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Results for “Myelin-Associated Glycoprotein”

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At least 19 recordsLinked to original sources
PubMed1979

Myelin-associated glycoprotein demonstrated immunocytochemically in myelin and myelin-forming cells of developing rat.

The unlabeled peroxidase-antiperoxidase method has been used with antiserum against "myelin-associated glycoprotein" to establish the presence of the glycoprotein in myelin and myelin-forming cells of the developing rat nervous system. Myelin-associated glycoprotein is found in oligodendroglial cytoplasm before the beginning of myelination. Staining intensity of oligodendroglia increases during early development and slowly declines during the period of rapid myelination. Myelin staining is confined to the periaxonal region of the myelin sheath and does not increase as large, compact sheaths are formed. Antiserum to central nervous system myelin-associated glycoprotein also stains Schwann cells in developing trigeminal ganglia and the periaxonal region of peripheral myelin sheaths.

Animals↗
PubMed1976

Effects of pronase and neuraminidase treatment on a myelin-associated glycoprotein in developing brain.

Rats (14 days old) were injected with [14c]fucose and young adult rats with [3H]fucose in order to label the myelin-associated glycoproteins. As previously reported, the major [14C]fucose-labelled glycoprotein in the immature myelin had a higher apparent molecular weight on sodium dodecyl sulphate/polyacrylamide gels that the [3H]fucose-labelled glycoprotein in mature myelin. This predominant doubly labelled glycoprotein component was partially purified by preparative gel electrophoresis and converted to glycopeptides by extensive Pronase digestion. Gel filtration on Sephadex G-50 separated the glycopeptides into several clases, which were designted A,B, C AND D, from high to low molecular weight. The 14C-labelled glycopeptides from immature myeline were enriched in the highest-molecular-weight class A relative to the 3H-labelled glycopeptides from mature myelin. Neuraminidase treatment of the glycoprotein before Pronase digestion greatly decreased the proportion of glycopeptides fractionating in the higher-molecular-weight classes and largely eliminated the developmental differences that were apparent by gel filtration. However, neuraminidase treatment did not decrease the magnitude of the developmental difference revealed by electrophoresing the intact glycoprotein on sodium dodecyl sulphate gels, although it did decrease the apparent molecular weight of the glycoprotein from both the 15-day-old and adult rats by an amount comparable in magnitude to that developmental difference. The results from gel filtration of glycopeptides indicate that there is a higher content of large molecular weight, sialic acid-rich oligosaccharide units in the glycoprotein of immature myelin. However, the higher apparent molecular weight for the glycoprotein from 15-day-old rats on sodium dodcyl sulphate gels is not due primarily to its higher sialic acid content.

Animals↗
PubMed1975

Change in a myelin-associated glycoprotein in rat brain during development: metabolic aspects.

The higher apparent molecular weight of the newly synthesized glycoprotein in immature rat myelin in comparison with that in mature myelin, which was originally demonstrated with radioactive fucose, was also shown by double labeling experiments with radioactive glucosamine or N-acetylmannosamine. In addition, periodic acid-Schiff staining of gels, on which the glycoproteins of mature and immature myelin were electrophoresed separately or mixed together, revealed that the stained glycoprotein in immature myelin had a higher apparent molecular weight. Age studies with radioactive fucose showed that the greatest difference in the apparent molecular weight of the newly synthesized glycoprotein occurred at 12 days. The magnitude of the difference decreased gradually with age until 25 days when the glycoprotein electrophoresed to the same position as that in more mature myelin. Long-term experiments, in which 12- or 13-day-old rats were injected with radioactive fucose and allowed to survive for varying periods of time before myelin isolation, also revealed a gradual decrease with age in the extent of the shift of the glycoprotein toward a higher molecular weight. The possible significance of the developmental change in the glycoprotein for the process of myelin formation is discussed.

Age Factors↗
PubMed1979

Lectin-binding proteins in central-nervous-system myelin. Detection of glycoproteins of purified myelin on polyacrylamide gels by [3h]concanavalin A binding.

Concanavalin A strongly agglutinates purified fragments of immature and mature rat brain myelin, but only weakly agglutinates mature bovine and human myelin fragments. A sensitive method involving [3H]concanavalin binding to sodium dodecyl sulphate/polyacrylamide gels was used to detect the concanavalin A-binding proteins in purified myelin. When applied to mature rat brain myelin proteins that had been labelled in vivo with [14C]fucose, the distribution of the [3H]concanavalin A on the gel was very similar to that of [14C]fucose with the major peak corresponding to the major myelin-associated glycoprotein. The technique revealed that the immature form of the myelin-associated glycoprotein with a slightly larger apparent molecular weight also bound concanavalin A, and that in purified immature rat myelin the quantitative importance of some of the other glycoproteins in binding concanavalin A was increased relative to the myelin-associated glycoprotein. The separated proteins of bovine and human myelin bound more [3H]-concanavalin A than those of rat myelin. In these species, the myelin-associated glycoprotein was a major concanavalin A-binding protein, although two higher-molecular-weight glycoproteins also bound significant quantities of [3H]concanavalin A. The results indicate that there are receptors for concanavalin A on the surface of rat, bovine and human myelin membranes and suggest that the myelin-associated glycoprotein is one of the principal receptors.

Adult↗
PubMed1979

Lectin-binding proteins in central-nervous-system myelin. Binding of glycoproteins in purified myelin to immobilized lectins.

The capacities of immature and mature rat brain myelin, bovine myelin and human myelin to be agglutinated by soya-bean agglutinin, Ricinus communis agglutinin, wheatgerm agglutinin, and Lotus tetragonolobus agglutinin were examined. The first two lectins, which are specific for galactose and N-acetylgalactosamine, strongly agglutinated immature and mature rat myelin, weakly agglutinated bovine myelin, but did not affect human myelin. The other myelin and lectin combinations resulted in very weak or no agglutination. [(3)H]Fucose-labelled glycoproteins of purified adult rat brain myelin were solubilized with sodium dodecyl sulphate and allowed to bind to concanavalin A-Sepharose and each of the other lectins mentioned above, which had been immobilized on agarose. About 60% of the radioactive fucose was in glycoproteins that bound to concanavalin A-Sepharose and these glycoproteins could be eluted with solutions containing methyl alpha-d-mannoside and sodium dodecyl sulphate. Periodate/Schiff staining or radioactive counting of analytical gels showed that most of the major myelin-associated glycoprotein (apparent mol.wt. approx. 100000) bound to the concanavalin A, whereas the glycoproteins that did not bind were mostly of lower molecular weight. Preparative polyacrylamide-gel electrophoresis of the glycoprotein fraction that was eluted with methyl alpha-d-mannoside yielded a relatively pure preparation of the myelin-associated glycoprotein. Similar results were obtained with each of the other lectins, i.e. the myelin-associated glycoprotein was in the fraction that bound to the immobilized lectin. Double-labelling experiments utilizing [(3)H]fucose-labelled glycoproteins from adult myelin and [(14)C]fucose-labelled glycoproteins from 14-day-old rat brain myelin did not reveal any difference in the binding of the mature and immature glycoproteins to any of the immobilized lectins. The results in this and the preceding paper [McIntyre, Quarles & Brady (1979) Biochem. J.183, 205-212] suggest that the myelin-associated glycoprotein is one of the principal receptors for concanavalin A and other lectins in myelin, and that this property can be utilized for the purification of this glycoprotein.

Agglutination↗
PubMed1992

Childhood peripheral neuropathy with autoantibodies to myelin glycoprotein P0.

The serum of a 4-year-old child with severe hypertrophic peripheral neuropathy contained high-titer polyclonal antibodies, mainly of IgG class, reacting with the 30-kd P0 glycoprotein of peripheral nerve. This was demonstrated by indirect immunofluorescence, immunoblot analysis of myelin proteins, and enzyme-linked immunosorbent assay with purified P0 glycoprotein. The antibodies did not react with myelin-associated glycoprotein, sulfated glycuronic acid-containing paragloboside (SGPG and SGLPG), or other peripheral nerve glycolipids or gangliosides. To our knowledge this is the first report of strong antibody activity specifically directed against P0. This antibody may play a causative role in the pathogenesis of the peripheral neuropathy in this patient.

Autoantibodies↗
PubMed1992

Differential upregulation of PLP and MAG genes in C6 glioma cells by N2A neuroblastoma conditioned medium.

The effect of factors released from N2A neuroblastoma cells on the expression of myelin protein genes in glioma C6 cells, i.e., proteolipid protein (PLP) and myelin-associated glycoprotein (MAG), was studied. Both cells lines were propagated in serum-free DMEM-F10 (1:1) medium. The addition of 50% N2A conditioned medium (N2ACM) stimulated the proliferation of C6 cells by approximately 4.5 fold as compared to control cells. The N2ACM-treated cells formed aggregates indicating increased cell-cell affinity. The exposure of C6 cells to N2ACM transiently stimulated the expression of both the MAG-specific and the PLP-specific messages up to eight and four fold over the control values, respectively. The maximal upregulation of the PLP gene occurred two days after N2ACM administration and preceded that of the MAG gene by two days. The effect of N2ACM was dose-dependent in the range of 12.5 to 50%. The secretion of N2A paracrine factors that stimulated the myelin gene expression was also time-dependent. The optimal conditioning time for the release of the PLP gene-stimulating activity was one day, while the maximal MAG gene-stimulating activity was found in the medium conditioned for 3 days. This cellular system may provide a convenient model for studies on trophic neuronal-glial interaction. Furthermore, the results indicate a difference in the regulatory mechanisms between the PLP and the MAG genes.

Animals↗
PubMed1992

Ascorbic acid upregulates myelin gene expression in C6 glioma cells.

The effect of ascorbic acid (AA) on rat glioma C6 cells was studied. At physiological AA concentrations of 0.1 and 1 mM, no morphological and no proliferative alterations in the C6 cultures were detectable. Although the total RNA content per cell was not affected by the AA-treatment, AA upregulated the expression of myelin-specific genes, i.e. proteolipid protein (PLP) and myelin-associated glycoprotein (MAG) genes as assessed by northern blot analysis. The steady-state level of the specific mRNAs increased transiently in the AA-treated cells. Three days after AA administration the message level reached a maximum of 10- and 2-fold over control for the PLP and MAG genes, respectively. The upregulation of the genes was directly related to AA concentration. The present data indicate a possible involvement of AA in the regulation of myelin gene activity in the CNS.

Animals↗
PubMed1976

Hypomyelination in copper-deficient rats. Prenatal and postnatal copper replacement.

Copper deficiency induced by a low copper diet in three generations of rats was associated with substantial reductions in the yield of myelin (56%), brain weight (11%), and body weight (43%) in F2 generation rat pups nursed by their own copper-deficient mothers. The composition of the purified myelin was not different from that of controls in the content of individual proteins, lipids, 2',3'-cyclic nucleotide 3'-phosphohydrolase (CNP) activity, or GM1 ganglioside. The major myelin-associated glycoprotein (mGP) was consistently shifted slightly toward higher apparent molecular weight in the copper-deficient animals. Postnatal copper replacement by a foster mother produced a normal yield of myelin per gram of brain tissue, but failed to reverse the deficiency of brain and body growth. After copper replacement in a copper-deficient mother's diet prior to conception, a subsequent litter showed correction of all abnormalities found in her previous litters. The results suggest that copper is essential for myelin formation and general growth during critical periods in development.

Age Factors↗
PubMed1978

Protein heterogeneity in rat CNS myelin subfractions.

Microsomal fraction-free myelin from forebrain and spinal cord of young and mature rats, when subjected to hypo-osmotic shock and slow speed centrifugation, yielded a myelin pellet and a supernatant fraction (SN 4). Fraction SN 4 consisted of small vesicular profiles in which the major myelin proteins were reduced whereas high molecular weight material such as Wolfgram protein, myelin-associated glycoprotein and CNP were substantially increased over myelin. A close correlation of the SN 4 fraction to the myelin-like fraction of Davison and coworkers was suggested. The myelin pellets were subfractioned on zonal sucrose gradients to yield bell-shaped particle distributions. Besides shifts in densities of the maxima between myelin of young and mature forebrain and spinal cord, a decrease was observed from the light to the heavy gradient end in basic proteins, and an increase in Wolfgram protein and other high molecular weight proteins. Proteolipid protein took an intermediate position. Light fractions from adult spinal cord displayed CNP activities below those of the total homogenate. This result, together with the very high CNP activities in fraction SN 4 casts some doubt on CNP being a marker for compact myelin; rather it appears that CNP is a marker for the process of myelin formation.

2',3'-Cyclic-Nucleotide Phosphodiesterases↗
PubMed1975

Isolation of axonally transported glycoproteins with goldfish visual system myelin.

[3H]fucose labeled glycoproteins which are rapidly transported in the goldfish optic nerve have been isolated with purified preparations of goldfish optic tectal myelin. SDS acrylamide gels of myelin proteins isolated one day after intraocular injection of fucose show a broad distribution of radioactivity among high molecular weight proteins. At progressively longer times after injection there is a shift in the distribution of radioactivity with the buildup of a peak of label with electrophoretic mobility corresponding to a molecular weight of approximately 50,000. There is no corresponding peak of radioactivity in gels of total tectal membranes. Gels of myelin labeled through intracranial injections of fucose also show no single prominent peak of radioactivity. Results are discussed with reference to possible mechanisms for the shift in radioactivity patterns on gels and the possible functional significance of the myelin-associated glycoproteins.

Animals↗
PubMed1975

[35-S]sulfate incorporation into myelin glycoproteinsmi=entral nervous system.

The in vivo incorporation of [35-S]sulfate and [3H]fucose into rat brain myelin was investigatedmmost of the 35S in the myelin was in sulfatide, but about 4% was associated with the residual proteins after chloroform/methanol extraction. Polyacrylamide gel electrophoresis of these proteins indicated that the major 35-S-labeled component corresponded to the major fucose-labeled glycoproteinmthe labeling of this predominant glycoprotein with sulfate was more selective than with fucose, since there was relatively little incorporation of sulfate into some of the minor fucose-labeled glycoproteins. There was little or no 35-S associated with proteolipid or basic protein on polyacrylamide gels. The fucose-labeled glycoproteins were converted to glycopeptides by pronase digestion and separated into two major classes by gel filtration on Sephadex-G-50. Only the higher molecular weight class contained significant amounts of 35-S. The association of 35-S with the glycopeptides was not due to binding of sulfatide or free inorganic sulfate. The results indicate that the predominant myelin-associated glycoprotein in rat brain is sulfated.

Animals↗
PubMed1977

A rapid procedure for selectively isolating the major glycoprotein from purified rat brain myelin.

Treatment of the chloroform/methanol-insoluble residue of rat brain myelin with lithium 3,5-di-iodosalicylate solubilized the major myelin-associated glycoprotein along with most other proteins and glycoproteins. Equilibration of the extract with phenol resulted in the selective partitioning of the major glycoprotein into the aqueous phase, whereas nearly all of the other proteins and glycoproteins went into the phenol phase.

Animals↗
PubMed1992

Immunochemical and clinical effects of immunosuppressive treatment in monoclonal IgM neuropathy.

A pathogenic role of the M protein in monoclonal IgM neuropathy has been suggested. This is based among other things on a close relation between immunosuppressive treatment, lowered concentration of M protein, and clinical effect. We studied five patients with monoclonal IgM and antibodies to peripheral nerve myelin. The immunosuppressive treatment was beneficial in three of the patients. In three patients there was a relationship between antibody concentration and clinical effect (in one there was no change in antibody concentrations and correspondingly no change in clinical status, and in two patients clinical improvement corresponded to decreased antibody concentrations). In two patients, however, there was no clear correlation, since one patient improved despite increasing antibody concentrations and one patient did not improve despite a lowered antibody concentration. It is therefore possible that other mechanisms may contribute to the effect of treatment.

Adult↗
PubMedDate not supplied

Changes in CNS myelin proteins and glycoproteins after in situ autolysis.

The effects of postmortem autolysis in situ on myelin proteins and glycoproteins were studied in 25- and 125-day-old mouse brain and in adult bovine brainstem. In bovine myelin a loss of the major myelin glycoprotein was the only difference observed when the tissue was left at 19 degrees C for 24 hours compared to immediately frozen material. In the autolysed mouse brain, the myelin major glycoprotein was the most affected component with a 55% decrease. Both myelin basic protein components were degraded with a 35% loss. The other myelin proteins did not change under the conditions used for this study. There was also no change in the specific activity of 2',3'-cyclic nucleotide 3'-phosphohydrolase, a myelin-associated enzyme. Using the double labelling technique with [3H]fucose and [3 5S] sulfate as precursors injected intracranially, a shift of the major myelin glycoprotein labelled with radioactive sulfate towards a smaller apparent molecular size was observed as a result of the autolysis whereas the electrophoretic mobility of the fucose labelled major peak was unaffected.

2',3'-Cyclic-Nucleotide Phosphodiesterases↗