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  • 1990-1994  (4)
  • 1980-1984  (6)
  • 1
    Electronic Resource
    Electronic Resource
    Entry of Newly Synthesized Gangliosides into Myelin (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 58 (1992), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Ganglioside synthesis and transport to myelin was studied in brainstem slices prepared from 19–21-day-old rats. The slices were incubated for up to 2 h in the presence of [3H]glucosamine to label primarily the hexosamine portion of complex gangliosides. The amount of radioactivity incorporated into gangliosides during slice incubations was only 10–15% of the amount of the label incorporated during in vivo labeling of brainstem gangliosides using equivalent amounts of [3H]glucosamine. Among individual gangliosides this inhibition was greater for the more complex gangliosides. When labeled gangliosides were isolated from homogenate and myelin fractions prepared from brain slices, the complex total gangliosides of both fractions showed a lag in labeling kinetics but with a lower specific radioactivity for the myelin fraction, reflecting the larger pool size and slower turnover rate exhibited by myelin components. Chase experiments showed that more complex gangliosides in homogenate exhibited almost no effect of chase after 30 min. Addition of the Golgi-disrupting agent monensin to slice incubations inhibited the labeling of all gangliosides except GM3, GM2, and GD3, and transport to myelin of all complex gangliosides except GM2. These results show that a monensin-sensitive mode of transport is responsible for the translocation of most newly synthesized gangliosides into myelin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1992.tb11367.x
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  • 2
    Electronic Resource
    Electronic Resource
    Effects of Monensin and Colchicine on Myelin Galactolipids (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 43 (1984), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Monensin and colchicine have been used in a variety of systems to disrupt functioning of the Golgi apparatus and transport of Golgi-derived vesicles to the plasma membrane. In this study the effects of monensin and colchicine on the synthesis of cerebroside and sulfatide and their appearance in myelin were examined to determine whether these myelin components are processed through the Golgi apparatus. Brain slices from rats 17 days old were incubated with [3H]galactose and [35S]sulfate to label cerebroside and sulfatide. Myelin was isolated on sucrose density gradients. Fractions highly enriched in cerebroside and sulfatide were prepared from homogenates and myelin fractions by lipid extraction, alkaline methanolysis, and in some cases TLC. Monensin at 0.1 μM had no significant effect on synthesis of these galactolipids as measured by incorporation of [3H]galactose into cerebroside or [35S]sulfate into sulfatide in homogenates. However, appearance of [35S]sulfatide in the myelin fraction was reduced to 49% of control, while appearance of [3H]cerebroside was not significantly reduced. Colchicine from 1 mM to 0.1 μM had effects similar to monensin, that is, appearance of [35S]sulfatide in myelin was depressed, but again [3H]cerebroside was not affected. Incorporation of [35S]sulfate into sulfatide in homogenate was 93% of control, while appearance of [35S]sulfatide in the myelin fraction was depressed to 58% of control. The inhibition of appearance of sulfatide in myelin by colchicine and monensin is consistent with the view that sulfation of cerebroside occurs in the Golgi and that sulfatide is transported via Golgi-derived vesicles to the forming myelin membrane. Further, synthesis of cerebroside and its appearance in myelin are not inhibited by colchicine or monensin, indicating that cerebroside destined for myelin is not processed through the Golgi apparatus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1984.tb06689.x
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  • 3
    Electronic Resource
    Electronic Resource
    Biochemical Expression of Mosaicism in Female Mice Heterozygous for the Jimpy Gene (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 42 (1984), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Expression of the jimpy gene in heterozygous females was analyzed by measuring galactolipid synthesis in brain during early myelination. Sulfatide labeling in brains of heterozygous females at 13–14 days is decreased to 40–80% that of female littermates who do not carry the jimpy gene. The activities of ceramide galactosyl transferase and cerebroside sulfotransferase and levels of myelin basic protein were similarly depressed. Since the jimpy gene was maintained with the Tabby gene in these studies, the effect of the Tabby gene on these parameters was examined and found to have no effect. These biochemical findings indicate that myelination is retarded in the brains of heterozygous jimpy females during the second week of development. However, at 18 days and thereafter, sulfatide labeling is less reduced, suggesting that the oligodendrocytes in brain attempt to compensate, in agreement with morphologic studies which show that myelin is decreased in brain during early development, but appears normal in adult animals.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1984.tb02704.x
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  • 4
    Electronic Resource
    Electronic Resource
    Kinetics of Entry of P0 Protein into Peripheral Nerve Myelin (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 37 (1981), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Sciatic nerves from 9-day-old rat pups were removed, sliced into 0.4-mm sections, and incubated with [3H]fucose or [14C]glycine precursors. The nerve slice system gave nearly linear incorporation of [3H]fucose as a function of time for 3 h, after an initial lag of ˜30 min for homogenate and ˜60 min for myelin. Incorporation of [3H]fucose at constant specific radioactivity was directly proportional to exogenous fucose levels over the range 3.0 × 10−8m to 1.5 × 10−6m. Analysis of labeled proteins by sodium dodecyl sulfate polyacrylamide gel electrophoresis showed that greater than 50% of labeled glycoprotein was P0, with no other major constituents. This system was used in fucose-chase experiments to determine that a period of ˜20 min elapses between fucosylation and assembly of P0 into myelin. Cycloheximide inhibition of protein synthesis was used to determine that a period of ˜33 min elapses between protein synthesis and appearance of P0 myelin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1981.tb05304.x
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  • 5
    Electronic Resource
    Electronic Resource
    Glycolipids and Transmembrane Signaling in Oligodendroglia (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 605 (1990), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1990.tb42384.x
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  • 6
    Electronic Resource
    Electronic Resource
    Effects of Monensin on Assembly of Po Protein into Peripheral Nerve Myelin (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 39 (1982), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The ionophore monensin has been used in a variety of systems to block secretion of glycoproteins or assembly of glycoproteins into membranes. We examined the effects of monensin on assembly of the Po glycoprotein into PNS myelin, and compared this agent with the glycosylation inhibitor tunicamycin in our system. Sciatic nerves from 9-day-old rat pups were sliced and incubated in vitro. Electron microscopy of the Schwann cells in slices incubated with monensin revealed extensive swelling of the Golgi complex. Incubation with 10−7M monensin inhibited total protein synthesis by about 20% and fucose incorporation into protein about 35%. Following isolation of myelin, proteins were separated by sodium dodecyl sulfate gel electrophoresis. Monensin inhibited the appearance of Po in myelin, while causing its accumulation in a denser membrane fraction. In addition, a slightly faster-migrating species of Po labeled with both [3H]fucose and [14C]glycine was observed in all fractions. Assembly of basic proteins into myelin was not affected. Preincubation with 10 μg/ml tunicamycin for 30 min prior to incubation with [3H]fucose and [14C]glycine for 2 h resulted in a 65% decrease in [3H]fucose incorporation into Po, and the appearance of a new [14C]glycine-labeled peak that migrated in the region of the 23K protein reported by Smith and Sternberger. [3H]Fucose incorporation was inhibited earlier, and to a greater extent, than protein synthesis. Our results show that processing of the Po glycoprotein is sensitive to both monensin and tunicamycin, and that monensin partially blocks assembly of Po into myelin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1982.tb11502.x
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  • 7
    Electronic Resource
    Electronic Resource
    Cerebroside Sulfotransferase in Golgi-Enriched Fractions from Rat Brain (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 38 (1982), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Golgi-enriched fractions were prepared from brainstems of 17-day-old rats by first floating off myelin, then fractionating the remaining pellet by a series of differential and density gradient centrifugations in sucrose. Fractions enriched in Golgi membranes were recovered at 0.46/0.76 m and 0.76/0.87 m interfaces on the final sucrose gradient as indicated by morphology and the biochemical markers thiamine pyrophosphatase and [3H]fucose-labeled glycoprotein. Morphology of the two fractions indicated very little contamination with myelin lamellae; however, the presence of significant levels of 2′, 3′-cyclic nucleotidase in the lighter fraction suggested a contribution from oligodendroglial or myelin-related membranes. Cerebroside sulfotransferase was highly enriched in the lighter Golgi-enriched fraction relative to the denser fraction, the post-34, 880 x g microsomes, and the myelin-like fraction. In contrast, ceramide galactosyl transferase was more evenly distributed among the fractions. Our results show a more highly localized distribution of sulfatide synthesis than of galactocerebroside synthesis, probably in Golgi membranes or oligodendroglia-related membranes with similar properties.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1982.tb10875.x
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  • 8
    Electronic Resource
    Electronic Resource
    Effects of Monensin on Posttranslational Processing of Myelin Proteins (1983)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 40 (1983), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Rat brain slices were incubated with [3H]palmitic acid and [14C]glycine to label the lipid and protein moieties, respectively, of myelin proteolipid protein (PLP). The effects of monensin on posttranslational processing of proteins were examined by measuring the appearance of [14C]glycine- and [3H]palmitate-labeled proteins in myelin and myelin-like fractions. At 0.01 and 0.10 μM, monensin did not appreciably affect total lipid or protein synthesis; higher concentrations caused increased inhibition. Monensin at 0.10 μM markedly decreased the appearance of [14C]glycine-labeled PLP in myelin, but had little effect on the 14C basic proteins or the incorporation of [3H]palmitic acid into total or myelin PLP. The same relative effect was apparent at higher monensin concentrations. In the myelin-like fraction, monensin at 0.10 μM also depressed entry of [14C]glycine into protein comigrating with PLP, and again had no effect on incorporation of [3H]palmitic acid. In addition, monensin increased the [3H]palmitate label associated with two high-molecular-weight proteins in the myelin-like fraction with no concomitant increase in [14C]glycine label.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1983.tb13575.x
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  • 9
    Electronic Resource
    Electronic Resource
    Maintenance of membrane sheets by cultured oligodendrocytes requires continuous microtubule turnover and Golgi transport (1994)
    Springer
    Neurochemical research 19 (1994), S. 631-639 
    Details
    ISSN: 1573-6903
    Keywords: Microtubule turnover ; Golgi transport ; oligodendrocytes ; membrane
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Oligodendrocytes in murine shakeoff cultures elaborate extensive membrane sheets containing networks of microtubules. Several membrane components, including proteolipid protein (PLP) and sulfatide, are transported through the Golgi en route to the plasma membrane or myelin (1,2). This transport is essential for membrane assembly, but its role in continuing maintenance of the sheets is not known. We examined the stability of the membrane sheets following microtubule stabilization with taxol or block of transport into the Golgi with brefeldin A. Within one to three hours, both agents had marked effects on the membrane sheets. While some oligodendrocytes maintained regions of normal membrane sheets, many showed retraction of the sheets, with the majority now exhibiting multiple processes rather than sheets. The distribution of sulfatide, PLP and tubulin in cell bodies, processes and sheets was altered in treated cells, as analyzed by immunocytochemical staining with antibodies to these components. The Golgi apparatus also showed reorganization in the presence of taxol, as visualized by binding of wheat germ agglutinin, a lectin with high affinity for distal Golgi vesicles. All of these effects were reversible when the agents were removed after 3 hours. Thus, maintenance of membrane sheets by oligodendrocytes in culture is a dynamic process, requiring ongoing microtubule turnover and transport of molecules through the Golgi.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00971340
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  • 10
    Electronic Resource
    Electronic Resource
    Analysis of myelin proteolipid protein and F0ATPase subunit 9 in normal andjimpy CNS (1994)
    Springer
    Neurochemical research 19 (1994), S. 1013-1022 
    Details
    ISSN: 1573-6903
    Keywords: Jimpy ; proteolipid protein ; F0 ATPase ; myelin ; neuroglia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Membrane fractions and chloroform-methanol (C-M) extracts ofjimpy (jp) and normal CNS at 17–20 days were examined by immunoblot and sequence analysis to determine whether myelin proteolipid protein (PLP) or DM-20 could be detected in jp CNS. No reactivity was detected in jp samples with several PLP antibodies (Abs) except with one Ab to amino acids 109–128 of normal PLP. Proteins in the immunoreactive bands ∼26 Mr comigrating with PLP were sequenced for the first 10–12 residues. A sequence corresponding to PLP was found in normal CNS, as expected, but not in the band from jp CNS. Our results provide no evidence for an aberrant form of PLP in jp CNS at 17–20 days. This and other studies suggest that the abnormalities in jp brain are not due to toxicity of the mutant jp PLP/DM-20 proteins. Interestingly, a sequence identical to the amino terminus of the mature proton channel subunit 9 of mitochondrial F0 ATPase was detected in the immunoreactive bands ∼26 Mr in both normal and jp samples. This identification was supported by reactivity with an Ab to the F0 subunit and by labeling with dicyclohexylcarbodiimide (DCCD). In contrast to PLP isolated from whole CNS, PLP isolated from myelin was devoid of F0 subunit 9 based on sequence analysis and lack of reactivity with an Ab to the F0 subunit, yet still reacted with DCCD. This finding rules out the possibility that contaminating F0 ATPase gives rise to the DCCD binding exhibited by PLP and confirms the possibility that PLP has proton channel activity, as suggested by Lin and Lees (1,2).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00968711
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