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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
25
|
| pubmed:dateCreated |
1993-7-23
|
| pubmed:abstractText |
In simple epithelial cells, the delivery of apical and basolateral proteins to the cell surface is mediated by sorting in the trans-Golgi network and transport via separate vesicular carriers. In order to identify the molecular machinery involved in protein sorting, we have recently studied a detergent-insoluble complex in Madin-Darby canine kidney (MDCK) cells, following CHAPS extraction of exocytic carrier vesicles, specifically including the apical marker protein influenza hemagglutinin (HA). Previously, a Triton X-100 insoluble membrane residue that was enriched in glycosylphosphatidylinositol-anchored (GPI) proteins and glycolipids was characterized and implicated in transport to the apical cell surface [Brown, D., & Rose, J. (1991) Cell 68, 533-544]. In this report, the protein compositions of the CHAPS and Triton complexes have been compared by two-dimensional gel analysis. Only a few major membrane proteins are found in the complexes. The protein compositions are qualitatively similar, but differ quantitatively in the individual components. The CHAPS complex is depleted of GPI-linked proteins and retains a minor fraction of lipids similar in composition to that of the Triton X-100 insoluble complex. We propose that in vivo the complexes form part of a sorting platform that mediates protein segregation and delivery to the apical cell surface.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/3-((3-cholamidopropyl)dimethylammoni...,
http://linkedlifedata.com/resource/pubmed/chemical/Cholic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Detergents,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosylphosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Methionine,
http://linkedlifedata.com/resource/pubmed/chemical/Nonidet P-40,
http://linkedlifedata.com/resource/pubmed/chemical/Polyethylene Glycols,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfur Radioisotopes
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0006-2960
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
29
|
| pubmed:volume |
32
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
6365-73
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8518282-Animals,
pubmed-meshheading:8518282-Cell Line,
pubmed-meshheading:8518282-Cell Membrane,
pubmed-meshheading:8518282-Cholic Acids,
pubmed-meshheading:8518282-Detergents,
pubmed-meshheading:8518282-Dogs,
pubmed-meshheading:8518282-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:8518282-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:8518282-Epithelium,
pubmed-meshheading:8518282-Glycosylphosphatidylinositols,
pubmed-meshheading:8518282-Golgi Apparatus,
pubmed-meshheading:8518282-Kidney,
pubmed-meshheading:8518282-Methionine,
pubmed-meshheading:8518282-Organelles,
pubmed-meshheading:8518282-Polyethylene Glycols,
pubmed-meshheading:8518282-Protein Biosynthesis,
pubmed-meshheading:8518282-Protein Processing, Post-Translational,
pubmed-meshheading:8518282-Proteins,
pubmed-meshheading:8518282-Sulfur Radioisotopes
|
| pubmed:year |
1993
|
| pubmed:articleTitle |
Glycosphingolipid-enriched, detergent-insoluble complexes in protein sorting in epithelial cells.
|
| pubmed:affiliation |
Cell Biology Programme, European Molecular Biology Laboratory, Heidelberg, Germany.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|