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  • 1
    Electronic Resource
    Electronic Resource
    Expression and Localization of Myelin Basic Protein in Oligodendrocytes and Transfected Fibroblasts (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 51 (1988), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Myelin basic protein (MBP) is a major structural component of myelin. It is expressed exclusively in myelinating glia (oligodendrocytes in the CNS and Schwann cells in the PNS) and is localized to the cytoplasmic surface of the plasma membrane and myelin membrane produced by these cells. The work described here concerns the mechanism of plasma membrane localization of MBP in myelinating glial cells and whether it involves differentiated functions specific to these cells or general functions of plasma membrane assembly common to all cells. To this end, the subcellular localization of endogenous MBP in mouse oligodendrocytes was compared with that of transiently expressed MBP in monkey fibroblasts (Cos-1 cells) transfected with an MBP expression vector containing cDNA for rat 14K MBP. The steady-state levels of MBP-specific RNA and of MBP poly-peptide expressed in the transfected fibroblasts were comparable to the levels expressed in oligodendrocytes in primary culture. MBP localization was analyzed in whole cells by immunofluorescence and in specific intracellular compartments by subcellular fractionation. The results show that MBP expressed in wild-type oligodendrocytes is localized to the plasma membrane. In contrast, MBP expressed in transfected fibroblasts appears dispersed in the cytoplasm and is distributed uniformly among the various subcellular fractions. Purified MBP added prior to subcellular fractionation to ho-mozygous shiverer oligodendrocytes (which express no MBP endogenously) is recovered predominantly in the plasma membrane fraction, whereas purified MBP added to mock-transfected fibroblasts exhibits a dispersed distribution among subcellular fractions. On the basis of these results, we propose a model whereby localization of MBP to the plasma membrane in oligodendrocytes involves interaction between the newly synthesized MBP polypeptide and specific MBP receptors which are present in oligodendrocyte plasma membrane, but not in fibroblast plasma membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1988.tb01153.x
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  • 2
    Electronic Resource
    Electronic Resource
    Human placental alkaline phosphatase differs from that of other species (1979)
    [s.l.] : Nature Publishing Group
    Nature 280 (1979), S. 602-605 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Table 1 Concentrations of various inhibitors required to produce 50% inhibition of alkaline phosphatase in placenta and liver of various mammals [I]50 (mM) HA Phe PGG Man Placenta 62.88 1.13 0.09 Liver 2.83 28.62 27.44 Dog Placenta 2.87 28.42 32.52 Liver 2.91 22.42 27.44 ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/280602a0
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  • 3
    Electronic Resource
    Electronic Resource
    Bovine papillomavirus E5 oncoprotein binds to the 16K component of vacuolar H + -ATPases (1991)
    [s.l.] : Nature Publishing Group
    Nature 352 (1991), S. 347-349 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Considerations of size, hydrophobicity, cell localization and lack of cysteine residues suggested that the 16K component of the F0-like proton channel of vacuolar H+-ATPases might be the E5-associated 16K protein. To evaluate this possibility, rabbit antiserum generated against the chicken-liver ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/352347a0
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  • 4
    Electronic Resource
    Electronic Resource
    Genetic variability of alkaline phosphatase expression in inbred mouse tissues (1985)
    Springer
    Biochemical genetics 23 (1985), S. 155-167 
    Details
    ISSN: 1573-4927
    Keywords: alkaline phosphatase ; gene expression ; inbred strains ; quantitative variation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Quantitative alkaline phosphatase (ALP; EC 3.1.3.1) expression varies among various tissues and among inbred mouse strains. There is about a 20-fold difference in ALP activity in lungs from CBA/J and C57L/J inbred strains and this difference is inherited additively with a heritability of 0.84. Studies of thermostability at 56 and 65° C and sensitivity toward inhibitors (l-phenylalanine, l-homoarginine, l-phenylalanylglycylglycine, and levamisole) do not demonstrate differences in the ALP from lungs or liver of the CBA/J and C57L/J strains. The ALP activity in intestine expressed by the intestinal locus varies over 100-fold between A/J and DBA/1J strains. Further studies of the mechanisms resulting in this difference in ALP activity should help elucidate the mechanisms for aberrant expression of ALP in malignancy and for manipulation of low ALP activity in hypophosphatasia.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00499120
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  • 5
    Electronic Resource
    Electronic Resource
    A genomic sequence of the Schizosaccharomyces pombe 16 kDa vacuolar H+-ATPase (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 7 (1991), S. 989-991 
    Details
    ISSN: 0749-503X
    Keywords: Sequence ; S. pombe ; vacuolar H+-ATPase ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have isolated the gene encoding the 16 kDa vacuolar H+-ATPase from Schizosaccharomyces pombe. On the basis of RNA splicing signals and amino acid sequence homology with other 16 kDa H+-ATPases, the genomic DNA sequence indicated the 16 kDa protein is encoded by five exons. The C-terminal 50 amino acids has more than 90% homology with vacuolar H+-ATPases of mammalian cells.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320070911
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