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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Experimental brain research 41 (1981), S. 271-279 
    ISSN: 1432-1106
    Keywords: Cerebellar enolases ; Neuronal marker ; Astrocytic marker ; Immunohistology
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary A comparative immunohistological study of the neurone-specific γγ enolase and αα enolase, demonstrates the exclusive neuronal localization of γγ enolase and its absence from glial cells. In contrast, αα enolase is located in astroglial cells. The validity of γγ enolase as a neuronal marker and αα enolase as an astrocytic marker, is confirmed both by a double labelling technique, using antibodies to αα and to γγ revealed with fluorescence or peroxidase in the same tissue sections, and by immunoelectronmicroscopy.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 42 (1984), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Quantitative and qualitative modifications of the specific binding sites for [3H]quinuclidinyl benzylate (QNB), a muscarinic antagonist, were studied during rat cerebellar postnatal development. Specific binding sites for QNB (QNB-sbs), regardless of whether they correspond to muscarinic acetylcholine receptors, are present with the highest density in the archicerebellar cortex, but the total amount per region is about the same in the archi-, paleo-, and neocerebellar cortex regions. Large amounts of QNB-sbs are also present in a cerebellar fraction including central white matter and deep cerebellar nuclei. QNB-sbs are low but present at birth and then accumulate during ontogenic development according to a curve which duplicates, with a delay of a few days, the curve of DNA accumulation. Dissection studies indicated that this curve does not depend on the preferential localization of QNB-sbs in a specific cerebellar region nor on the particular development of this region. The similarity of the QNB-sbs and the DNA developmental curves might indicate that the QNB-sbs are present on granule cells; however, a comparative analysis of the data in the literature suggests that a great many QNB-sbs are located on the Purkinje cell dendrites in the molecular layer, where all or some of them might correspond to the ex-trajunctional muscarinic acetylcholine receptor detected there by electrophysiology. It would appear that only a small percentage of cerebellar QNB-sbs corresponds to the cholinergic synapses present in cerebellar cortex; hence, the question of muscarinic receptors in the cerebellum should be re-examined.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Neurochemical research 7 (1982), S. 349-362 
    ISSN: 1573-6903
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A comparison is made of the immunohistochemistry at the ultrastructural level of three monoclonal antibodies directed against surface components of CNS cells. Hybridomas secreting these antibodies were obtained from two cell fusions of a rat myeloma cell line and immune splenocytes derived from rats immunized either with primary mouse brain cultured cells or membrane components. In cultures one antibody, anti-BSP-2 (Brain Surface Protein-2), was preferentially directed against neurones while another, anti-BSP-3 (Brain Surface Protein-3), preferentially labeled astrocytes. In mouse cerebellar sections, both labeled the surface of Purkinje cells, granule cells and astrocytes. In addition a cytoplasm localization was apparent in granule cells and astrocytes. Another antibody anti-MESA-1 (Mouse Endothelial Surface Antigen-1) reacted exclusively with the surface of endothelial cells lining blood vessels. These data are discussed with reference to the biochemical nature of the corresponding antigens and to known glycoproteins of neural cell membranes.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Journal of neurocytology 9 (1980), S. 783-798 
    ISSN: 1573-7381
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The ultrastructural localization of the neuron-specific enolase (14-3-2 protein) has been investigated in the cerebellum of the adult rat using the indirect antibody immunohistochemical method. The protein was found exclusively in neurons: perikaryal cytoplasm, axons and dendrites were labelled while nuclei were not. Reaction product was found to be attached to intracytoplasmic membranes, the surface membranes of mitochondria and microtubules in addition to its dispersion as a flocculent material throughout the cytoplasm. All classes of cerebellar neurons were found to be labelled though large variations in the level of labelling between different types of neuron were noted. Purkinje cells appeared to have a much lower cytoplasmic concentration of this protein than other neurons.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Journal of neurocytology 9 (1980), S. 637-646 
    ISSN: 1573-7381
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The distribution of the different types of glial cell in adult rat cerebellar cortex and in the underlying white matter was studied by immunohistology with a specific immune serum raised against form II of carbonic anhydrase, a specific marker for oligodendrocytes in rat cerebellum and an immune serum raised against glial fibrillary acidic protein, a specific astrocyte marker. The cellular specificity of each marker was confirmed by experiments in which the two antigens were revealed in the same cerebellar section. The unequivocal identification, with the optical microscope, of the different glial cell types allowed also a tentative estimation of the number of oligodendrocytes and astrocytes, in relation to Purkinje cells.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Journal of neurocytology 17 (1988), S. 485-498 
    ISSN: 1573-7381
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Intense and specific immunostaining of oligodendrocytesin vivo has been obtained for the first time using antibodies to galactocerebroside. We have examined the differentiation of oligodendrocytes in normal mice and then compared their differentiation to the myelin-deficient mouse jimpy, using immunoperoxidase, immunogold and immunofluorescence labelling techniques. We also compared staining for galactocerebroside with staining obtained using antibodies to myelin basic protein, carbonic anhydrase II, 2′, 3′-cyclic nucleotide 3′-phosphohydrolase and proteolipid protein. The results of this comparative study confirm previous tissue culture studies and show that galactocerebroside is specific for oligodendrocytesin situ. As in tissue culture, galactocerebroside is one of the earliest oligodendrocyte markers to be expressed, making it an important marker for studying the differentiation of this cell type. The shape of oligodendrocytesin situ changes distinctly with time, shifting from an early stellate form with numerous spidery processes to a cell with a few processes radiating from the perikaryon. These morphological changes are observed for both normal and jimpy mice and they parallel those describedin vitro. Oligodendrocytes in jimpy mice express most myelin markers, but the staining within the cells is generally less intense than in normal oligodendrocytes and the antigens are restricted to the cell body and processes without being incorporated into myelin sheaths. Quantification of the number of oligodendrocytes stained for galactocerebroside in normal and jimpy mice show that their number is not reduced in the corpus callosum and cerebellum during the first 2 weeks postnatal. This finding shows that many cells in jimpy mice which were considered to be unclassifiable by the application of morphological criteria have, in fact, differentiated to the stage where they are galactocerebroside-positive.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1573-7381
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary This study characterizes jimpy oligodendrocyte-enriched secondary cultures isolated from 10–12 daysin vitro primary glial cell cultures derived from 1–2-day-old jimpy mouse brains. Proliferation of defective oligodendrocytes was carefully investigated with regard to the expression of myelin basic protein and proteolipid protein and their respective mRNAs. Less than 5% of contaminating astrocytes (GFAP+ cells) were usually present. The identity of jimpy oligodendrocytes was confirmed using an antibody directed against a peptide from the wild type proteolipid protein C-terminal sequence for immunocytochernistry and an oligonucleotide complementary to mRNA derived from exon 5 of the proteolipid protein gene forin situ hybridization. Both the antibody and the probe recognize only normal oligondendrocytes while jimpy oligodendrocytes always remain unstained. Proteolipid protein in normal and jimpy oligodendrocytes was detected with antibody recognizing normal and mutated forms. Between 80 and 95% of the cells in normal and jimpy cultures at 2 and 4 daysin vitro in secondary cultures express myelin basic protein and proteolipid protein and their respective mRNAs. The percentage of oligodendrocytes (PLP+ or MBP+) in S phase of the cell cycle was 7–10% for both normal and jimpy oligodendrocytes. This contrasts with thein vivo situation where the proliferation rate of oligodendrocytes in jimpy brains is higher than in normal brains. In addition, jimpy oligodendrocytes remain unresponsive to basic fibroblast growth factor treatment while a similar treatment stimulates the proliferation of normal oligodendrocytes.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular histology 13 (1981), S. 137-148 
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Immunohistochemical methods were used to study in the optical and electron microscopes the localization of the so-called ‘non-neuronal enolase’ (the αα-isoenzyme) in adult mouse cerebellum. Three separate methods, including a novel modification involving sequential incubation with biotin-conjugated sheep anti-rabbit serum and avidin-conjugated peroxidase to reveal tissue-bound specific antibody, gave similar results. The enolase was found exclusively in astrocytes: astrocyte perikaryal cytoplasm and processes were heavily labelled and nuclei were frequently stained. The extensive network of astrocyte processes in the granular layer and white matter and the Bergmann fibres in the molecular layer are readily visualized by these methods. Neither neurones nor oligodendrocytes were found to be labelled. The results are discussed in relation to the possible existence of a hybrid form of the enolase and the biochemistry of cerebellar glial cells.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular histology 12 (1980), S. 473-483 
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The cellular and intracellular distribution of carbonic anhydrase isozyme II in rat cerebellum has been investigated with the electron microscope by the indirect antibody immunohistochemical technique. Unequivocal evidence is presented supporting the view that this enzyme is exclusively localized in oligodendrocytes. Myelin does not appear to contain detectable amounts of carbonic anhydrase though it is present in oligodendrocyte processes and in the layer of oligodendrocyte cytoplasm frequently seen to coat the external surface of myelinated fibres. The immune precipitate is found to be confined to the cytosol and the cytosolic surfaces of intracellular membranes. The data are discussed in relation to the possible function of the enzyme and the role of oligodendrocytes in the central nervous system.
    Type of Medium: Electronic Resource
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