title: Mutual modulation of sphingomyelinase and phospholipase A2 activities against mixed lipid monolayers by their lipid intermediates and glycosphingolipids.
abstract: Sphingomyelinase activity against pure sphingomyelin monolayers is constant up to a surface pressure of 18 mN/m and falls above it. Sphingomyelinase- and phospholipase A2-mediated phosphohydrolytic pathways are mutually modulated by the presence of their respective substrates and products. At 15 mN/m non-substrate lipids such as ceramide at a mole fraction of 0.1 in mixed films with the pure substrate, inhibit the sphingomyelinase activity. Ganglioside GM1, another ceramide-containing complex sphingolipid, also inhibits sphingomyelinase activity, while a chemically related glycosphingolipid such as asialo-GM1 has no effect. The activity is unaltered by dipalmitoylphosphatidylcholine and by an equimolar mixture of its products of hydrolysis by phospholipase A2, fatty acid and lysoderivative, but it is inhibited by only one of them or by dilauroylphosphatidylcholine. Phospholipase A2 is inhibited by sphingomyelin, and activated by ceramide and by palmitic acid, one of the products of its own phosphohydrolytic reaction.
authors.affiliation: Departamento de Quimica Biológica-CIQUIBIC, Facultad de Ciencias Químicas-CONICET, Universidad Nacional de Córdoba, Argentina.
authors.forename: M L
authors.initials: ML
authors.lastname: Fanani
authors.forename: B
authors.initials: B
authors.lastname: Maggio
mesh_terms: D000818:Animals; D001409:Bacillus cereus / Q000201:enzymology; D002518:Ceramides / Q000737:chemistry; D006028:Glycosphingolipids / Q000737:chemistry; D010741:Phospholipases A / Q000737:chemistry* / Q000378:metabolism; D054467:Phospholipases A2; D013108:Sphingomyelin Phosphodiesterase / Q000737:chemistry* / Q000378:metabolism; D013109:Sphingomyelins / Q000737:chemistry; D013552:Swine
chemical_list: D002518:Ceramides; D006028:Glycosphingolipids; D013109:Sphingomyelins; D010741:Phospholipases A; D054467:Phospholipases A2; D013108:Sphingomyelin Phosphodiesterase