Source:http://linkedlifedata.com/resource/pubmed/id/18349073
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 8
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pubmed:dateCreated |
2008-4-4
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pubmed:abstractText |
CD47 and SHPS-1 are transmembrane proteins that interact with each other through their extracellular regions and constitute a bidirectional cell-cell communication system (the CD47-SHPS-1 system). We have now shown that the trans-interaction of CD47 and SHPS-1 that occurred on contact of CD47-expressing CHO cells and SHPS-1-expressing CHO cells resulted in endocytosis of the ligand-receptor complex into either cell type. Such trans-endocytosis of CD47 by SHPS-1-expressing cells was found to be mediated by clathrin and dynamin. A juxtamembrane region of SHPS-1 was indispensable for efficient trans-endocytosis of CD47, which was also regulated by Rac and Cdc42, probably through reorganization of the actin cytoskeleton. Inhibition of trans-endocytosis of CD47 promoted the aggregation of CD47-expressing cells with the cells expressing SHPS-1. Moreover, CD47 expressed on the surface of cultured mouse hippocampal neurons was shown to undergo trans-endocytosis by neighboring astrocytes expressing endogenous SHPS-1. These results suggest that trans-endocytosis of CD47 is responsible for removal of the CD47-SHPS-1 complex from the cell surface and hence regulates the function of the CD47-SHPS-1 system, at least in neurons and glial cells.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Vesicular...,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD47,
http://linkedlifedata.com/resource/pubmed/chemical/Clathrin,
http://linkedlifedata.com/resource/pubmed/chemical/Dynamins,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ptpns1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/epsin
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9533
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
121
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1213-23
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pubmed:meshHeading |
pubmed-meshheading:18349073-Adaptor Proteins, Vesicular Transport,
pubmed-meshheading:18349073-Animals,
pubmed-meshheading:18349073-Antigens, CD47,
pubmed-meshheading:18349073-CHO Cells,
pubmed-meshheading:18349073-Clathrin,
pubmed-meshheading:18349073-Cricetinae,
pubmed-meshheading:18349073-Cricetulus,
pubmed-meshheading:18349073-Dynamins,
pubmed-meshheading:18349073-Endocytosis,
pubmed-meshheading:18349073-Fluorescent Antibody Technique,
pubmed-meshheading:18349073-GTP-Binding Proteins,
pubmed-meshheading:18349073-Mice,
pubmed-meshheading:18349073-RNA Interference,
pubmed-meshheading:18349073-Receptors, Immunologic
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pubmed:year |
2008
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pubmed:articleTitle |
Trans-endocytosis of CD47 and SHPS-1 and its role in regulation of the CD47-SHPS-1 system.
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pubmed:affiliation |
Laboratory of Biosignal Sciences, Institute for Molecular and Cellular Regulation, Gunma University, Gunma, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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