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paraproteinemias/carbohydrate
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IgM in a human neuropathy related to paraproteinemia binds to a carbohydrate determinant in the myelin-associated glycoprotein and to a ganglioside.
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The IgM in three patients with paraproteinemia and peripheral neuropathy was shown to bind to human myelin-associated glycoprotein (MAG) that had been purified to homogeneity by gel filtration on Sepharose CL-6B. The antigenic determinant reacting with the IgM from all three patients was in the
Plasma cell dyscrasia associated with the production of incomplete (?deleted) IgGlambda molecules, gamma heavy chains, and free lambda chains containing carbohydrate: description of the first case.
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[Protein-bound carbohydrate components in paraproteinemias].
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Serum IgG antibodies to P0 dimer and 35 kDa P0 related protein in neuropathy associated with monoclonal gammopathy.
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BACKGROUND
Peripheral neuropathies (PN) associated with monoclonal gammopathy (MG) are widely considered as autoimmune disorders, but the putative role of incriminated antigens is still not understood.
OBJECTIVE
Fifty five patients with PN associated with MG were studied to investigate whether new
Heterogeneity of antibody specificity in Taiwanese patients with polyneuropathy and IgM paraproteinemia.
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About half of the Caucasian patients with chronic polyneuropathy and IgM paraproteinemia show serum anti-myelin-associated glycoprotein (MAG) and anti-sulfoglucuronosyl glycosphingolipid (SGGLs) activities. These antibody activities have been demonstrated to react with a carbohydrate epitope known
The neuropathy of plasma cell dyscrasia: binding of IgM M-proteins to peripheral nerve glycolipids.
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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
The role of sulfoglucuronosyl glycosphingolipids in the pathogenesis of monoclonal IgM paraproteinemia and peripheral neuropathy.
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In IgM paraproteinemia and peripheral neuropathy, IgM M-protein secretion by B cells leads to a T helper cell response, suggesting that it is antibody-mediated autoimmune disease involving carbohydrate epitopes in myelin sheaths. An immune response against sulfoglucuronosyl glycosphingolipids
Primary structure of a deleted human lambda type immunoglobulin light chain containing carbohydrate: protein Sm lambda.
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An internal molecular deletion occurring in a human lambda type immunoglobulin light (L)-chain (Sm lambda) has been defined by sequence analysis. The Sm protein was isolated from the urine of a patient with a plasma cell dyscrasia involving the synthesis of an IgG molecule with both deleted gamma
Localization of the carbohydrate units in a human immunoglobulin light chain, protein Sm lambda.
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The carbohydrate structure and complete amino acid sequence of a human lambda-type immunoglobulin light chain, protein Sm lambda has been determined. The protein was isolated from the urine of a patient with a plasma cell dyscrasia resembling gamma-heavy-chain disease. 13 tryptic peptides covering
[The neuropathies of IgM monoclonal gammopathies].
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A peripheral polyneuropathy is often associated with an IgM monoclonal gammapathy. The monoclonal protein often binds to carbohydrate epitopes on glycoproteins and/or glycolipids of the human peripheral nerve. The clinical syndrome is related to the antigen-specificity of the IgM protein. Detection
The role of human natural killer-1 (HNK-1) carbohydrate in neuronal plasticity and disease.
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The human natural killer-1 (HNK-1) carbohydrate, a unique trisaccharide possessing sulfated glucuronic acid in a non-reducing terminus (HSO3-3GlcAß1-3Galß1-4GlcNAc-), is highly expressed in the nervous system and its spatiotemporal expression is strictly regulated. Mice deficient in the gene
Carbohydrate analysis of immunoglobulin G myeloma proteins by lectin and high performance liquid chromatography: role of glycosyltransferases in the structures.
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The carbohydrate structures and the enzymatic basis for glycosylation of IgG by bone marrow plasma cells were determined in 7 patients with monoclonal gammopathy of undetermined significance and 22 patients with IgG MM. Lectin-binding analysis showed that in all cases of monoclonal gammopathy of
Differential glycosylation of Bence Jones protein and kidney impairment in patients with plasma cell dyscrasia.
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Although Bence Jones protein (BJP) is generally accepted to be critically involved in the pathogenic process of kidney impairment in patients with myeloma, patients with BJP do not always have kidney dysfunction. As proteins often undergo glycosylation and alter their molecular nature, it is
Structure-Activity Relationship Studies, SPR Affinity Characterization, and Conformational Analysis of Peptides That Mimic the HNK-1 Carbohydrate Epitope.
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The design of molecules that mimic biologically relevant glycans is a significant goal for understanding important biological processes and may lead to new therapeutic and diagnostic agents. In this study we focused our attention on the trisaccharide human natural killer cell-1 (HNK-1), considered
Monoclonal IgM in two patients with motor neuron disease bind to the carbohydrate antigens Gal(beta 1-3)GalNAc and Gal(beta 1-3)GlcNAc.
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We investigated the epitope specificity of monoclonal antibodies (M-proteins) from two patients with motor neuron disease and IgM monoclonal gammopathy. In previous studies, both M-proteins bound to gangliosides GM1 and GD1b which share Gal(beta 1-3)GalNAc as their terminal structure, and to
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