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At least 415 records · Page 23Linked to original sources
PubMed1976

Effect of 5-bromo-2'-deoxyuridine or cytosine-B-D-arabinofuranoside hydrochloride on myelination in newborn rat cerebellum cultures following removal of myelination inhibiting antiserum to whole cord or cerebroside.

Myelination was inhibited in cultures of newborn rat cerebellum by exposure to antisera prepared by injecting rabbits with whole guinea pig spinal cord or cerebrosixde mixed with bovine serum albumin. At 15 days in vitro (DIV), when 90-100% of our control cultures were myelinated, antiserum inhibited cultures were washed and refed routine culture medium or medium containing 5-bromo-2'-deoxyuridine (BUdR) or cytosine-B-D-arabinofuranoside hydrochloride (ara-C) in concentrations previously shown to inhibit myelination in our system. The disinhibited cultures myelinated within 2-5 days of removal of antiserum regardless of the presence of BUdR or ara-C. The evidence suggests that the myelin-forming oligodendrocytes do not undergo cell division before myelination during disinhibition from antiserum. In addition, cultures exposed to BUdR on 5-7 DIV in the presence of antiserum and disinhibited at 10 DIV did not have myelinated axons as observed by light microscopy at 15 DIV. Thus, the BUdR sensitive oligodendrocyte division remained intact in antiserum inhibited cultures. We conclude that the antisera inhibit myelin formation without interrupting the pattern of cell division or the covert differentiation of oligodendrocytes.

Animals↗
PubMed1988

Interaction of 1-anilinonaphthalene 8-sulfonic acid with interfaces containing cerebrosides, sulfatides and gangliosides.

The fluorescence lifetime, quantum yield and emission spectra of 1-anilinonaphthalene 8-sulfonic acid (ANS) associated with interfaces of pure dipalmitoylphosphatidylcholine or its mixtures with phosphatidylserine, galactosylceramide, sulfatide or gangliosides GM1 and GD1a were studied at low and high ionic strength. Modification of the molecular organization of the lipid interfaces in the presence of the probe was also studied with mixed lipid monolayers. ANS has little affect on the intermolecular packing of the lipids but influences their surface potential, consistent with a location of ANS in the polar head group region of the interface. ANS senses a more polar microenvironment when associated with interfaces containing anionic glycosphingolipids at low ionic strength but, except for interfaces containing phosphatidylserine, it detects approximately the same polarity for neutral or anionic interfaces in 0.25 M NaCl.

Anilino Naphthalenesulfonates↗
PubMed1989

Interaction and fusion of unilamellar vesicles containing cerebrosides and sulfatides induced by myelin basic protein.

The effects of myelin basic protein on the aggregation, lipid bilayer merging, intercommunication of aqueous compartments and leakage of small unilamellar vesicles of egg phosphatidylcholine containing different proportions of galactocerebroside and sulfatide were investigated. This was performed employing light scattering, absorbance changes and fluorescence assays (resonance energy transfer, Terbium/dipicolinic acid assay and carboxyfluorescein release). The apposition of membranes rapidly induced by myelin basic protein is enhanced by sulfatide but reduced by galactocerebroside compared to vesicles of egg phosphatidylcholine alone. On the other hand, the presence of either glycosphingolipid in the membrane interferes with the induction by myelin basic protein of lipid bilayer merging, subsequent fusion and changes of the membrane permeability. Our results support an important modulation by sulfatide and galactocerebroside on the interactions among membranes induced by myelin basic protein, depending on the relative proportions of the glycosphingolipids and phosphatidylcholine.

Cerebrosides↗
PubMed1987

Assay for cerebroside sulfate (sulfatide) sulfatase in cultured skin fibroblasts with the natural activator protein.

A simple procedure was developed to assay the ability of arylsulfatase A in extracts of cultured skin fibroblasts to degrade the natural substrate, sulfatide, in the presence of the physiological activator protein but without detergents. Inhibitory substances were removed by dialysis and by batch-wise ion-exchange chromatography. The enzyme recoveries during purification were monitored with a newly developed method that employs the chromogenic substrate 4-nitrocatecholsulfate at an incubation temperature of 4 degrees C. The residual sulfatidase activities determined with this procedure in fibroblasts from patients with various forms of MLD correlated well with the severity of the disease.

Cells, Cultured↗