Characterization of sulfated glucuronic acid containing glycolipids reacting with IgM M-proteins in patients with neuropathy Academic Article uri icon

Overview

MeSH Major

  • Cauda Equina
  • Globosides
  • Glycolipids
  • Glycosphingolipids
  • Myelin Proteins
  • Nervous System Diseases

abstract

  • In some patients with neuropathy and plasma cell dyscrasia, the serum IgM M-proteins are known to bind to the myelin associated glycoprotein and to peripheral nerve glycolipids. We have isolated two acidic glycolipids which bind to the M-protein from human cauda equina by DEAE-Sephadex, Iatrobeads, and high performance liquid column chromatographies. The major acidic glycolipid migrated between GM1 and GD1a and the minor acidic glycolipid migrated between GD1a and GD1b. Their structures were elucidated by sugar analysis, enzymatic digestion, mild acid hydrolysis, permethylation, fast atom bombardment mass spectrometry, and NMR studies. Their core structure was confirmed to be paragloboside by high performance thin-layer chromatography-immunostaining using anti-paragloboside monoclonal antibody. Both acidic glycolipids lacked sialic acid but contained sulfated glucuronic acid as their acidic moiety. The sulfate group in the glucuronic acid was established by periodate oxidation and permethylation studies to be attached to the 3 position. The structures of the two acidic glycolipids are therefore consistent with the following: IV3GlcUA(3-sulfate)nLcOse4Cer and VI3GlcUA(3-sulfate)nLcOse6Cer. Additionally, the free carboxyl group on the glucuronic acid residue was shown to be necessary to bind the IgM M-proteins from neuropathy patients.

publication date

  • March 26, 1987

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed ID

  • 2433270

Additional Document Info

start page

  • 848

end page

  • 53

volume

  • 262

number

  • 2