Glee Yorke

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Bovine brain gangliosides were applied to primary and established neuronal cultures to examine the role of gangliosides in neuronal development. Media containing gangliosides enhanced the degree of axonal elongation exhibited by sensory ganglia neurons and increased the length and number of Neuro-2a neuroblastoma cell processes. Ganglioside-supplemented(More)
Gangliosides were previously reported to induce neuritogenesis in primary neuronal cultures and in some neurally derived cell lines. Because isolated gangliosides usually contain variable quantities of peptides, we investigated the possibility that neurite-stimulating activity could be caused by these contaminants. Ganglioside preparations from bovine brain(More)
The 4 major ganglioside species, GM1, GD1a, GD1b and GT1b (200 micrograms/ml), were tested individually for the ability to stimulate neuronal trophic responses. The growth parameters measured were: morphologic changes, quantitated by computer-assisted morphometry of neurite length and number per soma, and metabolic changes, indicated by alterations in(More)
The effect of ganglioside GM1 on components of the neuronal cytoskeleton was studied in Neuro-2a neuroblastoma cells using immunofluorescent, immunogold-labeled, and Western-blot analysis. Exposure of cells to GM1 for 24 h resulted in an increased microtubular network and level of tubulin, a redistribution of MAP2 immunoreactivity from perikarya to distal(More)
Primary cell cultures prepared from chick embryonic skeletal muscle and the rat myogenic line L6 were examined morphologically and biochemically during several stages of development. The L6 cells were cultured to provide three morphologically distinct populations: prefusion, postfusion, and a subclone of cells that did not fuse even at high density.(More)
Our previous immunofluorescence studies on neurons have demonstrated the presence of myosin in regions of neurons which contained actin. To determine if a system similar to the troponin complex of striated muscle is present in neurons, antibody shown to be specific for the calcium-binding component of troponin (troponin-C) was applied to cultures of(More)
Chymase isolated from rat skeletal muscle tissue was compared with other proteinases in rat muscle that hydrolyse chymase substrates. These enzymes were purified from the 100,000 x g supernatant of hind limb rat muscles homogenized with 0.15 M NaCl-20 mM phosphate buffer, pH 7.2. A metallproteinase (MMP-7-ase) and a serine proteinase (ATN-ase) were(More)