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The neuropathy of plasma cell dyscrasia

Binding of IgM M-proteins to peripheral nerve glycolipids

From the Department of Neurology (Drs. Freddo and Latov), Columbia University-College of Physicians and Surgeons. New York. NY; and the Department of Neurology (Drs. Ariga. Saito, Macala. and Yu). Yale University School of Medicine, New Haven, CT.

In some patients with neuropathy and plasma cell dyscrasia, the M-proteins bind to peripheral nerves. Binding of M-proteins to peripheral nerve glycolipids was examined by immunostaining after thin-layer chromatography. The IgM from 16 patients with anti-MAG M-proteins bound to the same two glycolipid bands in peripheral nerve. The IgM that bound to the glycolipids had the same idiotype as the anti-MAG M-protein, indicating that it was the M-protein that bound to both glycolipids. The reactive glycolipids did not contain sialic acid and were not gangliosides. No immunostaining of peripheral nerve glycolipids was observed with IgM from patients with neuropathy and IgM M-proteins that did not bind to MAG, and the anti-MAG antibodies did not bind to brain glycolipids. Anti-MAG M-proteins probably bind to the same or closely related carbohydrate determinants that are shared by a number of glycoproteins and glycolipids of peripheral nerve.

Address correspondence and reprint requests to Dr. Latov, Department of Neurology, Columbia University-College of Physicians and Surgeons. 630 West 168th Street. New York. NY 10032.

Supported by grants NS006.59, NS18016, and NS11853 from the National Institutes of Health: by a grant from the Muscular Dystrophy Association; and by grants RG1289B–3 and RG1531A–1 from the Multiple Sclerosis Society. Dr. L. Freddo is a visiting fellow from the University of Padova, Italy, and the recipient of a research fellowship from the Muscular Dystrophy Association.

Accepted for publication January 16, 1985.

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