rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
3
|
pubmed:dateCreated |
1983-10-21
|
pubmed:abstractText |
The envelope of vesicular stomatitis virus was fused with the apical plasma membrane of Madin-Darby canine kidney cells by low pH treatment. The fate of the implanted G protein was then followed using a protein A-binding assay, which was designed to quantitate the amount of G protein in the apical and the basolateral membranes. The implanted G protein was rapidly internalized at 31 degrees C, whereas at 10 degrees C no uptake was observed. Already after 15 min at 31 degrees C, a fraction of the G protein could be detected at the basolateral membrane. After 60 min 25-48% of the G protein was basolateral as measured by the protein A-binding assay. At the same time, 25-33% of the implanted G protein was detected at the apical membrane. Internalization of G protein was not affected by 20 mM ammonium chloride or by 10 microM monensin. However, the endocytosed G protein accumulated in intracellular vacuoles and redistribution back to the plasma membrane was inhibited. We conclude that the implanted G protein was rapidly internalized from the apical surface of Madin-Darby canine kidney cells and a major fraction was routed to the basolateral domain.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-1063404,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-28524,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-4342242,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-488350,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-567227,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-6156003,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-6176331,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-6183281,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-6245216,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-6248236,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-6251452,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-6257729,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-6263497,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-6265470,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-6277962,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-6288961,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-6292894,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-6298247,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-6329709,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-6765172,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-6780571,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-6831562,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-6885914,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-6928656,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-6933462,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-7190150,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-7298722,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-7328111,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-7419594,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-7463480,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6411736-786156
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pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
0021-9525
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
97
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
638-43
|
pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:6411736-Aminopeptidases,
pubmed-meshheading:6411736-Animals,
pubmed-meshheading:6411736-Cell Compartmentation,
pubmed-meshheading:6411736-Cell Membrane,
pubmed-meshheading:6411736-Cells, Cultured,
pubmed-meshheading:6411736-Dogs,
pubmed-meshheading:6411736-Egtazic Acid,
pubmed-meshheading:6411736-Endocytosis,
pubmed-meshheading:6411736-Epithelium,
pubmed-meshheading:6411736-Glycoproteins,
pubmed-meshheading:6411736-Hydrogen-Ion Concentration,
pubmed-meshheading:6411736-Kidney,
pubmed-meshheading:6411736-Membrane Glycoproteins,
pubmed-meshheading:6411736-Membrane Proteins,
pubmed-meshheading:6411736-Staphylococcal Protein A,
pubmed-meshheading:6411736-Viral Envelope Proteins,
pubmed-meshheading:6411736-Viral Proteins
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pubmed:year |
1983
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pubmed:articleTitle |
Transepithelial transport of a viral membrane glycoprotein implanted into the apical plasma membrane of Madin-Darby canine kidney cells. II. Immunological quantitation.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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