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rdf:type |
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lifeskim:mentions |
umls-concept:C0004083,
umls-concept:C0007634,
umls-concept:C0017262,
umls-concept:C0024518,
umls-concept:C0039194,
umls-concept:C0054543,
umls-concept:C0086418,
umls-concept:C0229664,
umls-concept:C0456387,
umls-concept:C0567416,
umls-concept:C0699040,
umls-concept:C1171362,
umls-concept:C1515670,
umls-concept:C1879547
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pubmed:issue |
24
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pubmed:dateCreated |
1999-7-6
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pubmed:abstractText |
Calreticulin is an endoplasmic reticulum resident molecule known to be involved in the folding and assembly of major histocompatibility complex (MHC) class I molecules. In the present study, expression of calreticulin was analyzed in human peripheral blood T lymphocytes. Pulse-chase experiments in [35S]methionine-labeled T cell blasts showed that calreticulin was associated with several proteins in the endoplasmic reticulum and suggested that it was expressed at the cell surface. Indeed, the 60-kDa calreticulin was labeled by cell surface biotinylation and precipitated from the surface of activated T cells together with a protein with an apparent molecular mass of 46 kDa. Cell surface expression of calreticulin by activated T lymphocytes was further confirmed by immunofluorescence and flow cytometry, studies that showed that both CD8+ and CD4+ T cells expressed calreticulin in the plasma membrane. Low amounts of cell surface calreticulin were detected in resting T lymphocytes. By sequential immunoprecipitation using the conformation independent monoclonal antibody HC-10, we provided evidence that the cell surface 46-kDa protein co-precipitated with calreticulin is unfolded MHC I. These results show for the first time that after T cell activation, significant amounts of calreticulin are expressed on the T cell surface, where they are found in physical association with a pool of beta2-free MHC class I molecules.
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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, CD44,
http://linkedlifedata.com/resource/pubmed/chemical/C1QBP protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calreticulin,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class I,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Complement,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/complement 1q receptor
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
16917-22
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10358038-Antibody Specificity,
pubmed-meshheading:10358038-Antigens, CD44,
pubmed-meshheading:10358038-Calcium-Binding Proteins,
pubmed-meshheading:10358038-Calreticulin,
pubmed-meshheading:10358038-Carrier Proteins,
pubmed-meshheading:10358038-Cell Membrane,
pubmed-meshheading:10358038-Histocompatibility Antigens Class I,
pubmed-meshheading:10358038-Humans,
pubmed-meshheading:10358038-Lymphocyte Activation,
pubmed-meshheading:10358038-Membrane Glycoproteins,
pubmed-meshheading:10358038-Membrane Proteins,
pubmed-meshheading:10358038-Mitochondrial Proteins,
pubmed-meshheading:10358038-Molecular Chaperones,
pubmed-meshheading:10358038-Precipitin Tests,
pubmed-meshheading:10358038-Protein Binding,
pubmed-meshheading:10358038-Receptors, Complement,
pubmed-meshheading:10358038-Ribonucleoproteins,
pubmed-meshheading:10358038-T-Lymphocytes
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pubmed:year |
1999
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pubmed:articleTitle |
Calreticulin is expressed on the cell surface of activated human peripheral blood T lymphocytes in association with major histocompatibility complex class I molecules.
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pubmed:affiliation |
Laboratory of Molecular Immunology, Institute for Molecular and Cell Biology, University of Porto, 4150 Porto, Portugal. farosa@ibmc.up.pt
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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