title: Relationship of membrane phospholipid composition, lactosylceramide molecular species, and the specificity of CMP-N-acetylneuraminate:lactosylceramide alpha 2,3-sialyltransferase to the molecular species composition of GM3 ganglioside.
abstract: The ceramide molecular species specificity of rat brain neuron CMP-N-acetylneuraminate:lactosylceramide alpha 2,3-sialyltransferase (LacCer alpha 2,3-ST) was determined using 19 molecular species of lactosylceramide incorporated into liposomes prepared with purified rat brain phospholipids. The neuron enzyme displayed a distinct molecular species specificity (which was different than the specificity of liver LacCer alpha 2,3-ST) based on both the long-chain base and the fatty acid composition of the lactosylceramide. Specifically, compared to the liver enzyme, relatively high activities were obtained with d18:1-16:0, d18:1-22:1, and d18:0-18:0 lactosylceramide molecular species. When the lipid composition of the neuron microsomal membranes was altered to resemble that of rat liver Golgi membrane lipids, the activities towards d18:1-16:0, d18:1-22:1, and d18:0-18:0 lactosylceramide molecular species were significantly (P < 0.01) reduced and the molecular species specificity of the neuron enzyme resembled that of liver LacCer alpha 2,3-ST. In the reciprocal experiment in which the lipid composition of the rat liver Golgi membranes was altered to resemble neuron microsomal membrane lipids, the molecular species specificity of liver LacCer alpha 2,3-ST was virtually identical to the specificity obtained with the native neuron enzyme. Analysis of the molecular species composition of lactosylceramide and GM3 in rat liver Golgi membranes revealed that the molecular species composition of rat liver Golgi membrane GM3 was precisely what would be expected based on the molecular species specificity of LacCer alpha 2,3-ST and the molecular species composition of lactosylceramide in the Golgi membrane.(ABSTRACT TRUNCATED AT 250 WORDS)
authors.affiliation: Department of Medicine, Boston University School of Medicine, MA 02118, USA.
authors.forename: H
authors.initials: H
authors.lastname: Kadowaki
authors.forename: M A
authors.initials: MA
authors.lastname: Grant
mesh_terms: D000818:Animals; D015703:Antigens, CD; D001921:Brain / Q000201:enzymology / Q000648:ultrastructure; D002462:Cell Membrane / Q000378:metabolism*; D005679:G(M3) Ganglioside / Q000378:metabolism*; D006028:Glycosphingolipids / Q000378:metabolism*; D006056:Golgi Apparatus / Q000648:ultrastructure; D007790:Lactosylceramides; D008081:Liposomes / Q000378:metabolism; D008099:Liver / Q000648:ultrastructure; D008297:Male; D008861:Microsomes / Q000648:ultrastructure; D009474:Neurons / Q000201:enzymology; D010743:Phospholipids / Q000378:metabolism*; D051381:Rats; D017207:Rats, Sprague-Dawley; D012799:Sialyltransferases / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D015703:Antigens, CD; D005679:G(M3) Ganglioside; D006028:Glycosphingolipids; D007790:Lactosylceramides; D008081:Liposomes; D010743:Phospholipids; C009744:CDw17 antigen; D012799:Sialyltransferases; C021343:haematoside synthetase