of Science ®Google Scholar
• Kikkawa U., Nishizuka Y. The role of protein kinase C in membrane signalling. Annual Review of Cell Biology 1986; 2: 149–178
   PubMedGoogle Scholar
• Nicoletti F., Meek J. L., Iadarola J. J., Chuang D. L. M., Roth B. L., Costa E. Coupling of inositol phospholipid metabolism with excitatory amino acid recognition sites in rat hippocampus. Journal of Neurochemistry 1986; 46: 40–46
   Google Scholar
• Lazarewicz J. W., Salinska E., Wroblewski J. T. NMDA receptor-mediated arachidonic acid release in neurons: role in signal transduction and pathological aspects. Advances in Experimental Medicine and Biology. Plenum, New York 1992; Vol. 318: 73–89
   Google Scholar
• Zeitler P., Wu Y. Q., Handwerger S. Melitin stimulates phosphoinositide hydrolysis and placental lactogen release: arachidonic acid as a link between phospholipase A2 and phospholipase C signal-transduction pathways. Life Sciences 1991; 48: 2089–2095
   Google Scholar
• Jain M. K., Berg O. The kinetic of interfacial catalysis by PLA2 and regualtion of interfacial activation: hopping versus scooting. Biochimica et Biophysica Acta 1989; 1002: 127–156
   PubMed Web of Science ®Google Scholar
• Ransac S., Moreau H., Rivière C., Verger R. Monolayer technique for studying phospholipase kinetics. Methods in Enzymology, E. A. Dennis. Academic, San Diego 1991; Vol. 197: 49–65
   Google Scholar
• Grainger D. W., Reichert A., Ringsdorf H., Salesse C. Hydrolytic action of phospholipase A2 in monolayers in the phase transition region: direct observation of enzyme domain formation using fluorescence microscopy. Biochimica et Biophysica Acta 1990; 1023: 365–379
   Google Scholar
• Bell J. D., Biltonen R. L. Activation of phospholipase A2 on lipid bilayers. Methods in Enzymology, E. A. Dennis. Academic, San Diego 1991; Vol. 197: 249–258
   Google Scholar
• Hirasawa K., Irvine R. F., Dawson R. M. C. The hydrolysis of phosphatidyl inositol monolayers at an air-water interface by the calcium-ion dependent phosphatidyl inositol phosphodiesterase of pig brain. Biochemical Journal 1981; 193: 607–614
   Google Scholar
• Quinn P. J., Barenholz Y. A comparison of the activity of phosphatidyl inositol phosphodiesterase against substrate in dispersions and as monolayers at the air-water interphase. Biochemical Journal 1975; 149: 199–208
   PubMed Web of Science ®Google Scholar
• El-Sayed M. Y., De Bose Ch., Coury L. A., Roberts M. F. Sensitivity of phospholipase C (Bacillus cereus) activity to phosphatidyl choline structural modifications. Biochimica et Biophysica Acta 1985; 837: 325–335
   PubMed Web of Science ®Google Scholar
• Tompkins T. A., Moscarello M. A. A 57-kDa phosphatidyl inositol-specific phospholipase C from bovine brain. Journal of Biological Chemistry 1991; 266: 4228–4236
   Google Scholar
• Rebecchi M., Boguslavsky V., Boguslavsky L., McLaughlin S. Phosphoinositide-specific phospholipase C-δ1. Effect of monolayer surface pressure and electrostatic surface potentials on activity. Biochemistry 1992; 31: 12748–12753
   PubMedGoogle Scholar
• Bianco I. D., Fidelio G. C., Maggio B. Modulation of phospholipase A2 activity by neutral and anionic glycosphingolipids in monolayers. Biochemical Journal 1989; 258: 95–99
   Google Scholar
• Bianco I. D., Fidelio G. D., Maggio B. Effect of sulfatide and gangliosides on phospholipase C and phospholipase A2 activity. A monolayer study. Biochimica et Biophysica Acta 1990; 1026: 179–185
   Google Scholar
• Bianco I. D., Fidelio G. D., Yu R. K., Maggio B. Degradation of dilauroylphosphatidylcholine by phospholipase A2 in monolayers containing glycosphingolipids. Biochemistry 1991; 30: 1709–1714
   Google Scholar
• Bianco I. D., Fidelio G. D., Yu R. K., Maggio B. Concerted modulation by myelin basic protein and sulfatide of the activity of phospholipase A2 against phospholipid monolayers. Biochemistry 1992; 31: 2636–2642
   Google Scholar
• Franson R. C., Harris L. K., Ghosh S. S., Rosenthal M. D. Sphingolipid metabolism and signal transduction: inhibition of in vitro phospholipase activity by sphingosine. Biochimica et Biophysica Acta 1992; 1136: 169–174
   Google Scholar
• Correa S. G., Bianco I. D., Riera C. M., Fidelio G. D. Anti-inflammatory effect of gangliosides in the rat. European Journal of Pharmacology 1991; 199: 93–98
   Google Scholar
• Perillo M. A., Polo A., Guidotti A., Costa E., Maggio B. Molecular parameters of semisynthetic derivatives of gangliosides and sphingosine in monolayers at the air-water interface. Chemistry and Physics of Lipids 1993; 65: 225–238
   Google Scholar
• Jain M. K., Yu B. Z., Kozubek A. Binding of PLA2 to zwitterionic bilayers is promoted by lateral segregation of anionic amphiphiles. Biochimica et Biophysica Acta 1989; 980: 23–32
   Google Scholar
• Bianco I. D., Maggio B. Interactions of neural and anionic glycosphingolipids with dilaurolphosphatidylcholine and dilauroylphosphatidic acid in mixed monolayers. Colloids and Surfaces 1989; 35: 97–99
   Google Scholar
• Yokoyama S., Kezdy F. J. Monolayers of long chain lecithin at the air-water interface and their hydrolysis by PLA2. Journal of Biological Chemistry 1991; 266: 4303–4308
   Google Scholar
• Maggio B., Bianco I. D., Montich G. G., Fidelio G. D., Yu R. K. Regulation by gangliosides and sulfatides of phospholipase A2 activity against dipalmitoyl- and dilauroylphosphatidylcholine in small unilamellar bilayer vesicles and mixed monolayers. Biochimica et Biophysica Acta 1994, (in press)
   Google Scholar
• Pattus F., Slotboom A. J., de Haas G. H. Regulation of phospholipase A2 activity by the lipid-water interface: a monolayer approach. Biochemistry 1979; 18: 2691–2697
   Google Scholar
• Bell J. D., Biltonen R. L. Molecular details of the activation of soluble phospholipase A2 on lipid bilayers. Journal of Biological Chemistry 1992; 267: 11046–11056
   Google Scholar
• Volwerk J. J., Jost P. C., de Haas G. H., Griffith O. H. Activation of porcine pancreatic phospholipase A2 by the presence of negative charges at the lipid-water interface. Biochemistry 1986; 25: 1726–1733
   PubMed Web of Science ®Google Scholar
• Thuren T., Tukki A. P., Virtanen J. A., Kinnunen P. K. J. Triggering of the activity of phospholipase A2 by an electric field. Biochemistry 1987; 26: 4907–4910
   PubMed Web of Science ®Google Scholar
• Conricode K. M., Ochs R. S. Mechanism for the inhibitory and stimulatory actions of proteins on the activity of phospholipase A2. Biochimica et Biophysica Acta 1989; 1003: 36–43
   Google Scholar
• Schwarzmann G., Hoffman-Bleihauer P., Schubert J., Sandhoff K., Marsh D. Incorporation of ganglioside analogs into fibroblast cell membranes. A spin-label study. Biochemistry 1983; 22: 5041–5048
   Google Scholar
• Maggio B., Montich G. G., Cumar F. A. Surface topography of sulphatide and gangliosides in unilamelar vesicles of dipalmitoyl phosphatidylcholine. Chemistry and Physics of Lipids 1988; 46: 137–146
   Google Scholar
• Sonnino S., Ghidoni R., Marchesini S., Tettamanti G. Cytosolic gangliosides: occurrences in calf brain as gangliosides-protein complexes. Journal of Neurochemistry 1979; 33: 117–121
   Google Scholar
• Hansson H. A., Holmgreng J., Svennerholm L. Ultrastructural localization of cell membrane GM1 ganglioside by cholerae toxin. Proceedings of the National Academy of Sciences, USA 1977; 74: 3782–3786
   PubMed Web of Science ®Google Scholar
• Landa C. A., Defilpo S. S., Maccioni H. J. F., Caputto R. Disposition of gangliosides and syaloglycoproteins in neuronal membranes. Journal of Neurochemistry 1981; 37: 813–823
   Google Scholar
• Higashi H., Omori A., Yamagata T. Calmodulin, a ganglioside binding protein. Binding of gangliosides to calmodulin in the presence of calcium. Journal of Biological Chemistry 1992; 267: 9831–9838
   PubMed Web of Science ®Google Scholar
• Gillard B. K., Jones M. A., Turner A. A., Lewis D. E., Marcus D. M. Interferon Y alters expression of endothelial cell surface glycosphingolipids. Archives of Biochemistry and Biophysics 1990; 279: 122–129
   Google Scholar
• Chigorno V., Valsecchi M., Acquotti D., Sonnino S., Tettamanti G. Formation of a cytosolic ganglioside-protein complex following administration of photoreactive ganglioside GM1 to human fibroblasts in culture. FEBS Letters 1990; 263: 329–331
   Google Scholar