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  • 1
    Digitale Medien
    Digitale Medien
    Isolation and Immunohistochemical Localization of a Chondroitin Sulfate Proteoglycan from Adult Rat Brain (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 51 (1988), S. 0 
    Details
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Abstract: A chondroitin sulfate proteoglycan called PGM 1 has been isolated from the particulate fraction of adult rat forebrain. Delipidation of the material, solubilization of proteoglycans in guanidinium chloride, precipitation at low ionic strength, and final extraction at pH 5.0 were used for its isolation. Proteoglycans were subjected to further purification by diethylaminoethyl-cellulose chromatography. Individual components were separated by gel filtration. PGM 1 appeared to be a high-molecular-weight chondroitin sulfate proteoglycan, capable of strong interaction with hy-aluronic acid. It was finally isolated by gel filtration on Ultrogel AcA 22 in the presence of 4 M guanidinium chloride. Monospecific antibodies obtained in rabbits against the purified molecule did not cross-react with other brain proteoglycans. Immunocytochemical techniques revealed an almost unique association of this compound with axons, particularly those known to contain neurofilaments. However, not all these axons and all parts of these axons contained PGM 1. This component was not detectable in liver, intestine, spleen, kidney, lung, heart, skin, hair, lens, and muscle, a finding suggesting a specificity for the nervous tissue. This component is expressed in neural cell cultures. Despite the preservation of the neuronal specificity, it seems to lose its specific axonal localization in vitro.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1988.tb01796.x
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  • 2
    Digitale Medien
    Digitale Medien
    Endogenous Lectin Cerebellar Soluble Lectin Involved in Myelination Is Absent from Nonmyelinating Schwann Cells (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 58 (1992), S. 0 
    Details
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Abstract: In the sciatic nerve, two major classes of Schwann cells are present which differ in their capability to produce myelin. Myelinating Schwann cells surround most of the axons with the formation of a typical myelin sheath. Nonmyelinating Schwann cells serve to insulate individual axons without formation of myelin. These dissimilarities between the two types of Schwann cells provided an interesting model for studying mechanisms underlying myelination and the formation of contacts between axons and myelinating cells. It is demonstrated here that the endogenous lectin cerebellar soluble lectin (CSL), implicated in myelin stabilization and in formation of contact between axon and myelinating cells in the CNS and in the sciatic nerve, is undetectable in nonmyelinating Schwann cells. In contrast, most axons surrounded by these cells contained the major axonal glycoprotein ligand of CSL, a 31-kDa glycoprotein which is present in large amounts. The possible relationship between the presence of CSL in Schwann cells and their capacity to interact with axons and to produce myelin are discussed.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1992.tb10052.x
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  • 3
    Digitale Medien
    Digitale Medien
    The Endogenous Lectin Cerebellar Soluble Lectin and Its Ligands in Central Nervous System Myelin of Myelin-Deficient (mld) Mutant Mice (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 56 (1991), S. 0 
    Details
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Abstract: The myelin-deficient (mld) mutation is an autosomal recessive mutation in the murine CNS exhibiting severe hypomyelination. The primary defect results in a drastic reduction of myelin basic protein synthesis caused by a duplication of the myelin basic protein gene with partial inversion of the upstream gene copy. The severe deficit of myelin basic protein is responsible for the absence of the major dense line but cannot explain the heterogeneity of myelin compaction found in mid. We have tested the hypothesis that the endogenous cerebellar soluble lectin (CSL) and/or its endogenous glycoprotein ligands could be involved in myelin abnormalities in the dysmyelinating mutant, mld. Immunocytochemical and immunoblotting techniques showed that the CSL level was not reduced significantly in the mld mutant. Furthermore, two ligands of CSL, the myelin-associated glycoprotein and an axonal glycoprotein, with a relative molecular mass of 31 kDa, were not decreased in level in the purified myelin fraction isolated from mld mice. In contrast, three minor glycoprotein ligands of CSL of relative molecular mass of 23, 18, and 16 kDa were greatly reduced in content. The reduced concentration of these low-molecular-mass glycoproteins in mld myelin suggests that they are constituents of compact myelin. Furthermore, the observation that CSL is specifically localized in vivo in regions where mld myelin is more compact and absent from regions devoid of myelin compaction may suggest that the endogenous CSL lectin, as well as its minor glycoprotein ligands, plays a role in the stabilization of the myelin sheath.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1991.tb08169.x
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  • 4
    Digitale Medien
    Digitale Medien
    Epidermal Growth Factor Enhances the Expression of an Endogenous Lectin in Aggregating Fetal Brain Cell Cultures (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: Aggregating cell cultures prepared from fetal rat telencephalon express the two subunits [cerebellar soluble lectins (CSL) 1 and 2] of a soluble, mannose-specific endogenous lectin (CSL) in a development-dependent manner. Increased CSL synthesis was found at an early postmitotic stage as well as during the period of maximal myelination. Repet-tive treatment of early cultures with epidermal growth factor EGF, 3 nM) caused a great stimulation of CSL biosynthesis. Immunocytochemical studies revealed particularly intense CSL-specific staining in small, EGF-responsive cells, presumably glial cells. Large quantities of CSL-immunoreactive material were found also in the extracellular space and on the external side of the plasma membrane, indicating abundant release of CSL. The present findings suggest that EGF or EGF-related factors in the brain are able to regulate the expression of an endogenous lectin, affecting brain ontogeny.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1989.tb08535.x
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  • 5
    Digitale Medien
    Digitale Medien
    Glycoproteins and lectins in cell adhesion and cell recognition processes (1992)
    Springer
    Journal of molecular histology 24 (1992), S. 791-804 
    Details
    ISSN: 1573-6865
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin
    Notizen: Summary The discovery of endogenous lectins having specific and high affinity for the carbohydrate portions of glycoproteins has opened up new directions in the field of cell adhesion and cell recognition. Two endogenous lectins, termed as CSL and R1, initially isolated from the rat cerebellum and having a wide distribution in mammalian tissues, have been shown to participate in essential mechanisms of cell adhesion. The membrane-bound lectin R1 seems to be involved in transient recognition between neuronal cells, followed by elimination of the glycoprotein ligands at the surface of the recognized cell. In contrast, CSL is a molecule involved in adhesion between various normal or transformed cells since it participates in the formation of tight junctions. The glycoprotein ligands recognized with higher affinity by these two lectins seem to possess a special structure which defines a sub-class of oncofetal HNK-1 glycans. The over-expression of the glycoprotein ligands of these lectins in most transformed cells provides new tools for understanding the underlying mechanism of malignant transformation as well as the generation of signals through cell adhesion.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01046351
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  • 6
    Digitale Medien
    Digitale Medien
    Endogenous lectin CSL is present on the membrane of cilia of rat brain ependymal cells (1988)
    Springer
    Journal of neurocytology 17 (1988), S. 745-751 
    Details
    ISSN: 1573-7381
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary An endogenous brain lectin, with a great affinity for oligomannosidic glycans, called CSL (for ‘cerebellar soluble lectin’), was detected on the surface of the cilia of ependymal cells both in cultures andin vivo. The lectin is not synthesized by the ependymal cells themselves.In vivo it is neither found in cerebrospinal fluid nor in cells of the choroid plexus. Probably, lectin CSL is produced by subependymal astrocytic cells. The membranes of ependymal cells seem to possess glycoprotein ligands for the lectin which explain the specific adhesion of CSL on the surface of these cells, particularly on the cilia. The localization of this adhesive molecule on cilia of ependymal cells suggests that it may play a role in trapping foreign cells, micro-organisms or debris.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01216703
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