Purification and partial characterization of the myelin-associated glycoprotein from adult rat brain

Quarles, Richard H.; Barbarash, Gary R.; Figlewicz, Denise A.; McIntyre, Laurence J.

doi:10.1016/0304-4165(83)90162-9

Cited by 79 publications

(26 citation statements)

References 11 publications

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“…Experiments in several laboratories have provided evidence that the monoclonal IgM in some of these patients binds to the myelin-associated glycoprotein (MAG) (10)(11)(12)(13)(14). In this paper, it is demonstrated that the monoclonal IgM antibodies in three neuropathy patients of this type bind to human MAG purified to homogeneity by the procedure routinely used in our laboratory for chemical studies on this glycoprotein (15). It is further shown that the antibodies are directed against determinants in the carbohydrate part of the MAG molecule.…”

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confidence: 86%

“…Comparison with known standards showed that the ganglioside reacting with the IgM chromatographed slower than GM1 and slightly faster than GDla. DISCUSSION Reactivity of the monoclonal IgM in several patients with paraproteinemia and peripheral neuropathy was demonstrated with MAG purified by a procedure developed in our laboratory for obtaining this glycoprotein in homogeneous form for chemical studies (15). IgM binding to the purified MAG was shown both by immunoblotting experiments and by double-antibody precipitation of 125I-labeled MAG.…”

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confidence: 98%

“…The maximal radioactivity that could be precipitated by the patients' sera was comparable to that precipitated by known rabbit anti-MAG antiserum. This shows that the component reacting with the 15 ,ug; C, 220 ng; D-G, 500 ng. The MAG and deglycosylated MAG on the various lanes ran as two closely spaced bands representing MAG and a slightly lower molecular weight derivative (dMAG) formed by a protease in purified myelin that has been described (31).…”

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confidence: 99%

“…Human and rat MAG were selectively extracted from the purified myelin by the lithium diiodosalicylate/phenol procedure (17) and further purified by gel filtration on Sepharose CL-6B as described (15). Deglycosylation of partially purified MAG obtained by the lithium diiodosalicylate/phenol procedure was carried out with trifluoromethanesulfonic acid (18).…”

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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.

Ilyas¹,

Quarles²,

MacIntosh³

et al. 1984

Proc. Natl. Acad. Sci. U.S.A.

220

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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 carbohydrate part of the MAG molecule. In addition, the IgM from the same three patients bound to a single ganglioside of human sciatic nerve. The results indicate that the IgM paraproteins in these patients react with a carbohydrate determinant that is shared between MAG and a peripheral nerve ganglioside.

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confidence: 86%

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confidence: 98%

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confidence: 99%

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confidence: 99%

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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.

Ilyas¹,

Quarles²,

MacIntosh³

et al. 1984

Proc. Natl. Acad. Sci. U.S.A.

220

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“…However, using 'YS to metabolically label cerebellar cell cultures, a labeled molecule of approximately 90,000 M, that binds to mOg-1 has been isolated on affinity columns containing purified goat anti-mouse IgM immunoglobulin, and it appears to be the Og-1 antigen. Although the molecular weight is similar to that of myelin-associated glycoprotein (MAG) (Quarles et al, 1983), mOg-1 does not react with rat or human MAG (A. Noronha, R. H. Quarles, and N. W. Seeds, unpublished observations).…”

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confidence: 99%

Oligodendroglia development in cell culture as monitored with a monoclonal antibody

Collins¹,

Seeds²

1986

J. Neurosci.

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A new marker for young oligodendrocytes has been identified by a monoclonal antibody (mOg-1, IgM isotype) prepared from cerebellar plasma membrane stimulated mouse lymphocytes. mOg-1 reactive cells in the mouse cerebellum first appear at day 19 of gestation. Future white matter layers of fixed sections of neonatal rat cerebellum were labeled with mOg-1. Although EM analysis has shown cell-surface binding by presumptive oligodendroglia in neonatal cerebellum, the antibody does not bind to compact myelin. In cell cultures prepared from L-d-old mice, 1.1% of the cells bound mOg-1 after 3 d in culture, but up to 5% of the cells bound mOg-1 after 2 weeks in culture. Of these same Og-l-positive cells, 69% bound anti-gabtctocerebroside and 65% bound anti-myelin basic protein. After a week in culture Og-l-positive cells often produced lamellar sheets extending a millimeter over the polylysine substratum in the absence of normal myelin formation. mOg-1 recognizes a cell-surface determinant distinct from well-characterized oligodendroglial molecules (galactocerebroside, sulfatide and myelin basic protein) that is expressed early in oligodendrocyte development. The antibody has been used to follow the maturation of oligodendrocytes in cultures of both normal and jimpy mouse cerebellum.The nervous system is a complex network derived from multiple associations between different cell types. The limited number of distinct cell types and the availability of neurological mutants with defective cerebellar histogenesis make the mouse cerebellum an attractive model for studying cell-cell interactions.The development of antibodies toward neural cell-surface molecules could be instrumental in establishing the role of specific determinants in histogenesis. We have used the hybridoma technology of Milstein (1975, 1976) In this report, we describe a monoclonal antibody (mOg-1) reactive with the surface of young oligodendrocytes, prior to the Received Dec. 19, 1985; revised Mar. 4, 1986; accepted Mar. 4, 1986. We woula like to thank Dr. Robert Lasher for his helpful discussions and S.Hat&e for her expert assistance. We thank Drs. Dahl, De.Vellis, Evans, Habig, Qua&s, Ranscht, and Rapport for their generous girt of antisera and tetanus toxin used in these studies. Some of these studies were submitted in partial fulfillment of the requirementi for the Doctor of Philosophy degree from the University of Colorado (1983). This work was su~ucwted in nart bv USPHS Grants NS-098 18and T32-bM-07342.

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Antibodies to Myelin-Associated Glycoprotein Are Found in Cerebrospinal Fluid in Polyneuropathy Associated With Monoclonal Serum IgM

Cruz¹,

Ernerudh²,

Solders³

et al. 1991

Archives of Neurology

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Purification and partial characterization of the myelin-associated glycoprotein from adult rat brain

Cited by 79 publications

References 11 publications

IgM in a human neuropathy related to paraproteinemia binds to a carbohydrate determinant in the myelin-associated glycoprotein and to a ganglioside.

IgM in a human neuropathy related to paraproteinemia binds to a carbohydrate determinant in the myelin-associated glycoprotein and to a ganglioside.

Oligodendroglia development in cell culture as monitored with a monoclonal antibody

Antibodies to Myelin-Associated Glycoprotein Are Found in Cerebrospinal Fluid in Polyneuropathy Associated With Monoclonal Serum IgM

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