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  • 1
    Electronic Resource
    Electronic Resource
    Purification, immunological characterization and cDNA cloning of a 47 kDa glycoprotein secreted by carrot suspension cells (1995)
    Springer
    Plant molecular biology 27 (1995), S. 901-910 
    Details
    ISSN: 1573-5028
    Keywords: carrot ; cell wall ; suspension culture ; secreted glycoprotein ; root ; nodulin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A 47 kDa glycoprotein, termed EP4, was purified from carrot cell suspension culture medium. An antiserum raised against EP4 also recognized a protein of 45 kDa that was ionically bound to the cell wall. EP4 was detected in culture media from both embryogenic and non-embryogenic cell lines and was found to be secreted by a specific subset of non-embryogenic cells. Secretion of the 47 kDa glycoprotein by embryogenic cells was not evident. The 45 kDa cell wall-bound EP4 protein was specific for non-embryogenic cells and was shown by immunolocalization to occur in the walls of clustered cells, with the highest levels in the walls separating adjacent cells. In seedlings, EP4 proteins were mainly found in roots. EP4 cDNA was cloned by screening a cDNA library with an oligonucleotide derived from an EP4 peptide sequence. The EP4 cDNA sequence was found to be 55% homologous to ENOD8, an early nodulin gene from alfalfa.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00037018
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Coordinate expression of antibody subunit genes yields high levels of functional antibodies in roots of transgenic tobacco (1994)
    Springer
    Plant molecular biology 26 (1994), S. 1701-1710 
    Details
    ISSN: 1573-5028
    Keywords: Antibody ; coordinated expression ; genetic engineering ; protein assembly ; root ; secretion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract To explore the feasibility of employing antibodies to obtain disease resistance against plant root pathogens, we have studied the expression of genes encoding antibodies in roots of transgenic plants. A model monoclonal antibody was used that binds to a fungal cutinase. Heavy and light chain cDNAs were amplified by PCR, fused to a signal sequence for secretion and cloned behind CaMV 35S and TR2′ promoters in a single T-DNA. The chimeric genes were cloned both in tandem and in a divergent orientation. The roots of tobacco plants transformed with these constructs produced antibodies that were able to bind antigen in an ELISA. Immunoblotting showed assembly to a full-size antibody. In addition, a F(ab′)2-like fragment was observed, which is probably formed by proteolytic processing. Both antibody species were properly targeted to the apoplast, but the full-size antibody was partially retained by the wall of suspension cells. The construct with divergent promoters showed a better performance than the construct with promoters in tandem. It directed the accumulation of functional antibodies to a maximum of 1.1% of total soluble protein, with half of the plants having levels higher than 0.35%. The high efficiency of this construct probably results from coordinated and balanced expression of light and heavy chain genes, as evidenced by RNA blot hybridization.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00019485
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  • 3
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    Switch in FGF signalling initiates glial differentiation in the Drosophila eye (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-07-15
    Description: The formation of a complex nervous system requires the intricate interaction of neurons and glial cells. Glial cells generally migrate over long distances before they initiate their differentiation, which leads to wrapping and insulation of axonal processes. The molecular pathways coordinating the switch from glial migration to glial differentiation are largely unknown. Here we demonstrate that, within the Drosophila eye imaginal disc, fibroblast growth factor (FGF) signalling coordinates glial proliferation, migration and subsequent axonal wrapping. Glial differentiation in the Drosophila eye disc requires a succession from glia-glia interaction to glia-neuron interaction. The neuronal component of the fly eye develops in the peripheral nervous system within the eye-antennal imaginal disc, whereas glial cells originate from a pool of central-nervous-system-derived progenitors and migrate onto the eye imaginal disc. Initially, glial-derived Pyramus, an FGF8-like ligand, modulates glial cell number and motility. A switch to neuronally expressed Thisbe, a second FGF8-like ligand, then induces glial differentiation. This switch is accompanied by an alteration in the intracellular signalling pathway through which the FGF receptor channels information into the cell. Our findings reveal how a switch from glia-glia interactions to glia-neuron interactions can trigger formation of glial membrane around axonal trajectories. These results disclose an evolutionarily conserved control mechanism of axonal wrapping, indicating that Drosophila might serve as a model to understand glial disorders in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Franzdottir, Sigridur Rut -- Engelen, Daniel -- Yuva-Aydemir, Yeliz -- Schmidt, Imke -- Aho, Annukka -- Klambt, Christian -- England -- Nature. 2009 Aug 6;460(7256):758-61. doi: 10.1038/nature08167. Epub 2009 Jul 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Neurobiologie, Universitat Munster, Badestr. 9, D-48149 Munster, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19597479" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/metabolism ; *Cell Differentiation ; Cell Movement ; Cell Proliferation ; Drosophila Proteins/metabolism ; Drosophila melanogaster/cytology/genetics/growth & development/*metabolism ; Eye/*cytology/growth & development/innervation/metabolism ; Fibroblast Growth Factors/*metabolism ; Guinea Pigs ; Ligands ; Neuroglia/*cytology/*metabolism ; *Signal Transduction
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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