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Demonstration of glucuronic acid on brain glycoproteins which react with HNK-1 antibody

1986; Elsevier BV; Volume: 138; Issue: 2 Linguagem: Inglês

10.1016/s0006-291x(86)80581-2

1090-2104

Victor E. Shashoua, Peter F. Daniel, Mary Moore, Firoze B. Jungalwala,

Immune Response and Inflammation

Ependymins, a family of extracellular glycoproteins of goldfish and mammalian brain, were shown to contain N-linked complex glycan chains. These glycoproteins reacted with a monoclonal antibody, HNK-1 which recognizes a membrane antigen on a subset of human lymphocytes, myelin-associated glycoprotein (MAG) and several neural cell adhesion molecules (N-CAM). The carbo-hydrate epitope reacting with HNK-1 antibody was previously shown to include a terminal 3-sulfoglucuronosyl residue present in certain glycolipids of the nervous tissue (Chou et al., Biochem. Biophys. Res. Commun. 1985, 128, 383–388). In this report, the presence of glucuronic acid in ependymins was demonstrated by gas-liquid chromatography and mass spectrometry. We suggest that a 3-sulfoglucuronosyl residue may be the common epitope on HNK-1-reactive glycoproteins.