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  • 1
    Digitale Medien
    Digitale Medien
    Characterization of Soluble Neural Cell Adhesion Molecule in Rat Brain, CSF, and Plasma (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 59 (1992), S. 0 
    Details
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Abstract: The polypeptide composition and glycosylation of soluble isoforms of neural cell adhesion molecule (NCAM) in developing rat brain, CSF, and plasma were characterized. Soluble NCAM in rat brain consisted of several glycosylated isoforms. The degree of glycosylation was developmentally regulated. After desialylation, four polypeptides of Mr values of ∼ 190,000 (sl), 135,000 (s2), 115,000 (s3), and 110,000 (s4) were observed. Polypeptides si, s2, and s3 were also present in CSF, whereas only s3 and s4 were observed in plasma. Treatment of soluble brain NCAM with N-glycosidase F, which removes N-linked carbohydrates, produced polypeptides of Mr values of ∼ 190,000, 125,000, and 108,000–97,000. The monoclonal antibody OB11, which recognizes an epitope on the cytoplasmic part of transmembrane forms of NCAM, did not react with any of the soluble isoforms. Purified soluble NCAM, consisting mainly of s3, contained an N-terminal sequence identical to that of membrane-associated NCAM. Gel nitration of s3 indicated that it was present as a dimer under the chosen conditions. NCAM-expressing glioma cells adhered specifically to immobilized soluble NCAM. This implies that functionally significant soluble forms of NCAM are present in the extracellular fluid.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1992.tb08321.x
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  • 2
    Digitale Medien
    Digitale Medien
    Equilibrium Binding Analysis of Neural Cell Adhesion Molecule Binding to Heparin (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 52 (1989), S. 0 
    Details
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Abstract: The kinetics of neural cell adhesion molecule (NCAM) binding to heparin were studied in a heparin-Sepharose-based solid-phase binding assay. The observed binding is time dependent and saturable. A binding constant of 5.2 ± 1.4 × 10−8M is observed for binding of newborn rat NCAM to heparin. This is ∼25 times lower than the binding constant determined for newborn rat NCAM homophilic binding. Both Scatchard and Hill plot analyses suggest the presence of only one binding site. Fab' fragments of antibodies to rat NCAM significantly inhibit binding, a result indicating that a specific site on NCAM is involved in binding to heparin. The binding is inhibited by heparin (IC50, ∼5 μg/ml), whereas chondroitin sulfate is a less potent inhibitor (IC50, ∼15 μg/ml).
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1989.tb07283.x
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  • 3
    Digitale Medien
    Digitale Medien
    Heterogeneity of Soluble Neural Cell Adhesion Molecule (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 53 (1989), S. 0 
    Details
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Abstract: Soluble neural cell adhesion molecule (NCAM) from rat brain neuronal cell culture media consists predominantly of a polypeptide of Mr∼ 115,000. Minor amounts of a polypeptide of Mr∼ 180,000 and two inconsistently appearing components of Mr 160,000 and 145,000 are also observed. The Mr 115,000 component is derived from the neuronal membrane NCAM components NCAM-A of Mr 190,000, NCAM-B of Mr 140,000, or both. Thus, as a part of the catabolism of membrane NCAM-A plus -B, a minor fraction is posttranslationally cleaved and recovered in the media as discernible soluble NCAM polypeptides. The half-life of membrane NCAM-A plus -B is 〈24 h. Astrocyte culture media contains a predominant soluble NCAM component of Mr 120,000 derived from membrane-associated NCAM-C. A close comparison of deglycosylated soluble NCAM from astrocyte and neuronal cultures showed a small but consistent difference in Mr, a result suggesting that different NCAM polypeptides are released from the membrane of neurons and astrocytes. In contrast to the Mr 115,000-120,000 NCAM polypeptides, the Mr 180,000 polypeptide from neuronal culture media does not seem to be derived from membrane-attached NCAM and may therefore represent a secreted NCAM isoform
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1989.tb08527.x
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  • 4
    Digitale Medien
    Digitale Medien
    Enzyme-Linked Immunosorbent Assay of the D2-Glycoprotein (1983)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 41 (1983), S. 0 
    Details
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Abstract: D2 is a glycoprotein enriched in neuronal membranes and probably involved in intercellular adhesion. An immunochemical relationship between D2 and the neuronal cell adhesion molecule from chick has been demonstrated. Changes in D2 concentration in human body fluids correlate to certain neurological diseases.We here report the purification of the D2 membrane proteins from fetal and adult human brain and the demonstration of physicochemical differences between the two proteins. Enrichments of 133 times (fetal D2) and 350 times (adult D2) were found. Specific rabbit antisera against the purified D2 proteins were produced, and this enabled the setting up of an enzyme-linked immunosorbent assay for D2 quantification in human brain extracts, cerebrospinal fluids, sera, and amniotic fluids.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1983.tb04750.x
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  • 5
    Digitale Medien
    Digitale Medien
    Quantification of the D2-Glycoprotein in Amniotic Fluid and Serum from Pregnancies with Fetal Neural Tube Defects (1983)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 41 (1983), S. 0 
    Details
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Abstract: D2 is a glycoprotein existing in both membrane-bound and soluble forms. Employing a specific rabbit antibody against purified human brain D2, we developed an enzyme-linked immunosorbent assay (ELISA) for the quantification of D2 and applied it to amniotic fluids from 87 normal and 36 pathological pregnancies. With a cut-off point of 150 ng D2/ml, no false positive D2 values were obtained in any of the amniotic fluids from normal fetuses, although the alpha-fetoprotein concentrations were slightly increased in 13 cases. No false negative D2 values were found in any of the 18 investigated amniotic fluids from fetuses with anencephaly. Of 8 amniotic fluids from fetuses with spina bifida, 2 false negative D2 values were found. No false negative alphafetoprotein values were found in any of the cases with neural tube defects in this study. In 10 amniotic fluids from fetuses with other malformations, 5 samples showed raised D2 concentrations. The D2 level in sera from 10 women carrying normal fetuses and 16 women carrying malformed fetuses was also determined, but no statistically significant difference in D2 level was found in the pathological sera when compared with normal sera. It was concluded that the determination of D2 concentrations in amniotic fluid by means of the D2-ELISA may be used as an additional test in the screening of fetal malformations in early pregnancy.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1983.tb04751.x
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  • 6
    Digitale Medien
    Digitale Medien
    ANTIGEN-ANTIBODY CROSSED ELECTROPHORESIS OF RAT BRAIN SYNAPTOSOMES AND SYNAPTIC VESICLES: CORRELATION TO WATER-SOLUBLE ANTIGENS FROM RAT BRAIN (1974)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 22 (1974), S. 0 
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    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: —Antigen-antibody crossed electrophoresis has been applied to the study of rat brain synaptosomes and synaptic vesicles. Several antigens could be visualized. By comparison with previously describéd water-soluble antigens from rat brain, some of the antigens in the synaptosome and the synaptic vesicle preparations were identified; among these were antigens which have been determined as brain-specific. Furthermore, the antisera against the two subcellular fractions were compared with the anti-serum against water-soluble antigens from rat brain.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1974.tb04330.x
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  • 7
    Digitale Medien
    Digitale Medien
    ShcA regulates neurite outgrowth stimulated by neural cell adhesion molecule but not by fibroblast growth factor 2: evidence for a distinct fibroblast growth factor receptor response to neural cell adhesion molecule activation (2004)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 91 (2004), S. 0 
    Details
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Homophilic binding in trans of the neural cell adhesion molecule (NCAM) mediates adhesion between cells and leads, via activation of intracellular signaling cascades, to neurite outgrowth in primary neurons as well as in the neuronal cell line PC12. NCAM mediates neurite extension in PC12 cells by two principal routes of signaling: NCAM/Fyn and NCAM/fibroblast growth factor receptor (FGFR), respectively. Previous studies have shown that activation of mitogen-activated protein kinases is a pivotal point of convergence in NCAM signaling, but the mechanisms behind this activation are not clear. Here, we investigated the involvement of adaptor proteins in NCAM and fibroblast growth factor 2 (FGF2)-mediated neurite outgrowth in the PC12-E2 cell line. We found that both FGFR substrate-2 and Grb2 play important roles in NCAM as well as in FGF2-stimulated events. In contrast, the docking protein ShcA was pivotal to neurite outgrowth induced by NCAM, but not by FGF2, in PC12 cells. Moreover, in rat cerebellar granule neurons, phosphorylation of ShcA was stimulated by an NCAM mimicking peptide, but not by FGF2. This activation was blocked by inhibitors of both FGFR and Fyn, indicating that NCAM activates FGFR signaling in a manner distinct from FGF2 stimulation, and regulates ShcA phosphorylation by the concerted efforts of the NCAM/FGFR as well as the NCAM/Fyn signaling pathway.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.2004.02772.x
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  • 8
    Digitale Medien
    Digitale Medien
    BRAIN-SPECIFIC ANTIGENS IN THE QUAKING MOUSE DURING ONTOGENY (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 27 (1976), S. 0 
    Details
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Abstract— By means of crossed Immunoelectrophoresis the concentrations of 7 brain-specific antigens have been investigated during the ontogenic development of normal and Quaking mice. Two proteins, the glial fibrillary acidic protein and the brain-specific membrane protein D5 were found to be strongly increased in mutant brains. The synaptosomal antigen synaptin (Cl), the 14-3-2 protein of neuronal cytoplasm, and the neuronal membrane antigens D1, D2 and D3 were all present at normal levels in mutant brains.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1976.tb05153.x
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  • 9
    Digitale Medien
    Digitale Medien
    Modulation of the homophilic interaction between the first and second Ig modules of neural cell adhesion molecule by heparin (2005)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 95 (2005), S. 0 
    Details
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: The second Ig module (IgII) of the neural cell adhesion molecule (NCAM) is known to bind to the first Ig module (IgI) of NCAM (so-called homophilic binding) and to interact with heparan sulfate and chondroitin sulfate glycoconjugates. We here show by NMR that the heparin and chondroitin sulfate-binding sites (HBS and CBS, respectively) in IgII coincide, and that this site overlaps with the homophilic binding site. Using NMR and surface plasmon resonance (SPR) analyses we demonstrate that interaction between IgII and heparin indeed interferes with the homophilic interaction between IgI and IgII. Accordingly, we show that treatment of cerebellar granule neurons (CGNs) with heparin inhibits NCAM-mediated outgrowth. In contrast, treatment with heparinase III or chondroitinase ABC abrogates NCAM-mediated neurite outgrowth in CGNs emphasizing the importance of the presence of heparan/chondroitin sulfates for proper NCAM function. Finally, a peptide encompassing HBS in IgII, termed the heparin-binding peptide (HBP), is shown to promote neurite outgrowth in CGNs. These observations indicate that neuronal differentiation induced by homophilic NCAM interaction is modulated by interactions with heparan/chondroitin sulfates.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.2005.03338.x
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  • 10
    Digitale Medien
    Digitale Medien
    An NCAM-derived FGF-receptor agonist, the FGL-peptide, induces neurite outgrowth and neuronal survival in primary rat neurons (2004)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 91 (2004), S. 0 
    Details
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: The Neural Cell Adhesion Molecule (NCAM) plays a crucial role in development of the central nervous system regulating cell migration, differentiation and synaptogenesis. NCAM mediates cell–cell adhesion through homophilic NCAM binding, subsequently resulting in activation of the fibroblast growth factor receptor (FGFR). NCAM-mediated adhesion leads to activation of various intracellular signal transduction pathways, including the Ras-mitogen activated protein kinase (MAPK) and the phosphatidylinositol-3-kinase (PI3K)-Akt pathways. A synthetic peptide derived from the second fibronectin type III module of NCAM, the FGL peptide, binds to and induces phosphorylation of FGFR without prior homophilic NCAM binding. We here present evidence that this peptide is able to mimic NCAM heterophilic binding to the FGFR by inducing neuronal differentiation as reflected by neurite outgrowth through a direct interaction with FGFR in primary cultures of three different neuronal cell types all expressing FGFR subtype 1: dopaminergic, hippocampal and cerebellar granule neurons. Moreover, we show that the FGL peptide promotes neuronal survival upon induction of cell death in the same three cell types. The effects of the FGL peptide are shown to depend on activation of FGFR and the MAPK and PI3K intracellular signalling pathways, all three kinases being necessary for the effects of FGL on neurite outgrowth and neuronal survival.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.2004.02779.x
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