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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2003-4-11
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pubmed:abstractText |
Engulfment of apoptotic cells requires presentation of new cell surface ligands by the dying cells. Using a differential proteomics technology, we identify that annexin I is a caspase-dependent engulfment ligand; it is recruited from the cytosol and exported to the outer plasma membrane leaflet, colocalizes with phosphatidylserine, and is required for efficient clearance of apoptotic cells. Furthermore, phosphatidylserine receptor (PSR) clustering around apoptotic cells indicates a requirement for annexin I. In the nematode Caenorhabditis elegans, downregulation of the annexin homolog prevents efficient engulfment of pharyngeal cell corpses. These results provide novel mechanistic insights into how apoptotic cells are removed and may explain a pathogenic mechanism of chronic inflammatory diseases where annexin I autoantibodies have been described.
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pubmed:grant |
http://linkedlifedata.com/resource/pubmed/grant/P01 HL070694-010004,
http://linkedlifedata.com/resource/pubmed/grant/P01 HL070694-019003,
http://linkedlifedata.com/resource/pubmed/grant/P01 HL070694-036744,
http://linkedlifedata.com/resource/pubmed/grant/P01 HL70694,
http://linkedlifedata.com/resource/pubmed/grant/P20 GM065764-010003,
http://linkedlifedata.com/resource/pubmed/grant/R01 HL 67569,
http://linkedlifedata.com/resource/pubmed/grant/R01 HL067569-01,
http://linkedlifedata.com/resource/pubmed/grant/R01 HL067569-02,
http://linkedlifedata.com/resource/pubmed/grant/R01 HL067569-03,
http://linkedlifedata.com/resource/pubmed/grant/R01 HL067569-04,
http://linkedlifedata.com/resource/pubmed/grant/RR13186
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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/Annexin A1,
http://linkedlifedata.com/resource/pubmed/chemical/Annexins,
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Helminth Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/JMJD6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Jumonji Domain-Containing Histone...,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nex-1 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/phosphatidylserine receptor
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1534-5807
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
587-98
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12689596-Animals,
pubmed-meshheading:12689596-Annexin A1,
pubmed-meshheading:12689596-Annexins,
pubmed-meshheading:12689596-Apoptosis,
pubmed-meshheading:12689596-Caenorhabditis elegans,
pubmed-meshheading:12689596-Caenorhabditis elegans Proteins,
pubmed-meshheading:12689596-Calcium Signaling,
pubmed-meshheading:12689596-Caspases,
pubmed-meshheading:12689596-Cell Membrane,
pubmed-meshheading:12689596-Cell Membrane Structures,
pubmed-meshheading:12689596-Down-Regulation,
pubmed-meshheading:12689596-Eukaryotic Cells,
pubmed-meshheading:12689596-Helminth Proteins,
pubmed-meshheading:12689596-Humans,
pubmed-meshheading:12689596-Jumonji Domain-Containing Histone Demethylases,
pubmed-meshheading:12689596-Jurkat Cells,
pubmed-meshheading:12689596-Ligands,
pubmed-meshheading:12689596-Membrane Proteins,
pubmed-meshheading:12689596-Peptide Fragments,
pubmed-meshheading:12689596-Phagocytosis,
pubmed-meshheading:12689596-Protein Transport,
pubmed-meshheading:12689596-Receptors, Cell Surface,
pubmed-meshheading:12689596-Signal Transduction,
pubmed-meshheading:12689596-Up-Regulation
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pubmed:year |
2003
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pubmed:articleTitle |
Annexin I is an endogenous ligand that mediates apoptotic cell engulfment.
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pubmed:affiliation |
Center for Vascular Biology, Department of Physiology, University of Connecticut School of Medicine, 263 Farmington Avenue, Farmington, CT 06030, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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