Abstract
Novel sulfated glucuronic acid-containing glycolipids have been identified in the nervous system. These glycolipids are highly antigenic and share antigenic determinants with several nervous system glycoproteins, such as neural cell adhesion molecules, myelin-associated glycoprotein, and ependymins. The structure of the major antigenic glycolipid from human peripheral nerve was determined by chemical and enzymatic degradation, incorporation studies, sugar analysis after permethylation, pertrimethylsilylation, and gas liquid chromatography-mass spectrometry techniques as well as fast atom bombardment-mass spectrometry of the native antigen. The following structure was established for the major antigenic glycolipid. sulfate-3-GlcA beta(1---3)Gal beta(1----4)GlcNAc beta(1----3)Gal beta(1----4)Glc beta(1----1)-ceramide. The major fatty acids in the ceramide were 18:0, 18:1, 24:0, and 24:1, with C18-sphingenine as the long chain base.
Highlights
Novel sulfated glucuronic acid-containing glyco- HSB-2 andrecognizing surface antigens oansubset of human lipids have been identified in the nervous system. lymphocytes including natural killer cells [5, 6]
Thefollowing sion molecules such as N-CAM, L1, and J1 antigens, which are specificallyinvolved in neural cell interactions [10,11,12] and on a group of glycoproteins called ependymins localized in the extracellulafrluid of goldfish brain andwhich have been shown to alter during learning and memory processes [13].We have shown that the glycolipid antigens recognized structure was established for the major antigenic glycolipid
The antigenicglycolipidswere found in the tetrasialoganglioside fraction which was eluted with 0.5 M ammonium acetate in methanol
Summary
Vol 261, No 25, Issue of September 5, pp. 11717-11725,1986 Printed in U.S.A. Structure of Sulfated Glucuronyl Glycolipidsin the Nervous System Reacting with HNK-1 Antibody and SomeIgM Paraproteins in Neuropathy*. The reactive epitope is alsoexpressed on certain neuralcell adhestructure of the major antigenic glycolipid from human peripheral nerve was determined by chemical and enzymatic degradation, incorporation studies, sugar analysis after permethylation, pertrimethylsilylation, and gas liquid chromatography-mass spectrometry techniques as well as fast atombombardment-mass spectrometry of the native antigen Thefollowing sion molecules such as N-CAM, L1, and J1 antigens, which are specificallyinvolved in neural cell interactions [10,11,12] and on a group of glycoproteins called ependymins localized in the extracellulafrluid of goldfish brain andwhich have been shown to alter during learning and memory processes [13].We have shown that the glycolipid antigens recognized structure was established for the major antigenic glycolipid. Proteins [2, 3]
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