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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1990-8-29
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pubmed:abstractText |
Madin-Darby canine kidney cells (MDCK) were transfected with a cDNA encoding the glycosyl-phosphatidylinositol (GPI)-anchored protein mouse Thy-1 in order to study the steady-state surface distribution of exogenous and endogenous GPI-linked proteins. Immunofluorescence of transfected cells grown on collagen-coated coverslips showed that expression of Thy-1 was variable throughout the epithelium, with some cells expressing large amounts of Thy-1 adjacent to very faintly staining cells. Selective surface iodination of cells grown on collagen-coated or uncoated transwell filters followed by immunoprecipitation of Thy-1 demonstrated that all the Thy-1 was present exclusively in the apical plasma membrane. Although cells grown on uncoated filters had much smaller amounts of Thy-1, it was consistently localized on the apical surfaces. Immunofluorescent localization of Thy-1 on 1 micron frozen sections of filter-grown cells demonstrated that all the Thy-1 was on the apical surface and there was no detectable intracellular pool. Phosphatidylinositol-specific phospholipase C digestion of intact iodinated monolayers released Thy-1 only into the apical medium, indicating that Thy-1 was processed normally in transfected cells and was anchored by a GPI-tail. In agreement with previous findings, endogenous GPI-linked proteins were found only on the apical plasma membrane. These results suggest that there is a common mechanism for sorting and targeting of GPI-linked proteins in polarized epithelial cells.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Thy-1,
http://linkedlifedata.com/resource/pubmed/chemical/Glycolipids,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosylphosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Iodine Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol...,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoinositide Phospholipase C,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Diester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9533
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
96 ( Pt 1)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
143-9
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:1973690-Animals,
pubmed-meshheading:1973690-Antigens, Surface,
pubmed-meshheading:1973690-Antigens, Thy-1,
pubmed-meshheading:1973690-Cell Line,
pubmed-meshheading:1973690-Dogs,
pubmed-meshheading:1973690-Epithelial Cells,
pubmed-meshheading:1973690-Epithelium,
pubmed-meshheading:1973690-Glycolipids,
pubmed-meshheading:1973690-Glycosylphosphatidylinositols,
pubmed-meshheading:1973690-Iodine Radioisotopes,
pubmed-meshheading:1973690-Kidney,
pubmed-meshheading:1973690-Membrane Proteins,
pubmed-meshheading:1973690-Phosphatidylinositol Diacylglycerol-Lyase,
pubmed-meshheading:1973690-Phosphatidylinositols,
pubmed-meshheading:1973690-Phosphoinositide Phospholipase C,
pubmed-meshheading:1973690-Phosphoric Diester Hydrolases,
pubmed-meshheading:1973690-Protein Processing, Post-Translational,
pubmed-meshheading:1973690-Recombinant Proteins,
pubmed-meshheading:1973690-Transfection
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pubmed:year |
1990
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pubmed:articleTitle |
Polarity of endogenous and exogenous glycosyl-phosphatidylinositol-anchored membrane proteins in Madin-Darby canine kidney cells.
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pubmed:affiliation |
Department of Anatomy and Cellular Biology, Harvard Medical School, Boston, MA 02115.
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pubmed:publicationType |
Journal Article
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