|
|
||||||||
Journal of Lipid Research, Vol 36, 1274-1282, Copyright © 1995 by Lipid Research, Inc.
H Kadowaki and MA Grant
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)
ARTICLES
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
Department of Medicine, Boston University School of Medicine, MA 02118, USA.
![]()
CiteULike
Complore
Connotea
Del.icio.us
Digg
Reddit
Technorati What's this?
This article has been cited by other articles:
![]() |
D. S. Lin, M. Neuringer, and W. E. Connor Selective changes of docosahexaenoic acid-containing phospholipid molecular species in monkey testis during puberty J. Lipid Res., March 1, 2004; 45(3): 529 - 535. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Journal of Biological Chemistry |
| Molecular and Cellular Proteomics | ASBMB Today |