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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2000-4-26
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pubmed:databankReference |
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pubmed:abstractText |
T lymphocyte activation evokes distinct changes in cell surface O-glycans. CD8+ T cells undergo an elimination of sialic acid on core 1 O-glycans and an induction of core 2 O-glycans until either apoptotic death or differentiation into memory cells. We find that the ST3Gal-I sialyltransferase is required for core 1 O-glycan sialylation and its deficiency induces core 2 O-glycan biosynthesis. Apoptosis ensues with the loss of peripheral CD8+ T cells in the absence of immune stimulation. Cell surface ligation of the ST3Gal-I substrate CD43 recapitulates this phenotype by a caspase 3-independent mechanism. Control of core 1 O-glycan sialylation in T lymphocytes by ST3Gal-I comprises a homeostatic mechanism that eliminates CD8+ T cells by apoptosis while facilitating the production of viable CD8+ memory T cells.
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pubmed:grant |
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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, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD43,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Sialoglycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sialyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Spn protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/beta-galactoside...
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1074-7613
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
273-83
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10755614-Animals,
pubmed-meshheading:10755614-Antigens, CD,
pubmed-meshheading:10755614-Antigens, CD43,
pubmed-meshheading:10755614-Apoptosis,
pubmed-meshheading:10755614-Base Sequence,
pubmed-meshheading:10755614-CD8-Positive T-Lymphocytes,
pubmed-meshheading:10755614-Caspase 1,
pubmed-meshheading:10755614-Cytotoxicity, Immunologic,
pubmed-meshheading:10755614-Enzyme Activation,
pubmed-meshheading:10755614-Gene Expression Regulation,
pubmed-meshheading:10755614-Glycoproteins,
pubmed-meshheading:10755614-Homeostasis,
pubmed-meshheading:10755614-Lymphocyte Activation,
pubmed-meshheading:10755614-Mice,
pubmed-meshheading:10755614-Molecular Sequence Data,
pubmed-meshheading:10755614-Mutagenesis,
pubmed-meshheading:10755614-Polysaccharides,
pubmed-meshheading:10755614-Sialoglycoproteins,
pubmed-meshheading:10755614-Sialyltransferases,
pubmed-meshheading:10755614-Substrate Specificity
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pubmed:year |
2000
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pubmed:articleTitle |
The ST3Gal-I sialyltransferase controls CD8+ T lymphocyte homeostasis by modulating O-glycan biosynthesis.
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pubmed:affiliation |
Howard Hughes Medical Institute, the Glycobiology Research and Training Center, and Department of Cellular and Molecular Medicine, University of California, San Diego, La Jolla 92093, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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