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  • Articles: DFG German National Licenses  (2)
  • A antigenicity  (1)
  • Thyroid cell  (1)
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  • Articles: DFG German National Licenses  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Biosynthesis and intracellular pool of aminopeptidase N in rabbit enterocytes (1985)
    Springer
    The journal of membrane biology 83 (1985), S. 139-146 
    Details
    ISSN: 1432-1424
    Keywords: intestine ; aminopeptidase N ; biosynthesis ; glycoproteins ; A antigenicity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary A papain treatment at 15°C and pH 7.3 of a microsomal fraction from rabbit enterocytes quantitatively releases the aminopeptidase N integrated in the plasma membranes without solubilizing the enzyme integrated in the intracellular membranes. Working on A+ rabbits, characterized by the presence on the brush-border hydrolases of glycans corresponding to the human blood group A-determinant structure, it was possible to separate the intracellular aminopeptidase into two major molecular forms with or without these determinants. The molecular form devoid of human blood group A antigenicity corresponds to the only stable intermediate of glycosylation, bearing N-linked high mannose oligosaccharides. This endoglycosidase H-sensitive form is fully active and represents in the steady state about 1% of the total cellular aminopeptidase. It contains a cytoplasmic sequence of about 3000 daltons that has not yet been detected in the mature form. The A antigenicity is acquired simultaneously with processing of high mannose glycans to complex glycans. Pulse chase labeling of jejunum loops with [35S]-methionine showed that the complete processing of the transient form synthesized during 10 min takes 1 hr. During the last 30 min of processing, all the newly transformed molecules are transported to the plasma membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01868745
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Aminopeptidase N is a marker for the apical pole of porcine thyroid epithelial cells in vivo and in culture (1981)
    Springer
    Cell & tissue research 221 (1981), S. 137-146 
    Details
    ISSN: 1432-0878
    Keywords: Aminopeptidase ; Thyroid ; Thyroid cell ; Membrane marker ; Polarization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary An aminopeptidase N has been detected by immunofluorescence in the apical plasma membrane of porcine thyroid cells, facing the follicular lumen. Freshly isolated cells obtained by tissue trypsinization, lose their polarity and exhibit a homogeneous enzyme distribution over the whole plasma membrane. In thyrotropin-stimulated cultured cells organized into follicles, the enzyme is localized in the apical cell pole. In monolayer cells, on the other hand, the enzyme is distributed over the whole surface facing the medium. In both types of cultures fluorescence is also observed in intracytoplasmic organelles. In vivo, aminopeptidase is a marker of the apical part of the thyroid plasma membrane, but its in vitro localization depends upon cell differentiation related to the culture conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00216576
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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