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  • 1
    Electronic Resource
    Electronic Resource
    Cell biology Caught in the traffic (2007)
    [s.l.] : Nature Publishing Group
    Nature 448 (2007), S. 266-267 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The gut, like other tubular structures in the body, is lined with a monolayer of epithelial cells, which forms the main interface between the external and internal environments of an organism. A defining characteristic of these cells is their polarity — that is, their apical and basolateral ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/448266a
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  • 2
    Electronic Resource
    Electronic Resource
    Intracellular Sorting of Plasma Membrane Glycoproteins in Epithelial Cells (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 435 (1984), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1984.tb13813.x
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  • 3
    Electronic Resource
    Electronic Resource
    Targeting of transmembrane and GPI-anchored forms of N-CAM to opposite domains of a polarized epithelial cell (1991)
    [s.l.] : Nature Publishing Group
    Nature 353 (1991), S. 76-77 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] After transfection of the cDNAs for chicken ssd, sd and Id N-CAM into the canine kidney epithelial cell line MDCK we determined the localization of the isoforms by indirect immuno-fluorescence. The ssd N-CAM is expressed apically (Fig. la, 6, g, /i), and both sd (Fig. Ic, d) and Id (Fig. le, f) ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/353076a0
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  • 4
    Electronic Resource
    Electronic Resource
    Integral and peripheral protein composition of the apical and basolateral membrane domains in MDCK cells (1989)
    Springer
    The journal of membrane biology 107 (1989), S. 277-286 
    Details
    ISSN: 1432-1424
    Keywords: epithelial cells ; cell polarity ; plasma membrane proteins ; sulfo-NHS-biotin ; streptavidin ; Triton X-114
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Selective biotinylation of the apical or basolateral domains of confluent MDCK monolayers grown on polycarbonate filters with a water soluble biotin analog, sulfo-NHS-biotin, was employed to reveal strikingly distinct patterns of endogenous “peripheral” and “integral” membrane proteins. “Peripheral” proteins were found to be approximately fivefold more abundant with this procedure than “integral” membrane proteins, both on the apical and on the basolateral surface. The distinct apical and basal patterns were shown to depend upon the integrity of the monolayer; when the tight junctions were disrupted by preincubation in calcium-depleted medium, the patterns appeared practically indistinguishable. Two-dimensional gel electrophoresis demonstrated that only a very small percentage of the biotinylated proteins were found in similar amounts on both apical and basolateral domains. These results indicate that the sorting mechanisms that segregate apical and basolateral epithelial proteins are very strict. The simple procedure described here has clear advantages over other methods available to label apical and basal epithelial surface domains, namely, higher accessibility of the biotin probe to the basolateral membrane, possibility of purifying biotinylated proteins via immobilized streptavidin and minimal exposure of the researcher to isotopes. It should be very useful in characterizing the apical and basolateral protein compositions of other epithelial cells and in studies on the development of epithelial cell polarity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01871942
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  • 5
    Electronic Resource
    Electronic Resource
    Emerging functional roles for the glycosyl-phosphatidylinositol membrane protein anchor (1990)
    Springer
    The journal of membrane biology 117 (1990), S. 1-10 
    Details
    ISSN: 1432-1424
    Keywords: phospholipase ; cell surface polarity ; lateral mobility ; hormone action
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Conclusion Experimental evidence has accumulated over the past few years to suggest that the GPI protein anchor may play a broad role in the regulation of membrane protein function. The significant changes in the biophysical properties of proteins that are membrane-anchored through GPI in lieu of a hydrophobic transmembrane peptide indicates a variety phobic transmembrane peptide indicates a variety of potential new functions served by the anchor structure itself. Moreover, the number of structural variations within the family of GPI molecules indicates a further opportunity for subspecialization of such anchored proteins, especially regarding cellular localization, mobility, metabolism and susceptibility to enzymatically-induced release. It is likely that further exploration of the structure and function of the GPI anchor may reveal additional roles for this unusual mechanism of membrane-protein attachment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01871561
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  • 6
    Electronic Resource
    Electronic Resource
    Collagen receptors mediate early events in the attachment of epithelial (MDCK) cells (1987)
    Springer
    The journal of membrane biology 98 (1987), S. 223-236 
    Details
    ISSN: 1432-1424
    Keywords: epithelia ; MDCK cells ; cell-substrate interaction ; collagen receptor ; epithelial polarity ; laminin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Madin-Darby canine kidney (MDCK) cells kept in suspension culture for 12–15 hr displayed high-affinity binding sites for125I-lathyritic (soluble) collagen (120,000/cell,K D =30nm) and preferred collagens types I and IV over laminin or fibronectin as substrates during the first hour of attachment. On the other hand, after 4 hr, attachment to all four substrates was equally efficient. Upon challenge with a collagen substrate, the high-affinity sites were rapidly recruited on it (T1/2=6 min). Their occupancy by soluble collagen triggered the exocytosis of a second large population of low-affinity collagen binding sites that included laminin and seems to be involved in a second cell-attachment mechanism. These results are compatible with a twostep model of MDCK cell attachment to the substrate: first, via high-affinity collagen binding sites, and second, via laminin of cellular origin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01871185
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  • 7
    Electronic Resource
    Electronic Resource
    Preferred apical distribution of glycosyl-phosphatidylinositol (GPI) anchored proteins: A highly conserved feature of the polarized epithelial cell phenotype (1990)
    Springer
    The journal of membrane biology 113 (1990), S. 155-167 
    Details
    ISSN: 1432-1424
    Keywords: protein targeting ; biotin labeling ; epithelial polarity ; glycolipids ; glycosyl-phosphatidylinositol
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary We use a sensitive biotin polarity assay to survey the surface distribution of glycosyl-phosphatidylinositol (GPI) anchored proteins in five model epithelial cell lines derived from different species (dog, pig, man) and tissues, i.e., kidney (MDCK I, MDCK II, LLC-PK1) and intestine (Caco-2 and SK-CO15). After biotinylation of apical or basolateral surfaces of confluent monolayers grown on polycarbonate filters, GPI-anchored proteins are identified by their shift from a Triton X-114 detergent-rich phase to a detergent-poor phase in the presence of phosphatidylinositol-specific phospholipase C. All GPI-anchored proteins detected (3–9 per cell type, at least 13 different proteins) are found to be apically polarized; no GPI-anchored protein is observed preferentially localized to the basal surface. One of the GPI-anchored proteins is identified as carcinoembryonic antigen (CEA). Survey of MDCK II-RCA r , a mutant cell line with a pleiotropic defect in galactosylation of glycoproteins and glycolipids (that presumably affects GPI anchors) also reveals an apical polarization of all GPI-anchored proteins. In contrast, analysis of MDCK II-ConA′ (a mutant cell line with an unknown defect in glycosylation) revealed five GPI-anchored proteins, two of which appeared relatively unpolarized. Our results indicate that the polarized apical distribution of GPI-anchored proteins is highly conserved across species and tissue-type and may depend on glycosylation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01872889
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  • 8
    Electronic Resource
    Electronic Resource
    Characterization of the ribosomal binding site in rat liver rough microsomes: Ribophorins I and II, two integral membrane proteins related to ribosome binding (1978)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 8 (1978), S. 279-302 
    Details
    ISSN: 0091-7419
    Keywords: rat liver endoplasmic reticulum ; rough microsomes ; membrane-bound polysomes ; ribosome-binding sites ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Rat liver rough endoplasmic reticulum membranes (ER) contain two characteristic transmembrane glycoproteins which have been designated ribophorins I and II and are absent from smooth ER membranes. These proteins (MW 65,000 and 63,000 respectively) are related to the binding sites for ribosomes, as suggested by the following findings: (i) The ribophorin content of the rough ER membranes corresponds stoichiometrically to the number of bound ribosomes; (ii) ribophorins are quantitatively recovered with the bound polysomes after most other ER membrane proteins are dissolved with the nonionic detegent Kyro EOB; (iii) in intact rough microsomes ribophorins can be crosslinked chemically to the ribosomes and therefore are in close proximity to them.Treatment of rough microsomes with a low Triton X-100 concentration leads to the lateral displacement of ribosomes on the microsomal surface and to the formation of aggregates of bound ribosomes in areas of membranes which frequently invaginate into the microsomal lumen. Subfractionation of Triton-treated microsomes containing invaginations led to the recovery of smooth and “rough-inverted” vesicles. Ribophorins were present only in the latter fraction, indicating that both proteins are displaced together with the ribosome-binding capacity of rough and smooth microsomal membranes reconstituted after solubilization with detergents sugest that ribophorins are necessary for in vitro ribosome binding. Ribophorin-like proteins were found in rough microsomes obtained from secretory tissues of several animal species. The two proteins present in rat lacrimal gland microsomes have the same mobility as hepatocyte ribophorins and cross-react with antisera against them.
    Additional Material: 18 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400080307
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