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  • 1
    Electronic Resource
    Electronic Resource
    Localization and targeting of SCG10 to the trans-Golgi apparatus and growth cone vesicles (2000)
    Oxford, UK : Blackwell Science Ltd
    European journal of neuroscience 12 (2000), S. 0 
    Details
    ISSN: 1460-9568
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: SCG10 is a membrane-associated, microtubule-destabilizing protein of neuronal growth cones. Using immunoelectron microscopy, we show that in the developing cortex of mice, SCG10 is specifically localized to the trans face Golgi complex and apparently associated with vesicular structures in putative growth cones. Consistent with this, subcellular fractionation of rat forebrain extracts demonstrates that the protein is enriched in the fractions containing the Golgi apparatus and growth cone particles. In isolated growth cone particles, SCG10 was found to be particularly concentrated in the growth cone vesicle fraction. To evaluate the molecular determinants of the specific targeting of SCG10 to growth cones, we have transfected PC12 cells and primary neurons in culture with mutant and fusion cDNA constructs. Deletion of the amino-terminal domain or mutations within this domain that prevented palmitoylation at cysteines 22 and 24 abolished Golgi localization as well as growth cone targeting, suggesting that palmitoylation of the amino-terminal domain is a necessary signal for Golgi sorting and possibly transport of SCG10 to growth cones. Fusion proteins consisting of the amino-terminal domain of SCG10 and the cytosolic proteins stathmin or glutathione-S-transferase colocalized with a Golgi marker, α-mannosidase II, and accumulated in growth cones of both axons and dendrites. These results reveal a novel axonal/dendritic growth cone targeting sequence that involves palmitoylation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1460-9568.2000.00112.x
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  • 2
    Electronic Resource
    Electronic Resource
    Characterization of a Mouse Serotonin 5-HT3 Receptor Purified from Mammalian Cells (1998)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 70 (1998), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: A serotonin 5-HT3 receptor was functionally expressed to high levels and on a large scale in mammalian cells with the Semliki Forest virus system. Conditions were optimized to maximize detergent solubilization of the receptor, while preserving ligand binding activity. An efficient one-step purification yielding ∼50% of the histidine-tagged 5-HT3 receptor was achieved with immobilized metal ion chromatography. The expressed receptor, in both membranes and purified preparations, exhibited wild-type ligand binding properties, characterized by one class of binding sites. The purity of the receptor was shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, yielding a single band at 65 kDa, and was confirmed by the specific ligand binding activity of ∼5 nmol/mg of protein. Deglycosylation of the receptor reduced the estimated relative molecular mass to 49 kDa. The apparent molecular mass of the functional receptor complex was determined by size exclusion chromatography to be 280 kDa, suggesting that the 5-HT3 receptor is a pentameric homooligomer. The secondary structure of the 5-HT3 receptor as determined by circular dichroism appeared to consist of mainly α-helices (50%) and β-strands (24%), with minor contributions from nonregular structure (9%). The binding of either agonist or antagonist did not alter the secondary structure of the receptor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1998.70020824.x
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  • 3
    Electronic Resource
    Electronic Resource
    Low protein serum-free medium for antibody-production in stirred bioreactors (1989)
    Springer
    Biotechnology letters 11 (1989), S. 455-460 
    Details
    ISSN: 1573-6776
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A chemically defined serum-free medium was modified with respect to protein content by substituting PEG (polyethylen glycol) for BSA-FA (bovine serum albumin fatty acid complex). The outstanding advantage of this low-protein medium is the excellent support of hybridoma-growth and MAb (monoclonal antibody)-production in stirred bioreactors even when inoculated at low cell concentrations. Using this medium, the secreted MAbs were a major part of the total protein. Addition of lipoproteins was in most cases not found to be necessary, and when they were added at higher concentrations even a toxic effect was observed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01026641
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  • 4
    Electronic Resource
    Electronic Resource
    Induction of human IgE synthesis in B cells by mast cells and basophils (1993)
    [s.l.] : Nature Publishing Group
    Nature 365 (1993), S. 340-343 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] HMC-1 is an immature mast cell line expressing several mast cell antigens but not FcsRl (ref. 10). KU812 is an immature basophilic cell line". To identify new cellular mechanisms for the control of IgE production, we tested the ability of these cell lines to induce IgE synthesis in purified B cells ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/365340a0
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  • 5
    Electronic Resource
    Electronic Resource
    Cellcube: A new system for large scale growth of adherent cells (1995)
    Springer
    Biotechnology techniques 9 (1995), S. 725-728 
    Details
    ISSN: 1573-6784
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A new disposable cell culture unit for adherent cell lines, the CellCube, was used to grow a variety of mammalian cell lines. A small unit with 2m2 growth surface area generated up to 4·109 cells. The disposable system consists of a series of polystyrene plates, mounted into a cubical container. A simple construction consisting of a spinner system for medium conditioning, rotameters for gas mixing and a peristaltic pump for medium circulation provided conditions for culture growth.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00159237
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  • 6
    Electronic Resource
    Electronic Resource
    Large scale transient expression with COS cells (1995)
    Springer
    Cytotechnology 18 (1995), S. 183-192 
    Details
    ISSN: 1573-0778
    Keywords: CD40 ; COS ; low protein serum-free medium ; scale up ; stransfection ; transient expression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract We demonstrate here that transient expression with COS cells can be performed at the one litre scale for a period of more than 10 days. Cells grown in T225 flasks were transfected by electroporation, transferred into spinners, and then grown either in suspension or on microcarriers. A daily medium change significantly extented culture life and production time, compared with standard protocols. Concentrations of the product, the secreted fusion protein CD40-Fc, were comparable in microcarrier and suspension culture. Cultures were started in fetal calf serum containing medium and the subsequent production process was performed in a low protein serum free medium which allowed easy downstream processing. 10 litres of supernatant, collected from one transfected batch of cells, yielded 30 mg of purified and biologically active protein. In addition to developing a simplified protocol for generation of cells we also reduced the material (DNA, cuvettes) required for electroporation. Our results show that scale up of transient expression to the litre scale can be successfully acieved. This provides a new tool to generate milligram quantities of protein within weeks of gene cloning.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00767766
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  • 7
    Electronic Resource
    Electronic Resource
    Erratum (1989)
    Springer
    Biotechnology letters 11 (1989), S. 757-758 
    Details
    ISSN: 1573-6776
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01044112
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