Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1999-1-22
pubmed:abstractText
The alpha1,3-fucosyltransferase, FucT-VII, is crucial for the formation of ligands for all three selectins, and its expression regulates the synthesis of these ligands. Short-term polarized T helper (Th)1, but not Th2 or naive CD4(+) T cells, can home to sites of inflammation, but the molecular basis for this difference has remained unclear. Here we show that naive CD4(+) T cells do not express FucT-VII and fail to bind vascular selectins. We also show that when CD4(+) T cells are activated in the presence of the Th1 polarizing cytokine interleukin (IL)-12, levels of FucT-VII mRNA and binding to E- and P-selectin are significantly augmented. In contrast, activation of CD4(+) T cells in the presence of IL-4, a Th2 polarizing cytokine, inhibited FucT-VII expression and binding to vascular selectins. T cell activation upregulated expression of the Core2 transferase, C2GnT, equivalently regardless of the presence or absence of polarizing cytokines. These data indicate that the selective ability of Th1 cells, as opposed to Th2 cells or naive CD4(+) T cells, to recognize vascular selectins and home to sites of inflammation is controlled principally by the expression of a single gene, FucT-VII.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9858509-1705666, http://linkedlifedata.com/resource/pubmed/commentcorrection/9858509-1760836, http://linkedlifedata.com/resource/pubmed/commentcorrection/9858509-7678617, http://linkedlifedata.com/resource/pubmed/commentcorrection/9858509-8621728, http://linkedlifedata.com/resource/pubmed/commentcorrection/9858509-8666674, http://linkedlifedata.com/resource/pubmed/commentcorrection/9858509-8752218, http://linkedlifedata.com/resource/pubmed/commentcorrection/9858509-8822932, http://linkedlifedata.com/resource/pubmed/commentcorrection/9858509-8896391, http://linkedlifedata.com/resource/pubmed/commentcorrection/9858509-8916952, http://linkedlifedata.com/resource/pubmed/commentcorrection/9858509-8985251, http://linkedlifedata.com/resource/pubmed/commentcorrection/9858509-9028320, http://linkedlifedata.com/resource/pubmed/commentcorrection/9858509-9053457, http://linkedlifedata.com/resource/pubmed/commentcorrection/9858509-9103426, http://linkedlifedata.com/resource/pubmed/commentcorrection/9858509-9257857, http://linkedlifedata.com/resource/pubmed/commentcorrection/9858509-9302298, http://linkedlifedata.com/resource/pubmed/commentcorrection/9858509-9500790, http://linkedlifedata.com/resource/pubmed/commentcorrection/9858509-9551886, http://linkedlifedata.com/resource/pubmed/commentcorrection/9858509-9670926, http://linkedlifedata.com/resource/pubmed/commentcorrection/9858509-9686572
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation..., http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Neoplasm, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins, http://linkedlifedata.com/resource/pubmed/chemical/CTAGE1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Enterotoxins, http://linkedlifedata.com/resource/pubmed/chemical/Fucosyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Glycosyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-12, http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2, http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-4, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Phytohemagglutinins, http://linkedlifedata.com/resource/pubmed/chemical/Selectins, http://linkedlifedata.com/resource/pubmed/chemical/Superantigens, http://linkedlifedata.com/resource/pubmed/chemical/enterotoxin F, Staphylococcal, http://linkedlifedata.com/resource/pubmed/chemical/galactoside 3-fucosyltransferase
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0022-1007
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
188
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2225-31
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:9858509-Antigens, CD, pubmed-meshheading:9858509-Antigens, Differentiation, T-Lymphocyte, pubmed-meshheading:9858509-Antigens, Neoplasm, pubmed-meshheading:9858509-Bacterial Toxins, pubmed-meshheading:9858509-CD4-Positive T-Lymphocytes, pubmed-meshheading:9858509-Cell Adhesion, pubmed-meshheading:9858509-Cells, Cultured, pubmed-meshheading:9858509-Endothelium, Vascular, pubmed-meshheading:9858509-Enterotoxins, pubmed-meshheading:9858509-Fucosyltransferases, pubmed-meshheading:9858509-Glycosyltransferases, pubmed-meshheading:9858509-Humans, pubmed-meshheading:9858509-Immunologic Memory, pubmed-meshheading:9858509-Interleukin-12, pubmed-meshheading:9858509-Interleukin-2, pubmed-meshheading:9858509-Interleukin-4, pubmed-meshheading:9858509-Lymphocyte Activation, pubmed-meshheading:9858509-Membrane Glycoproteins, pubmed-meshheading:9858509-Phytohemagglutinins, pubmed-meshheading:9858509-Selectins, pubmed-meshheading:9858509-Superantigens, pubmed-meshheading:9858509-Th1 Cells, pubmed-meshheading:9858509-Th2 Cells
pubmed:year
1998
pubmed:articleTitle
Interleukin 12 and interleukin 4 control T cell adhesion to endothelial selectins through opposite effects on alpha1, 3-fucosyltransferase VII gene expression.
pubmed:affiliation
Department of Microbiology-Immunology, Northwestern Medical School, Chicago, Illinois 60611, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't